IntechOpen was founded by scientists, for scientists, in order to make book publishing accessible around the globe. Over the last two decades, this has driven Open Access (OA) book publishing whilst levelling the playing field for global academics. Through our innovative publishing model and the support of the research community, we have now published over 5,700 Open Access books and are visited online by over three million academics every month. These researchers are increasingly working in broad technology-based subjects, driving multidisciplinary academic endeavours into human health, environment, and technology.
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By listening to our community, and in order to serve these rapidly growing areas which lie at the core of IntechOpen's expertise, we are launching a portfolio of Open Science journals:
All three journals will publish under an Open Access model and embrace Open Science policies to help support the changing needs of academics in these fast-moving research areas. There will be direct links to preprint servers and data repositories, allowing full reproducibility and rapid dissemination of published papers to help accelerate the pace of research. Each journal has renowned Editors in Chief who will work alongside a global Editorial Board, delivering robust single-blind peer review. Supported by our internal editorial teams, this will ensure our authors will receive a quick, user-friendly, and personalised publishing experience.
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"By launching our journals portfolio we are introducing new, dedicated homes for interdisciplinary technology-focused researchers to publish their work, whilst embracing Open Science and creating a unique global home for academics to disseminate their work. We are taking a leap toward Open Science continuing and expanding our fundamental commitment to openly sharing scientific research across the world, making it available for the benefit of all." Dr. Sara Uhac, IntechOpen CEO
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"Our aim is to promote and create better science for a better world by increasing access to information and the latest scientific developments to all scientists, innovators, entrepreneurs and students and give them the opportunity to learn, observe and contribute to knowledge creation. Open Science promotes a swifter path from research to innovation to produce new products and services." Alex Lazinica, IntechOpen founder
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In conclusion, Natalia Reinic Babic, Head of Journal Publishing and Open Science at IntechOpen adds:
\\n\\n
“On behalf of the journal team I’d like to thank all our Editors in Chief, Editorial Boards, internal supporting teams, and our scientific community for their continuous support in making this portfolio a reality - we couldn’t have done it without you! With your support in place, we are confident these journals will become as impactful and successful as our book publishing program and bring us closer to a more open (science) future.”
\\n\\n
We invite you to visit the journals homepage and learn more about the journal’s Editorial Boards, scope and vision as all three journals are now open for submissions.
\\n\\n
Feel free to share this news on social media and help us mark this memorable moment!
After years of being acknowledged as the world's leading publisher of Open Access books, today, we are proud to announce we’ve successfully launched a portfolio of Open Science journals covering rapidly expanding areas of interdisciplinary research.
\n\n\n\n
IntechOpen was founded by scientists, for scientists, in order to make book publishing accessible around the globe. Over the last two decades, this has driven Open Access (OA) book publishing whilst levelling the playing field for global academics. Through our innovative publishing model and the support of the research community, we have now published over 5,700 Open Access books and are visited online by over three million academics every month. These researchers are increasingly working in broad technology-based subjects, driving multidisciplinary academic endeavours into human health, environment, and technology.
\n\n
By listening to our community, and in order to serve these rapidly growing areas which lie at the core of IntechOpen's expertise, we are launching a portfolio of Open Science journals:
All three journals will publish under an Open Access model and embrace Open Science policies to help support the changing needs of academics in these fast-moving research areas. There will be direct links to preprint servers and data repositories, allowing full reproducibility and rapid dissemination of published papers to help accelerate the pace of research. Each journal has renowned Editors in Chief who will work alongside a global Editorial Board, delivering robust single-blind peer review. Supported by our internal editorial teams, this will ensure our authors will receive a quick, user-friendly, and personalised publishing experience.
\n\n
"By launching our journals portfolio we are introducing new, dedicated homes for interdisciplinary technology-focused researchers to publish their work, whilst embracing Open Science and creating a unique global home for academics to disseminate their work. We are taking a leap toward Open Science continuing and expanding our fundamental commitment to openly sharing scientific research across the world, making it available for the benefit of all." Dr. Sara Uhac, IntechOpen CEO
\n\n
"Our aim is to promote and create better science for a better world by increasing access to information and the latest scientific developments to all scientists, innovators, entrepreneurs and students and give them the opportunity to learn, observe and contribute to knowledge creation. Open Science promotes a swifter path from research to innovation to produce new products and services." Alex Lazinica, IntechOpen founder
\n\n
In conclusion, Natalia Reinic Babic, Head of Journal Publishing and Open Science at IntechOpen adds:
\n\n
“On behalf of the journal team I’d like to thank all our Editors in Chief, Editorial Boards, internal supporting teams, and our scientific community for their continuous support in making this portfolio a reality - we couldn’t have done it without you! With your support in place, we are confident these journals will become as impactful and successful as our book publishing program and bring us closer to a more open (science) future.”
\n\n
We invite you to visit the journals homepage and learn more about the journal’s Editorial Boards, scope and vision as all three journals are now open for submissions.
\n\n
Feel free to share this news on social media and help us mark this memorable moment!
\n\n
\n'}],latestNews:[{slug:"step-in-the-right-direction-intechopen-launches-a-portfolio-of-open-science-journals-20220414",title:"Step in the Right Direction: IntechOpen Launches a Portfolio of Open Science Journals"},{slug:"let-s-meet-at-london-book-fair-5-7-april-2022-olympia-london-20220321",title:"Let’s meet at London Book Fair, 5-7 April 2022, Olympia London"},{slug:"50-books-published-as-part-of-intechopen-and-knowledge-unlatched-ku-collaboration-20220316",title:"50 Books published as part of IntechOpen and Knowledge Unlatched (KU) Collaboration"},{slug:"intechopen-joins-the-united-nations-sustainable-development-goals-publishers-compact-20221702",title:"IntechOpen joins the United Nations Sustainable Development Goals Publishers Compact"},{slug:"intechopen-signs-exclusive-representation-agreement-with-lsr-libros-servicios-y-representaciones-s-a-de-c-v-20211123",title:"IntechOpen Signs Exclusive Representation Agreement with LSR Libros Servicios y Representaciones S.A. de C.V"},{slug:"intechopen-expands-partnership-with-research4life-20211110",title:"IntechOpen Expands Partnership with Research4Life"},{slug:"introducing-intechopen-book-series-a-new-publishing-format-for-oa-books-20210915",title:"Introducing IntechOpen Book Series - A New Publishing Format for OA Books"},{slug:"intechopen-identified-as-one-of-the-most-significant-contributor-to-oa-book-growth-in-doab-20210809",title:"IntechOpen Identified as One of the Most Significant Contributors to OA Book Growth in DOAB"}]},book:{item:{type:"book",id:"5060",leadTitle:null,fullTitle:"Milk Proteins - From Structure to Biological Properties and Health Aspects",title:"Milk Proteins",subtitle:"From Structure to Biological Properties and Health Aspects",reviewType:"peer-reviewed",abstract:"Milk proteins have nutritional value and extraordinary biological properties. Research over the last decades has provided new insight into the structure and the function of milk bioactive peptides. Some of these peptides are delivered directly into milk, and some are encrypted in major proteins such as caseins and lactoglobulins. These peptides have antimicrobial functions modulating the gut microflora. Even when milk is undisputedly the first food for mammals, milk proteins sometimes can be a health threat, either because of allergic reaction or because of toxicity. In this regard, in vitro studies showed donkey's casein and major whey proteins to be more digestible than cows' for human consumption. In this book, readers will find updated research on the major milk proteins' structure, bioactive peptides, milk protein allergy, therapeutic strategies, and chemical markers that can be used to detect cow milk intolerance in infants. This book provides the most current scientific information on milk proteins, from structure to biological properties. It will be of great benefit for those interested in milk production, milk chemistry, and human health.",isbn:"978-953-51-2537-2",printIsbn:"978-953-51-2536-5",pdfIsbn:"978-953-51-5451-8",doi:"10.5772/60465",price:119,priceEur:129,priceUsd:155,slug:"milk-proteins-from-structure-to-biological-properties-and-health-aspects",numberOfPages:296,isOpenForSubmission:!1,isInWos:1,isInBkci:!1,hash:"4a7d2e5f38e97aaea90bb3fec55b3751",bookSignature:"Isabel Gigli",publishedDate:"September 7th 2016",coverURL:"https://cdn.intechopen.com/books/images_new/5060.jpg",numberOfDownloads:30974,numberOfWosCitations:81,numberOfCrossrefCitations:40,numberOfCrossrefCitationsByBook:3,numberOfDimensionsCitations:111,numberOfDimensionsCitationsByBook:6,hasAltmetrics:1,numberOfTotalCitations:232,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"September 21st 2015",dateEndSecondStepPublish:"October 12th 2015",dateEndThirdStepPublish:"January 8th 2016",dateEndFourthStepPublish:"February 7th 2016",dateEndFifthStepPublish:"March 8th 2016",currentStepOfPublishingProcess:5,indexedIn:"1,2,3,4,5,6",editedByType:"Edited by",kuFlag:!1,featuredMarkup:null,editors:[{id:"175679",title:"Dr.",name:"Isabel",middleName:null,surname:"Gigli",slug:"isabel-gigli",fullName:"Isabel Gigli",profilePictureURL:"https://mts.intechopen.com/storage/users/175679/images/system/175679.jpeg",biography:"ISABEL GIGLI finished Veterinary Medicine and received her Doctoral of Science degree in Physiology (2001); she completed her doctoral research training at the Institute of Biology and Experimental Medicine (IByMe), in Buenos Aires, Argentina. Afterwards, she completed a three year Post doctoral training at the University of Cornell, USA. In addition, she worked two years at the University of Palermo, Italy. Her field of research is mammary gland physiology. With an increasing interest in sustainability and environment, in the last couple of years she focused her research on alternative uses of whey. Dr Gigli is a full-time professor at the School of Agriculture at the National University of La Pampa (UNLPam), Argentina, teaching physiology of lactation and milk production.",institutionString:"National University of La Pampa",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"2",totalChapterViews:"0",totalEditedBooks:"3",institution:{name:"National University of La Pampa",institutionURL:null,country:{name:"Argentina"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"333",title:"Food Chemistry",slug:"food-science-food-chemistry"}],chapters:[{id:"51587",title:"Casein Proteins: Structural and Functional Aspects",doi:"10.5772/64187",slug:"casein-proteins-structural-and-functional-aspects",totalDownloads:4771,totalCrossrefCites:16,totalDimensionsCites:38,hasAltmetrics:1,abstract:"Mammalian milk is a complex fluid mixture of various proteins, minerals, and lipids, which play an important role in providing nutrition and immunity to the newborn. Casein proteins, which form about 80% of the bovine milk proteins, form large colloidal particles with calcium phosphate to form casein micelles, which for many years have been an important subject of interest. Casein micelles are composed of four main types of proteins: αS1‐casein, αS2‐casein, β‐casein, and k‐casein. These constituent casein proteins lack well‐defined secondary and tertiary structure due to large amount of propyl residues. These micelles are being extensively studied because of their importance in functional behavior of milk and various milk products. However, the exact structure and nature of these casein micelles are still under debate. These different casein proteins possess different functional properties due to their primary amino acid sequence.",signatures:"Mohd Younus Bhat, Tanveer Ali Dar and Laishram Rajendrakumar\nSingh",downloadPdfUrl:"/chapter/pdf-download/51587",previewPdfUrl:"/chapter/pdf-preview/51587",authors:[{id:"178323",title:"Dr.",name:"Laishram R",surname:"Singh",slug:"laishram-r-singh",fullName:"Laishram R Singh"},{id:"183444",title:"Mr.",name:"Md. Younus",surname:"Bhat",slug:"md.-younus-bhat",fullName:"Md. Younus Bhat"}],corrections:null},{id:"50314",title:"Measurement of Casein Micelle Size in Raw Dairy Cattle Milk by Dynamic Light Scattering",doi:"10.5772/62779",slug:"measurement-of-casein-micelle-size-in-raw-dairy-cattle-milk-by-dynamic-light-scattering",totalDownloads:3427,totalCrossrefCites:2,totalDimensionsCites:7,hasAltmetrics:0,abstract:"The particle size of milk influences its microstructure and defines the qualities of dairy products, such as colloidal stability and texture. Moreover, differences in casein micelle size may affect milk processing, especially cheese making. Hence, the size of casein micelle is an important characteristic of raw milk and determines the yield of dairy products. The aim of the present research is to estimate the casein micelle size in the raw milk of dairy cattle by dynamic light scattering. The obtained results may be used for genetic elaboration of the breed, as well as to increase the competitiveness of the milk industry by selection of animals with higher casein micelle size.",signatures:"Peter Hristov, Ivan Mitkov, Daniela Sirakova, Ivan Mehandgiiski and\nGeorgi Radoslavov",downloadPdfUrl:"/chapter/pdf-download/50314",previewPdfUrl:"/chapter/pdf-preview/50314",authors:[{id:"73228",title:"Associate Prof.",name:"Peter",surname:"Hristov",slug:"peter-hristov",fullName:"Peter Hristov"},{id:"73247",title:"Associate Prof.",name:"Georgi",surname:"Radoslavov",slug:"georgi-radoslavov",fullName:"Georgi Radoslavov"},{id:"75249",title:"MSc.",name:"Ivan",surname:"Mehandzhiyski",slug:"ivan-mehandzhiyski",fullName:"Ivan Mehandzhiyski"},{id:"183257",title:"B.Sc.",name:"Ivan",surname:"Mitkov",slug:"ivan-mitkov",fullName:"Ivan Mitkov"},{id:"186009",title:"Dr.",name:"Daniela",surname:"Sirakova",slug:"daniela-sirakova",fullName:"Daniela Sirakova"}],corrections:null},{id:"50508",title:"Structure, Oligomerisation and Interactions of β-Lactoglobulin",doi:"10.5772/62992",slug:"structure-oligomerisation-and-interactions-of-lactoglobulin",totalDownloads:2622,totalCrossrefCites:3,totalDimensionsCites:9,hasAltmetrics:0,abstract:"β-Lactoglobulin (βLg), as the most abundant whey protein in ruminant milk and as a useful model protein, is the subject of countless biophysical studies in the literature, yet its physiological role is hitherto unknown. This chapter deals with studies that focus on the structure of βLg, its oligomeric behaviour and the interactions that this protein participates in. These and further studies are necessary to understand how the protein’s physicochemical properties may influence the processing, digestion and immunogenicity of ruminant milks and their products. However, there is also a need for research into the interactions that occur naturally between βLg and other components in milk, as this may give us insight into the physiological role of the protein.",signatures:"Jennifer M. Crowther, Geoffrey B. Jameson, Alison J. Hodgkinson\nand Renwick C.J. Dobson",downloadPdfUrl:"/chapter/pdf-download/50508",previewPdfUrl:"/chapter/pdf-preview/50508",authors:[{id:"178312",title:"Dr.",name:"Renwick",surname:"Dobson",slug:"renwick-dobson",fullName:"Renwick Dobson"},{id:"179047",title:"Ms.",name:"Jennifer",surname:"Crowther",slug:"jennifer-crowther",fullName:"Jennifer Crowther"},{id:"179048",title:"Dr.",name:"Alison",surname:"Hodgkinson",slug:"alison-hodgkinson",fullName:"Alison Hodgkinson"},{id:"179049",title:"Prof.",name:"Geoff",surname:"Jameson",slug:"geoff-jameson",fullName:"Geoff Jameson"}],corrections:null},{id:"50600",title:"Human Milk Lactoferrin and Antibodies: Catalytic Activities, Complexes, and Other Features",doi:"10.5772/63200",slug:"human-milk-lactoferrin-and-antibodies-catalytic-activities-complexes-and-other-features",totalDownloads:1465,totalCrossrefCites:1,totalDimensionsCites:3,hasAltmetrics:0,abstract:"Human milk is a source of biologically active proteins, including lactoferrin (LF) and antibodies (Abs). These proteins are considered as the most polyfunctional proteins of human milk. Apparently, human milk is not a simple mixture of proteins and peptides: recently it was shown that human milk contains stable supramolecular protein complex, composed of LF, α‐lactalbumin, milk albumin, β‐casein, IgG, and sIgA molecules. We believe that the whole set of different biological functions of the individual milk proteins is significantly supplemented by features of their complexes.",signatures:"Sergey E. Sedykh, Valentina N. Buneva and Georgy A. Nevinsky",downloadPdfUrl:"/chapter/pdf-download/50600",previewPdfUrl:"/chapter/pdf-preview/50600",authors:[{id:"47119",title:"Dr.",name:"Georgy",surname:"Nevinsky",slug:"georgy-nevinsky",fullName:"Georgy Nevinsky"},{id:"178315",title:"Dr.",name:"Valentina",surname:"Buneva",slug:"valentina-buneva",fullName:"Valentina Buneva"},{id:"178316",title:"Ph.D.",name:"Sergey",surname:"Sedykh",slug:"sergey-sedykh",fullName:"Sergey Sedykh"}],corrections:null},{id:"50749",title:"Milk Proteins: Processing of Bioactive Fractions and Effects on Gut Health",doi:"10.5772/63509",slug:"milk-proteins-processing-of-bioactive-fractions-and-effects-on-gut-health",totalDownloads:1706,totalCrossrefCites:3,totalDimensionsCites:5,hasAltmetrics:0,abstract:"Milk is nature’s most complete food. While milk clearly provides basic nutritional requirements, bioactive components within milk also impart a wide range of additional health benefits to both the neonate and the adult. However, human milk is compositionally different from cow’s milk, and certain protein components of cow’s milk can act as allergens to susceptible humans. One way of extracting the benefits of cow’s milk proteins, while eliminating the risk of allergenicity in humans, is to hydrolyse the milk proteins. Hydrolysis of milk proteins generates smaller peptide sequences from their parent protein that can be biologically active when released. At an industrial scale, hydrolysis of milk proteins can be achieved through either enzymatic hydrolysis or fermentation. An alternative process of generating similar sized peptides is by in silico synthesis. These compounds can subsequently be developed as fortifying food agents.",signatures:"Anindya Mukhopadhya and Torres Sweeney",downloadPdfUrl:"/chapter/pdf-download/50749",previewPdfUrl:"/chapter/pdf-preview/50749",authors:[{id:"178622",title:"Dr.",name:"Torres",surname:"Sweeney",slug:"torres-sweeney",fullName:"Torres Sweeney"},{id:"179091",title:"Dr.",name:"Anindya",surname:"Mukhopadhya",slug:"anindya-mukhopadhya",fullName:"Anindya Mukhopadhya"}],corrections:null},{id:"50690",title:"Bioactive Peptides from Milk",doi:"10.5772/62993",slug:"bioactive-peptides-from-milk",totalDownloads:2414,totalCrossrefCites:1,totalDimensionsCites:6,hasAltmetrics:0,abstract:"Milk is a major source of dietary energy, protein and fat. Due to their specific biological properties leading to health benefits, bioactive peptides (BAPs) derived from milk proteins have been a subject of intensive research during past two decades. These peptide sequences, encrypted within proteins, are liberated in vivo during gastrointestinal digestion or in vitro by fermentation with proteolytic starter cultures or using proteases. BAP generally comprises 2–20 amino acid (AA) residues. Isolation and characterization of BAP of different bioactivities from milk protein hydrolysates of cow, buffalo, camel, goat, mare, sheep, donkey and yak milks have been reported. Bioactivities of BAP, which depend on constituent AAs and the sequence, include mineral binding, opioid, angiotensin-converting enzyme (ACE) inhibition, immunomodulatory, cytotoxicity, antibacterial and antithrombotic. This chapter focuses on the methodologies adopted to produce BAPs and their prospective role in health enhancing nutraceuticals/pharmaceuticals.",signatures:"R. Anusha and O.S. Bindhu",downloadPdfUrl:"/chapter/pdf-download/50690",previewPdfUrl:"/chapter/pdf-preview/50690",authors:[{id:"180942",title:"Dr.",name:"Pradip",surname:"Bindhu",slug:"pradip-bindhu",fullName:"Pradip Bindhu"},{id:"185368",title:"Mrs.",name:"Anusha",surname:"R",slug:"anusha-r",fullName:"Anusha R"}],corrections:null},{id:"51564",title:"An Important Milk Enzyme: Lactoperoxidase",doi:"10.5772/64416",slug:"an-important-milk-enzyme-lactoperoxidase",totalDownloads:3225,totalCrossrefCites:6,totalDimensionsCites:12,hasAltmetrics:1,abstract:"It has been acknowledged since ancient times that milk and dairy products have a vital role in nutrition and contribute considerably to human health. Because of its content, Because of its content, it has many important effects on the life that include immunoglobulins, enzymes, hormones, growth factors, antibacterial agents, fat acids, vitamins, and minerals. Approximately 70 indigenous enzymes have been reported in normal bovine milk, including lactoperoxidase. Lactoperoxidase LPO is a natural constituent of milk, saliva, and tears. It also exists in all mammary milk. LPO is an iron heme group basic glycoprotein, with a molecular weight of approximately 78 kDa. The LPO enzyme catalyzes the H2O2 +SCN- → OSCN- + H2O reaction. Hydrogen peroxide and hypothiocyanate are indispensable for antimicrobial activity. The biological significance of LPO is involved in the natural host defense system against pathogenic microorganisms.",signatures:"Zeynep Koksal, Ilhami Gulcin and Hasan Ozdemir",downloadPdfUrl:"/chapter/pdf-download/51564",previewPdfUrl:"/chapter/pdf-preview/51564",authors:[{id:"178914",title:"Prof.",name:"İlhami",surname:"Gulcin",slug:"ilhami-gulcin",fullName:"İlhami Gulcin"},{id:"178915",title:"Dr.",name:"Zeynep",surname:"Köksal",slug:"zeynep-koksal",fullName:"Zeynep Köksal"}],corrections:null},{id:"50211",title:"Bioactive Lactoferrin-Derived Peptides",doi:"10.5772/62569",slug:"bioactive-lactoferrin-derived-peptides",totalDownloads:1577,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"Lactoferrin (LF) is a member of the transferrin family that is a cationic iron-binding protein. It is an 80-kDa glycoprotein that is found in many secretions in the body and is highly present in milk and colostrums. It exerts antibacterial effects and has a wide range of biological activities. Moreover, it is considered as a precursor of different peptides that have multifunctional bioactivities. During the last decade, several applications of LF and its peptides have been discovered, which has led to its commercial production. Therefore, LF and its peptides can offer a variety of specialized ingredients that can be tailored to meet the needs of natural food preservatives and functional food ingredients.",signatures:"Adham M. Abdou and Hend A. Elbarbary",downloadPdfUrl:"/chapter/pdf-download/50211",previewPdfUrl:"/chapter/pdf-preview/50211",authors:[{id:"151093",title:"Dr.",name:"Adham",surname:"Abdou",slug:"adham-abdou",fullName:"Adham Abdou"},{id:"184758",title:"Dr.",name:"Hend",surname:"Elbarbary",slug:"hend-elbarbary",fullName:"Hend Elbarbary"}],corrections:null},{id:"50445",title:"The Protein Component of Sow Colostrum and Milk",doi:"10.5772/62841",slug:"the-protein-component-of-sow-colostrum-and-milk",totalDownloads:2263,totalCrossrefCites:2,totalDimensionsCites:8,hasAltmetrics:0,abstract:"The production of colostrum and milk by the sow are primary limiting factors affecting survival, growth and development of the piglets. The proteins of colostrum and milk provide not only a supply of amino acids to the neonate but also a wide range of bioactive factors. Proteins in sow mammary secretions include those associated with the milk fat membranes, caseins, mammary-derived whey proteins, immunoglobulins, hormones and growth factors, enzymes, and a wide range of other proteins. Concentrations of most milk-specific proteins typically are lower in colostrum than in milk, while concentrations of immunoglobulins and other bioactive proteins often are enriched in colostrum compared with mature milk. Dietary protein is utilized for milk protein production with approximately 50% efficiency. During both the colostrum period and at peak lactation as much as 700–800 g of protein is secreted daily by today’s highly prolific sows. Estimates of daily milk protein secretion during lactation suggest that sows are not able to consume sufficient dietary protein and energy to account for output of solids in milk and therefore must mobilize body protein and body fat to support their milk production. Milk protein content typically is not affected by dietary treatment, indicating that the sow mobilizes her body reserves to maintain milk production and milk protein production. These observations are of particular interest for today’s highly prolific sows, which may require more dietary protein than previous genotypes.",signatures:"P.K. Theil and W.L. Hurley",downloadPdfUrl:"/chapter/pdf-download/50445",previewPdfUrl:"/chapter/pdf-preview/50445",authors:[{id:"136109",title:"Dr.",name:"Walter",surname:"Hurley",slug:"walter-hurley",fullName:"Walter Hurley"},{id:"185771",title:"Dr.",name:"Peter",surname:"Theil",slug:"peter-theil",fullName:"Peter Theil"}],corrections:null},{id:"50213",title:"Donkey Milk Proteins: Digestibility and Nutritional Significance",doi:"10.5772/62597",slug:"donkey-milk-proteins-digestibility-and-nutritional-significance",totalDownloads:2026,totalCrossrefCites:3,totalDimensionsCites:16,hasAltmetrics:0,abstract:"Donkey milk is particularly recommended for infant nutrition as substitute of cow milk in case of sensitive neonates (showing cow milk protein allergies). Its protein composition and the ratio between caseins and whey proteins reveals a high similarity with human milk, thus, in the last 10 years, an increasing interest arose to obtain a full characterisation of donkey milk proteins, here acknowledged. Digestibility data, mainly derived in vitro with human gastrointestinal enzymes, showed the high digestibility of donkey caseins and major whey proteins, except lysozyme and α-lactalbumin which proved to be quite resistant. The reported antimicrobial properties of donkey milk open concrete possibilities to use donkey milk as natural food preservative. Due to its attractive healthy properties, donkey milk was investigated for useful applications or to develop novel foods characterised by a high nutritional profile.",signatures:"Donata Marletta, Flavio Tidona and Salvatore Bordonaro",downloadPdfUrl:"/chapter/pdf-download/50213",previewPdfUrl:"/chapter/pdf-preview/50213",authors:[{id:"178798",title:"Prof.",name:"Donata",surname:"Marletta",slug:"donata-marletta",fullName:"Donata Marletta"},{id:"184946",title:"Dr.",name:"Flavio",surname:"Tidona",slug:"flavio-tidona",fullName:"Flavio Tidona"},{id:"184947",title:"Prof.",name:"Salvatore",surname:"Bordonaro",slug:"salvatore-bordonaro",fullName:"Salvatore Bordonaro"}],corrections:null},{id:"50202",title:"Usefulness of Faecal Markers in Cow’s Milk Protein Immunomediated Reactions",doi:"10.5772/62544",slug:"usefulness-of-faecal-markers-in-cow-s-milk-protein-immunomediated-reactions",totalDownloads:1817,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"Cow’s milk protein allergy (CMPA) affects children most commonly than adults, with symptoms usually developing before 1 year of age and within 1 week after the intake of cow’s milk. Food allergies can be divided into: IgE mediated and non-IgE mediated. Some reactions may include both mechanisms (mixed type). The most studied faecal Mar-kers, so far, are calprotectin, Tumor necrosis factor-alpha (TNF-α), beta-defensin and eosinophil cationic protein (ECP). Calprotectin belongs to the S-100 family of calcium-binding proteins and seems to be involved in the regulation of inflammation. Faecal calprotectin (FC) values are significantly higher in infants suspected of having CMPA than in a comparison group of healthy infants. Moreover, there is a significant decrease in FC in infants with CMPA after a period of dietary antigen elimination, although levels use to remain higher than in age- and diet-matched comparisons. TNF-α is a cytokine involved in systemic inflammation and is one of the cytokines that make up the acute phase reaction. TNF-α expression in the epithelial cells and mononuclear cells in the lamina propria is markedly increased in FPIES patients. TNF-α is also increased in the stools of patients with gastrointestinal milk allergy after milk challenge. Defensins are small (~29 to 42 amino acid) cationic arginine and cysteine rich, amphipathic peptides with a molecular weight of 3–5 kDa. They can be classified into three groups: α-, β- and θ-defensins. Among them, only α- and β-defensins are expressed in humans. Defensins display various functions, including antimicrobial activity and also act as chemoattractant. They contribute to host immunity and to maintain the balance between pathogens and normal flora. Beta-defensins values detected in infants with a previous diagnosis of CMPA prior to the oral food challenge, and during each provocation do not seem to show significant changes. ECP is a single-chain, zinc-containing protein with a molecular weight ranging from 16 to 22 kDa and is one of the most important proteins in the granules of eosinophil granulocytes. Infants with atopic eczema exhibit a specific faecal protein pattern characterized by an increase in both ECP and TNF-α. The faecal concentration of ECP enhances particularly in patients with immediate-type reactions to the cow’s milk challenge whereas faecal TNF-α enhances in those with delayed-type reactions, confirming the different pathogenesis (IgE mediated and non-IgE mediated) of these two types of reactions.",signatures:"Maria Elisabetta Baldassarre, Raffaella Panza and Nicola Laforgia",downloadPdfUrl:"/chapter/pdf-download/50202",previewPdfUrl:"/chapter/pdf-preview/50202",authors:[{id:"176045",title:"Prof.",name:"Maria Elisabetta",surname:"Baldassarre",slug:"maria-elisabetta-baldassarre",fullName:"Maria Elisabetta Baldassarre"},{id:"176169",title:"Dr.",name:"Raffaella",surname:"Panza",slug:"raffaella-panza",fullName:"Raffaella Panza"},{id:"176170",title:"Prof.",name:"Nicola",surname:"Laforgia",slug:"nicola-laforgia",fullName:"Nicola Laforgia"}],corrections:null},{id:"50598",title:"Allergenic Milk Proteins. Friend or Foe Nutritional Proteins?",doi:"10.5772/62628",slug:"allergenic-milk-proteins-friend-or-foe-nutritional-proteins-",totalDownloads:1808,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:1,abstract:"Allergies are complex inflammatory diseases with a not fully understood etiology. Several factors, including genetic, environmental, age of exposition, diet, etc., are associated with the induction of these diseases. The incidence of allergies has increased during the last decades and constitutes the most common immune-based disease worldwide. According to the hygiene hypothesis, a lower exposure to pathogens and commensal microbes that reside in the intestinal lumen is responsible for the rapid rise of the prevalence of atopic and allergic disorders, specifically food allergy. To overcome this tendency, the immunological mechanisms underlying this pathology should be better understood, which will undoubtedly impact the development of novel therapies. A large body of evidence demonstrates that immunotherapies constitute corrective treatments of the impaired regulation of the immune system in allergic patients.",signatures:"Guillermo Docena, Paola Smaldini, Renata Curciarello and Angela\nMaría Candreva",downloadPdfUrl:"/chapter/pdf-download/50598",previewPdfUrl:"/chapter/pdf-preview/50598",authors:[{id:"70459",title:"Dr.",name:"Guillermo",surname:"Docena",slug:"guillermo-docena",fullName:"Guillermo Docena"}],corrections:null},{id:"50650",title:"Insights into the Interaction of Milk and Dairy Proteins with Aflatoxin M1",doi:"10.5772/63433",slug:"insights-into-the-interaction-of-milk-and-dairy-proteins-with-aflatoxin-m1",totalDownloads:1854,totalCrossrefCites:3,totalDimensionsCites:7,hasAltmetrics:0,abstract:"In this chapter, up-to-date data regarding the nature of protein interaction with a contaminant such as aflatoxin M1 (AFM1) is detailed. Considering that AFM1 is a relevant toxin present in milk and dairy products, it is important to understand such interaction. With this in mind, some specific features of protein chemistry and structure are discussed. AFM1 presence and origin in milk and the latest approaches in AFM1 chemical analysis with special attention to sample preparation techniques to eliminate milk protein–AFM1 interaction will also be addressed. Emphasis will be given to the interaction of AFM1 with whey proteins of which little has been described. In order to represent such interactions, recent scientific evidence is briefly discussed which describes the outcome, stability, and distribution of the toxin among the fractions, especially during the cheese-making process. An in silico model is presented in which some details of the AFM1-protein interactions are described. Finally, two technological applications of proteins in the food industry which are affected negatively by AFM1 contamination, are provided as an example of how the contaminant has a deep relationship in protein behaviour.",signatures:"Fabio Granados-Chinchilla",downloadPdfUrl:"/chapter/pdf-download/50650",previewPdfUrl:"/chapter/pdf-preview/50650",authors:[{id:"178287",title:"B.Sc.",name:"Fabio",surname:"Granados",slug:"fabio-granados",fullName:"Fabio Granados"}],corrections:null}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},subseries:null,tags:[{id:"65",label:"highly cited contributor"}]},relatedBooks:[{type:"book",id:"8625",title:"Whey",subtitle:"Biological Properties and Alternative Uses",isOpenForSubmission:!1,hash:"449a36f43c9a30ae4d43f9775599e8ac",slug:"whey-biological-properties-and-alternative-uses",bookSignature:"Isabel Gigli",coverURL:"https://cdn.intechopen.com/books/images_new/8625.jpg",editedByType:"Edited by",editors:[{id:"175679",title:"Dr.",name:"Isabel",surname:"Gigli",slug:"isabel-gigli",fullName:"Isabel Gigli"}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"5507",title:"Current Topics in Lactation",subtitle:null,isOpenForSubmission:!1,hash:"ac8a108f23ad313d4ea64202d68c7502",slug:"current-topics-in-lactation",bookSignature:"Isabel Gigli",coverURL:"https://cdn.intechopen.com/books/images_new/5507.jpg",editedByType:"Edited by",editors:[{id:"175679",title:"Dr.",name:"Isabel",surname:"Gigli",slug:"isabel-gigli",fullName:"Isabel Gigli"}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1408",title:"Scientific, Health and Social Aspects of the Food Industry",subtitle:null,isOpenForSubmission:!1,hash:"e683dc398eabec0db3a88e891209a406",slug:"scientific-health-and-social-aspects-of-the-food-industry",bookSignature:"Benjamin Valdez",coverURL:"https://cdn.intechopen.com/books/images_new/1408.jpg",editedByType:"Edited by",editors:[{id:"65522",title:"Dr.",name:"Benjamin",surname:"Valdez",slug:"benjamin-valdez",fullName:"Benjamin Valdez"}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"8504",title:"Pectins",subtitle:"Extraction, Purification, Characterization and Applications",isOpenForSubmission:!1,hash:"ff1acef627b277c575a10b3259dd331b",slug:"pectins-extraction-purification-characterization-and-applications",bookSignature:"Martin Masuelli",coverURL:"https://cdn.intechopen.com/books/images_new/8504.jpg",editedByType:"Edited by",editors:[{id:"99994",title:"Dr.",name:"Martin",surname:"Masuelli",slug:"martin-masuelli",fullName:"Martin Masuelli"}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"7332",title:"Some New Aspects of Colloidal Systems in Foods",subtitle:null,isOpenForSubmission:!1,hash:"0dd822267e027684bd3ff53da4f2ef41",slug:"some-new-aspects-of-colloidal-systems-in-foods",bookSignature:"Jafar M. 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\r\n\tOrganic electronics can impact healthcare, sports, and national security through inventions such as real-time biosensing and drug-delivery, stretchable and flexible sport track gear, and the electronic- nose and tongue. Organic semiconductors, based on carbon and hydrogen, two of the most abundant and low cost materials, can transduce ionic and electronic carriers into quantifiable data paving the way for multi-functional applications that are not easy to create with other material systems and often go beyond the working principle of the conventional field-effect transistor. We will begin our review with a general overview of the current state of OFETs focusing on complex architectures, materials and fabrication processes. We will discuss the device physics and explain the doping mechanisms that can exist in organic semiconducting channel materials. Then we will focus on exciting applications that include the electronic- nose and tongue, myriad biosensing applications for preventive, point-of-care testing and real-time drug delivery, emerging physico-chemical low cost sensing applications, and the well known flexible, stretchable electronics.
",isbn:null,printIsbn:"979-953-307-X-X",pdfIsbn:null,doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,isSalesforceBook:!1,hash:"787c5b02acbbf3f4efda634be5e6f3c0",bookSignature:"Dr. Jonathan Sayago",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/7741.jpg",keywords:"double-gate, floating-gate, abundant materials, charge carrier mobilities, electronic nose, electronic tongue, preventive health care, real-time drug delivery, radiation dosimeters, pH meter, sport track gear, wearable electronics",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:0,numberOfDimensionsCitations:0,numberOfTotalCitations:0,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"November 7th 2019",dateEndSecondStepPublish:"March 10th 2020",dateEndThirdStepPublish:"May 9th 2020",dateEndFourthStepPublish:"July 28th 2020",dateEndFifthStepPublish:"September 26th 2020",remainingDaysToSecondStep:"2 years",secondStepPassed:!0,currentStepOfPublishingProcess:5,editedByType:null,kuFlag:!1,biosketch:null,coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"198513",title:"Dr.",name:"Jonathan",middleName:null,surname:"Sayago",slug:"jonathan-sayago",fullName:"Jonathan Sayago",profilePictureURL:"https://mts.intechopen.com/storage/users/198513/images/system/198513.jpg",biography:"Jonathan Javier Sayago Hoyos is a research associate at the National Autonomous University of Mexico. During his doctoral studies, Dr. Sayago tackled the problem of achieving low-voltage organic transistors employing electrolytes as the gating medium. His research contributed to shedding light on fundamental physicochemical processes in electrochemical transistors and energy storage devices. After his PhD studies, Dr. Sayago worked as a consultant for Bowhead Health Inc., a Canadian startup company aiming for the commercialization of bioelectronic devices for preventive medical applications. His team designed and built a biosensor device capable of testing 50 µl of blood which led the company to secure a private funding from the world-class Mexican company Grupo Arcoiris. As a Postdoctoral Researcher at the Institute of Renewable Energies, UNAM, Dr. Sayago investigates biocompatible and biodegradable electrodes engineered for energy storage and heat transfer applications. Derived from this work he authored and co-authored over 10 articles in highly recognized international journals, 3 book chapters and participated in numerous international conferences and workshops. Dr. Sayago has taught courses in mathematics, advanced physics laboratory, computer assisted design and 3D printing, and tutoring sessions. 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1. Introduction
1.1. Cellulose and cellulose biomass
A cellulose molecule is a linear polymer of D-anhydroglucopyranose units linked by β-1, 4-glucosidic bonds (Figure 1). On its reducing end, a cellulose molecule has an unsubstituted hemiacetal. On its non-reducing end, it has a hydroxyl group.
Figure 1.
Molecular structure of a cellulose molecule.
Cellulose is the skeleton structure of almost all green plants. It is particularly abundant in non-food plants like trees and grasses, which typically have 40-60% cellulose, 20-40% hemicellulose, and 10-25% lignin (Lynd et al., 2002; Yang et al., 2007). There are four major polymorphs of cellulose: I, II, III, and IV. Cellulose I, often found in native cellulose, contains allomorphs Iα (bacteria and algae) and Iβ (higher plants) (Kontturi et al., 2006; Pérez & Samain, 2010). Cellulose I, when treated with a concentrated alkaline solution, turns into cellulose II, a thermodynamically more stable crystalline form than cellulose I. Cellulose IIII can be obtained when cellulose microcrystal is subjected to supercritical ammonia. The structure of another allomorph of cellulose III, IIIII is still being debated. Cellulose IVI and IVII are formed when cellulose III is heated in glycerol at 260°C (Peter, 2001).
Figure 2.
A) Hydrophilic and hydrophobic sites of cellulose. (B) Schematic drawing of the intrasheet hydrogen-bonding network in cellulose Iα.
Various noncovalent interactions such as hydrogen bonding and van der Waals interactions are present in the ultrastructure of cellulose. While the OH-O hydrogen bonding is mostly responsible for cellulose intrasheet interactions, both the weaker CH-O hydrogen bonding and van der Waals interactions contribute to cellulose intersheet interactions (Li Q. & Renneckar, 2011). Figure 2 shows the arrangement of the intrasheet hydrogen bonding network in cellulose Iα and the resulting hydrophilic and hydrophobic sites of the ring plane (Brown & Saxena, 2007). Overall, because of these noncovalent interactions, cellulose chains aggregate into various forms of ultrastructure, which do not melt or dissolve in any common solvents. Such aggregation prevents the potential cleavage sites (i.e., glycosidic bonds) of a cellulose chain from being accessed by cellulase.
1.2. Degradation of cellulose in biomass conversion
The biomass conversion is the key step to produce biofuel from cellulosic biomass. Such conversion is often accomplished either through biochemical methods or thermochemical methods, where the polysaccharides in cellulosic biomass are hydrolyzed by biochemical agents such as cellulase enzyme, or by thermal treatment such as gasification to produce simple sugars that are fermentable to produce biofuel products (Dwivedi et al., 2009). For biochemical methods (Gray et al., 2006), cellulases are usually employed to convert the solid cellulosic biomass into glucose or small sugar polymers that can be readily fermented with microorganism to produce ethanol. Compared to thermochemical methods which often require a large amount of acid and energy, biochemical methods are more environmentally friendly and economically feasible because of their better conversion efficiencies and milder operating conditions. By far the enzyme-based biochemical methods are considered as the most promising technologies for biomass conversion. However, because of biomass recalcitrance and high cost of cellulase in biomass conversion, the current process for biofuel production is not yet a viable option for the large-scale production (Dwivedi et al., 2009). Much research and developmental efforts have been dedicated to the improvement of the efficiency of cellulase in biomass conversion. One feasible approach is through the incorporation of new features (mutations) into cellulase that accelerate key steps (e.g., rate limiting step) of the enzymatic process. This approach requires a comprehensive mechanistic understanding of cellulose hydrolysis by cellulase.
Figure 3.
The process of biomass conversion through the enzyme-based biochemical method.
1.3. Cellulase and enzymatic hydrolysis of cellulose
Cellulase (Lynd et al., 2002; Mosier et al., 1999;\n\t\t\t\t\tWilson & Irwin, 1999), like all glycosyl hydrolase enzymes found in bacteria, fungi, plants and some invertebrate animals, breaks down β-1, 4-glycosidic bonds of cellulose through general acid/base catalysis. There are mainly three kinds of cellulases: exo-β-1, 4-D-glucanase, endo-β-1, 4-D-glucanase and β-D-glucosidase. Each enzyme alone cannot hydrolyze the complex crystalline cellulose efficiently but working synergistically with other types of cellulases can increase the rate of hydrolysis significantly (Dwivedi et al., 2009; Lynd et al., 2002).
Exo-β-1, 4-D-glucanase can access individual cellulose chains from the exposed reducing end or non-reducing end and cleave two to four glucose units at a time to produce tetrasaccharides or disaccharides (i.e., cellobioses) (Figure 4).
Endo-β-1, 4-D-glucanase breaks internal glycosidic bonds of individual cellulose chains to disrupt the network structure of cellulose and expose individual polysaccharide chains (Figure 4).
β-D-Glucosidase or cellobiase hydrolyzes cellobiose to release D-glucose units.
Figure 4.
Schematic illustration of cellulose hydrolysis by exo-β-1, 4-D-glucanase and endo-β-1, 4-D-glucanase.
Most of fungal cellulases have a domain like structure that contains a catalytic domain (CD) and a carbohydrate binding module (CBM) (Martin, 2000). These two domains are connected by a peptide linker, which is known to maintain the separation between the CD and the CBM (Figure 5). The CD contains the enzyme active site that is responsible for cellulose hydrolysis. The CBM is a contiguous amino acid sequence that anchors the CD onto the surface of cellulose through hydrogen bonding and van der Waals interactions (Boraston et al., 2004; Guillén et al., 2010). Cellulases can be grouped into families according to sequence similarities of their amino acid residues within their CDs and CBMs.
Figure 5.
The domain like structure of the cellulase cellobiohydrolase I (CBH I) that is bound to cellulose Iβ microfibril. (Zhong et al., 2008)
Cellulose hydrolysis by cellulase is a multi-step process (Chundawat et al., 2011) that is initiated with the binding of cellulase (E) onto the surface of cellulose (S), shown in Figure 6. After this “initial binding” step, a single cellulose chain will be separated from the cellulose aggregate by cellulase and pulled into the active site of cellulase. This is the “decrystallization” step which forms a pseudo-Michaelis complex (E*S). E*S will then undergo “hydrolytic cleavage” to produce cellobiose as the product (P).
Figure 6.
Mechanism of cellulose hydrolysis by cellulase.
For cellulose hydrolysis, the substrate cellulose is water insoluble and resistant to the attack by biological agents. This makes the formation of E*S much more difficult compared to those formed with soluble substrates.
1.4. Knowledge gap
The initial binding (step 1 in Figure 6) has been extensively studied over the years. A Langmuir equation is widely used as a simplified mechanistic model to describe the formation of ES resulting from the initial interaction between the cellulase and the cellulose, which often reaches steady-state within half an hour (Lynd et al., 2002; Zhang Y. H. & Lynd, 2004). Other equilibrium binding models and dynamic binding models have also been proposed to account for the complexities of the binding process including the partially irreversible adsorption of cellulase, multiple types of adsorption site, and so on (Lynd et al., 2002).
For cellulose hydrolysis, most recent studies have been focused on elucidation of the mechanism of the hydrolytic cleavage reaction (step 3 in Figure 6) (Divne et al., 1998; Li Y. et al., 2007; Parsiegla et al., 2008). Some of the key amino acid residues involved in cleavage reactions have been identified. The distinctions between endo- and exo-glucanases, and between retention and inversion for the stereo configuration of the products have been made after years of biochemical and biophysical studies. The majority of studies on the hydrolytic cleavage step were done by measuring the concentration of the sugars (P) released during cleavage of soluble cellodextrins or insoluble cellulose.
Meanwhile, very little success has been achieved in obtaining fundamental knowledge of the enzymatic decrystallization reaction in step 2 (DOE/SC-0095, 2006). In particular, the importance of enzymatic decrystallization was largely unnoticed until very recently (Chundawat et al., 2011; DOE/SC-0095, 2006; Wilson, 2009). Several pieces of biochemical and physical evidence have indicated the presence of such an activity. Back to 1997, Wilson and his coworker showed that cleavage of the β-1, 4-glycosidic linkage in crystalline cellulose is not the rate-limiting step for T. fusca endoglucanase E2 (Zhang S. & Wilson, 1997). They speculated that the binding of a cellulose chain from a microfibril into the active site of a cellulase is the rate-limiting step for degradation of crystalline cellulose (Wilson, 2009). Lee and coworkers found indentations and paths on the surface of cotton fibers that had been treated with a cellulase that was incapable of hydrolytic cleavage (Lee et al., 2000). The evidence suggests that such surface modifications on cellulose are likely caused by the decrystallization activity of cellulase.
Figure 7.
Mechanistic models of enzymatic decrystallization. (A) The CBM model: the CBM serves as a wedge to assist the release of a single cellulose chain. (B) The CD model: the protrusion of the CD domain serves as a wedge to assist the release of a single cellulose chain.
The mechanistic model for enzymatic decrystallization proposed by Reilly and coworkers is shown in Figure 7A (Mulakala & Reilly, 2005). In this model, the CBM is inserted under a cellulose chain like a wedge to separate the chain from the cellulose network. Then the released cellulose chain is pulled into the active site of the CD along the top face of the CBM to achieve the decrystallization. In this model, the CBM is essential to enzymatic decrystallization of cellulose. Numerous biochemical studies, however, have shown that in the absence of the CBM, the CD domain alone still retains 20~50% of the hydrolytic activity on crystalline cellulose (Reinikainen et al., 1992; Srisodsuk et al., 1993;\n\t\t\t\t\tVan Tilbeurgh et al., 1986). To resolve this discrepancy, we propose an alternative mechanistic model, where a wedge-like structure at the bottom of the CD can be inserted under the cellulose chain to lift it into the active site of the CD (Figure 7B). Since decrystallization by cellulase has been speculated to be the rate limiting step for the degradation of crystalline cellulose (DOE/SC-0095, 2006; Wilson, 2009), understanding the mechanism of this enzymatic activity becomes essential to a comprehensive understanding of cellulose hydrolysis by cellulase.
2. Innovative approach and microcantilever
2.1. Existing technologies and their technical limitations
The conventional approaches to study the cellulose hydrolysis by cellulase are based on the measurement of the concentration of glucose or other simple sugars that are produced in the hydrolytic process. These approaches are not suitable for studying the decrystallization process because no new product is formed and released from this process. Spectroscopic techniques such as Fourier transform infrared spectroscopy (Fengel et al., 1995), Raman spectroscopy (Schenzel et al., 2005), and x-ray photoelectron spectroscopy (Ahola et al., 2008; Fardim et al., 2005) have been used to study the structural change of cellulose fibers. All these techniques focus on the global variations of cellulose. Since cellulose decrystallization only occurs on the outer layer within a relative small region of the surface of cellulose, these techniques are not sensitive enough for such study. Quartz crystal microbalance has been used to study the enzymatic hydrolysis of cellulose (Ahola et al., 2008; Rojas Orlando et al., 2007;\n\t\t\t\t\tTuron et al., 2008), however, its suitability for studying decrystallization has not yet been demonstrated.
Figure 8.
Various shapes of AFM probes.
Atomic force microscopy (AFM) has been used to examine changes of surface morphology of cellulose. Typical size of AFM probe is 200 μm x 40 μm x 1 μm (length x width x thickness) with various shapes (Figure 8). Lee and coworkers used the tapping mode AFM to exam the effects of three different cellulases on the surface of cotton fibers (Lee et al., 2000). Li and coworkers used the AFM to detect structural changes of cellulose microfibril fragments caused by sonication (Li Q. & Renneckar, 2011). With this powerful surface imaging tool, we can investigate the surface change caused by enzymatic activities. However, AFM imaging is mostly limited to the surface analysis at discrete time points. Additionally a high quality image requires that the surface area of cellulose be prepared prior to imaging. Any extensive handling may potentially alter the surface properties and delay the timely analysis under the assay conditions. Therefore, AFM imaging is not an ideal approach for analyzing the dynamic impact of cellulase on cellulose. Both scanning electron microscopy and transmission electron microscopy have similar limitations. This has led to the development of the microcantilever technique for cellulase study.
2.2. Microcantilever and its applications
The microcantilever is a highly sensitive nanomechanical sensor that originates from a micro-fabricated AFM probe. Typical dimensions of a microcantilever, which are similar to AFM probes, are 200 µm long, 1 µm thick, and 20 µm wide (Goeders et al., 2008; Lavrik et al., 2004). The microcantilever is capable of detecting minute changes in interaction energy between individual molecules in the thin film of a polymer coating (cellulose, protein, DNA, or polymer brush) in the form of a measurable bending (10-6 to 10-12 m) of the microcantilever (Moulin et al., 1999; Mukhopadhyay et al., 2005; Shu et al., 2005; Yan et al., 2006; Zhao et al., 2010; Zhou et al., 2006). The microcantilever bending can be measured based on the deflection of a laser beam reflecting from the tip of the microcantilever in the AFM (Figure 9). Overall, the microcantilever detection has high specificity, high sensitivity, and quick response.
Figure 9.
Working scheme of the microcantilever.
Dynamic mode (Vashist, 2007): When an analyte is adsorbed on an oscillating microcantilever, the microcantilever will oscillate at a lower frequency. The difference in frequency can be used to measure properties of adsorbates, such as viscosity and density, etc.
Static mode (Vashist, 2007): Adsorbates tend to induce a significant change in surface stress of a microcantilever, which results in a deflection of the microcantilever (Lavrik et al., 2004; Shuttleworth, 1950). The surface stress and the deflection of the microcantilever are quantitatively related (Yan et al., 2006):
Δz=3(1−ν)l2Et2ΔσE1
(1)
Where Δz is the deflection of the microcantilever at the end of the microcantilever, ν and E are Poisson’s ratio and Young’s modulus of the microcantilever, t and l are the thickness and length of the microcantilever, and ∆σ is the differential stress on the microcantilever. Using the static mode microcantilever sensor, Ji and coworkers investigated the conformational change of calmodulin (Yan et al., 2006). Sauers and coworkers successfully detected 2-mercaptoethanol using a gold-coated microcantilever (Datskos & Sauers, 1999). Zhou and coworkers successfully demonstrated the use of the microcantilever bending as a means to probe changes in internal structure of polymer brushes in response to changes in pH and electrolyte concentration (Zhou et al., 2006).
2.3. Microcantilever in cellulose study
In cellulose, the interaction energy arises from noncovalent interactions (hydrogen bonding and van der Waals interactions) between tightly packed cellulose chains. To release cellulose chains, surface-adsorbed cellulase must break up noncovalent interactions between cellulose chains through decrystallization, which results in a change in overall interaction energy in the cellulose. If cellulose is deposited onto a microcantilever, such dynamic change in interaction energy will be transduced from the cellulose coating into the microcantilever, and will result in a measurable bending of the microcantilever. Thus, the unique link between the enzymatic decrystallization and the resulting energy alteration in cellulose measured by the microcantilever bending has provided a novel strategy to experimentally examine this unusual enzymatic activity.
Such adsorbate-induced bending often occurs in the presence of a specific interaction (e.g., decrystallization) between an adsorbate (e.g., cellulase) and a substrate (e.g., cellulose) that can alter the internal energy of the substrate. Since a mere adsorption such as the initial binding of cellulase on cellulose has a very minimum impact on the internal energy of cellulose, it will not induce a measurable bending even though the surface-bound cellulase changes the overall gravity (mass) on the microcantilever. Therefore the microcantilever bending can be attributed primarily to enzymatic actions (e.g., enzymatic decrystallization and hydrolytic cleavage) after the initial binding. Because the extent of bending is linearly proportional to the effective concentration of adsorbed species on the microcantilever (Berger et al., 1997; Desikan et al., 2006; Velanki & Ji, 2006), the real-time measurement of the microcantilever bending will reveal the kinetics for enzymatic actions including enzymatic decrystallization by cellulase. To our knowledge, this is the first use of a nanomechanical sensor to study mechanistic enzymology and heterogeneous enzymatic catalysis that involves a solid substrate (e.g., cellulose).
3. Investigation of the interaction between cellulase and cellulose
3.1. Materials and methods
Materials: Microcrystalline cellulose, dimethyl sulfoxide (DMSO), and N-methylmorpholine -N-oxide (NMMO) were purchased from Sigma-Aldrich (St. Louis, MO). Polyvinylamine (PVAM) was purchased from BASF (Florham Park, NJ). The microcantilevers (200 µm × 25 µm × 2 µm, 0.1 N/m) were home-made.
Preparation of the cellulose-coated microcantilever (Zhao et al., 2010): The cellulose II model surface was prepared on the front side of a microcantilever that was made of SiO2. The surface of the microcantilever was first treated with UV ozone for 20 min. It was then immersed in 0.22% PVAM for 60 min followed by rinsing with water. Both the front side and the back side of the microcantilever were coated with PVAM. A suspension of 0.5 mg of microcrystalline cellulose powder in 25 mL of 50% NMMO was heated while stirring until a transparent brown solution was obtained. While still warm, DMSO was added to afford a cellulose solution with a final concentration of 1%. This solution was first evenly applied onto the surface of the front side of the PVAM-coated microcantilever and then allowed to sit for about 1 h. Afterwards a drop of water was added to form the cellulose film. The resulting cellulose-coated microcantilever was soaked in water for additional 4 h, during which the water was replaced every 30 min. Finally the cellulose-coated microcantilever was incubated in an oven at 80°C for 1 h to complete the surface coating.
AFM imaging (Zhao et al., 2010): To characterize the coverage, morphology, roughness, and thickness of surface coatings, AFM imaging was performed using a Nanoscope IIIa multimode scanning probe microscope from Digital Instruments, Inc. The samples were scanned in contact mode in air using silicon nitride cantilevers (MLCT) manufactured by Veeco (Camarillo, CA), with a nominal spring constant of 0.05 N/m. Images were obtained from at least three different surface areas of the sample with a typical size of 5 µm × 5 µm. The images of both height and deflection modes were captured and the surface morphology was analyzed using the image-processing software.
Microcantilever measurement: All the experiments were performed using a modified commercial Nanoscope III scanning probe microscope (Digital Instruments/Veeco, Santa Barbara, CA). The cellulose-coated microcantilever was mounted with the coating facing down in a liquid cell of the AFM with a volume of 50 μL. The solutions were introduced through injection. The cellulose-coated microcantilever was usually allowed to equilibrate in the assay buffer (25 mM sodium acetate, pH 5.5) for at least 2 h prior to any addition. The enzyme solution was prepared in the same buffer 30 min prior to use. Each assay was run against a reference to allow the subtraction of the background signal and to control for the bulk solvent effect. A desktop PC, running programs written in LabView (National Instruments, Austin, TX), was used to record the microcantilever deflection signal from the AFM via a data acquisition board with a maximum data acquisition rate of 300 kHz. The deflection measurement was monitored using a 5 mW laser diode with a wavelength of 680 nm, and a split position sensitive detector. During a measurement, 100,000 data points were taken every 30 seconds at a rate of 100 kHz. The bending of the microcantilever was obtained by simply averaging the data points.
3.2. Preparation of a cellulose-coated microcantilever
The surface of a microcantilever was coated with a model film of cellulose II having a thickness between 10 to 20 nm. It is generally agreed that the natural substrate is often too complicated to be useful for detailed characterizations of cellulases (Kontturi et al., 2006). Various cellulose model surfaces have therefore been developed in the past decade (Kontturi et al., 2006) and utilized extensively in a variety of studies including the investigation of the interaction between cellulose and cellulase. Among all the model surfaces, cellulose II has been used most often and there is much technical information available about it. In addition, the surface of cellulose II is easy to prepare and characterize. All of these make the cellulose II film an ideal model surface for the current study.
For attaching cellulose to the surface of a microcantilever, an anchoring layer of PVAM was first prepared (Figure 10A). The cellulose dissolved in a hot mixture of NMMO and DMSO was then deposited onto the top of the anchoring layer (Falt et al., 2003; Zhao et al., 2010). The cellulose coating on the microcantilever was characterized with AFM imaging and the results of the modification of the surface topography after each coating step were shown in the Figures 10B to D. A typical PVAM-coated surface is shown as a layer of small oval particles in Figure 10C. The smoothness and thickness of the coating can be adjusted by changing the coating time. The cellulose II model film on the microcantilever exhibits a cement-like characteristic with a cover of thick, short fibers (Figure 10D).
Figure 10.
Surface coating on the microcantilever (Zhao et al., 2010). (A) The coating scheme. (B) to (D) AFM images of surface coatings (5 µm × 5 µm).
3.3. Examination of morphological and structural changes of cellulose surface
The microcantilever coated with cellulose II was treated with a successive exposure of different water/salt solutions. The result of bending of the microcantilever is presented in Figure 11 (Zhao et al., 2010). In the experiment, the cellulose-coated microcantilever was allowed to equilibrate in water for 2 h to achieve a stable baseline. The bending of the microcantilever was measured based on the deflection of the microcantilever at its apex. The measurement was initiated with the injection of water and a constant bending was observed during the first 45 min. The level of bending remained virtually constant even after the injection of a solution of 0.1 M NaCl. Upon the subsequent treatment of higher concentrations of NaCl (0.5 and 1 M), a continuous rise in bending was detected at a pace of roughly 1 nm/min and a cumulative bending of more than 100 nm was observed. To compensate for bulk effects of the buffer and the salt, we measured the differential bending, termed simply ‘‘bending’’ hereafter, which is defined as the difference in deflection of the microcantilever with the cellulose coating and without the cellulose coating.
The observed bending of the microcantilever can be attributed to the change in interaction energy within the outlayer of the cellulose surface. It has been shown previously that a cellulose model film undergoes a change in internal charge density when exposed to an electrolyte solution. And the magnitude of the change in charge density depends on the concentration of the electrolyte (Ahola et al., 2008; Freudenberg et al., 2007; Tammelin et al., 2006). Such change likely alters the intermolecular repulsion among cellulose molecules, which leads to the change in interaction energy. When the cellulose is deposited onto one side of the microcantilever (Figure 10A), the change in the interaction energy in the cellulose coating can exert a differential mechanical stress between the opposite surfaces of the microcantilever, leading to the continuous bending of the microcantilever (Figure 11A). Meanwhile, the change in interaction energy also causes the change in surface morphology of the cellulose coating as indicated by the image shown in Figure 11D.
Figure 11.
The morphological changes of the cellulose coating monitored by means of the microcantilever technique (Zhao et al., 2010). (A) The bending of the microcantilever increased with the increasing NaCl concentration. (B) AFM image of the surface of the cellulose coating on the microcantilever. (C) AFM image of the cellulose surface (as shown in (B)) after being treated with 0.1 M NaCl. (D) The cellulose surface (as shown in (C)) after being treated with 1.0 M NaCl. Mean roughness: 2.59 nm with a Z range of 25 nm.
Overall, this study validates that the microcantilever technique is highly sensitive and specific in detecting real-time changes in interaction energy in the surface layer of the cellulose coating on the microcantilever. So, it is feasible of using the microcantilever technique to monitor the dynamic change in interaction energy in the surface layer of the cellulose caused by enzymatic decrystallization. The microcantilever bending also correlates well with the change in molecular structure of the surface region of the cellulose film.
3.4. Detection of the enzymatic decrystallization by cellulase on cellulose
The cellulose coating on a microcantilever was treated with the cellulase CBH I (cellobiohydrolase I, kd = 1 μM, mw = 66 kD), an exoglucanase from Trichoderma reesei in 25 mM sodium acetate buffer, pH 5.5 at 25°C. Immediately after the addition of 0.15 μM of CBH I, a bell-shaped bending curve was obtained (Figure 12A), which implies that the cellulase is capable of inducing bending of the cellulose-coated microcantilever.
Figure 12.
A) The progress curves of cellulase actions on cellulose measured by the microcantilever sensor. (B) The progress curves of CBM and cellulase actions on cellulose measured by the microcantilever sensor.
Next, the cellulose coating was treated with 0.9 μM of the carbohydrate binding module (CBM, kd = 0.6 μM, mw = 17 kD) from Clostridium cellulovorans, the domain that anchors cellulase to cellulose at 25°C. Figure 12B clearly shows that exposing the cellulose to the CBM does not generate any measurable bending in microcantilever over the course of 120 min. Over the same time frame of the previous experiment, CBH I that contains both CD and CBM domains did induce bending, as shown in Figure 12A. Notably, more weight was probably adsorbed onto the surface of the cellulose coating in the presence of the CBM than in the presence of CBH I due to the difference in protein concentration used in each experiment. This result confirmed that the change in mass (gravity) due to the initial binding of the CBM on the surface of the cellulose does not generate any bending in microcantilever, which was fully expected for a mere protein binding (physisorption) in liquid media. Thus, the cellulase-induced bending shown in Figure 12A was not caused by the initial binding between the cellulase (via the CBM of the cellulase) and the cellulose coating. This bending can therefore be attributed to the result of the cellulase actions that occurred after its initial binding on cellulose. Such actions may include enzymatic decrystallization and/or subsequent hydrolytic cleavage (Figure 6). After the addition of the CBM, the subsequent addition of CBH I (cellulase) did not generate any bending until approximately 6 h later (Figure 12B). This result verified that the CBM was indeed bound to the surface of the cellulose and the cellulose-bound CBM prevented the subsequent binding of CBH I to the cellulose. We believe that the bending in microcantilever beginning after 500 min was due to a slow displacement of the cellulose-bound CBM by CBH I.
4. Conclusion
These studies have demonstrated that a nanomechanical sensor in microcantilever is capable of detecting the interaction between cellulase and cellulose in real time. More specifically, this technique can be used to probe the dynamic process of the enzymatic decrystallization of cellulose by cellulase. The bending of the microcantilever is likely a result of the change in interaction energy within the cellulose caused by the interaction between cellulase and cellulose (e.g., enzymatic decrystallization), not by the adsorption of cellulase onto cellulose. The innovative microcantilever sensor approach will be used to determine the kinetics of the enzymatic decrystallization by cellulase.
Acknowledgement
This work was supported in part by a grant from the National Science Foundation (NSF) CBET-0843921, Drexel University Career Development award, and subcontract XCO-4-33099-01 from the National Renewable Energy Laboratory funded by the U.S. DOE Office of the Biomass Program.
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Introduction",level:"1"},{id:"sec_1_2",title:"1.1. Cellulose and cellulose biomass",level:"2"},{id:"sec_2_2",title:"1.2. Degradation of cellulose in biomass conversion",level:"2"},{id:"sec_3_2",title:"1.3. Cellulase and enzymatic hydrolysis of cellulose",level:"2"},{id:"sec_4_2",title:"1.4. Knowledge gap",level:"2"},{id:"sec_6",title:"2. Innovative approach and microcantilever",level:"1"},{id:"sec_6_2",title:"2.1. Existing technologies and their technical limitations",level:"2"},{id:"sec_7_2",title:"2.2. Microcantilever and its applications",level:"2"},{id:"sec_8_2",title:"2.3. Microcantilever in cellulose study",level:"2"},{id:"sec_10",title:"3. Investigation of the interaction between cellulase and cellulose",level:"1"},{id:"sec_10_2",title:"3.1. Materials and methods",level:"2"},{id:"sec_11_2",title:"3.2. Preparation of a cellulose-coated microcantilever",level:"2"},{id:"sec_12_2",title:"3.3. Examination of morphological and structural changes of cellulose surface",level:"2"},{id:"sec_13_2",title:"3.4. Detection of the enzymatic decrystallization by cellulase on cellulose",level:"2"},{id:"sec_15",title:"4. Conclusion",level:"1"},{id:"sec_16",title:"Acknowledgement",level:"1"}],chapterReferences:[{id:"B1",body:'AholaS.SalmiJ.JohanssonL. S.LaineJ.ÖsterbergM.2008Model films from native cellulose nanofibrils. Preparation, swelling, and surface interactions. Biomacromolecules,\n\t\t\t\t\t94127312821525-7797'},{id:"B2",body:'AholaS.TuronX.ÖsterbergM.LaineJ.RojasO. J.2008Enzymatic hydrolysis of native cellulose nanofibrils and other cellulose model films: Effect of surface structure. Langmuir,\n\t\t\t\t\t242011592115990743-7463'},{id:"B3",body:'BergerR.DelamarcheE.LangH. P.GerberC.GimzewskiJ. K.MeyerE.GuntherodtH.J.1997Surface stress in the self-assembly of alkanethiols on gold. Science (Washington, D. C.),\n\t\t\t\t\t2765321202120240036-8075'},{id:"B4",body:'BorastonA. B.BolamD. 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Drexel University, Department of Chemistry, Philadelphia, USA
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1. Introduction
Neglected tropical diseases (NTDs) include a collection of chronic, disabling, and physically disfiguring infectious diseases that usually affect dwellers of poor rural populations in tropical and sub-tropical countries of the world [1]. Apart from their negative impact on the health of victims, NTDs exert an immense socio-economic burden on the society as a result of the social stigma and physical disabilities associated with them. These interrelated negative outcomes perpetuate a cycle of poverty and unproductivity resulting in a consistent decline in economic growth [2]. As a major element of the Millennium Development Goals (MDGs), much effort is being put in for the elimination of the NTDs [3].
Among the NTDs, helminth infections especially soil-transmitted helminthiasis (STHs) and schistosomiasis are among the most prevalent afflictions of humans [4]. About 2 billion people are estimated to suffer from helminth infections worldwide, out of whom 300 million suffer from severe morbidity [5]. The negative impact of helminth infections on human growth and development (including cognitive development in childhood and nutritional status), pregnancy and work performance cannot be overemphasized. Though considered as acute health problems in some developed parts of the world, chronic parasitic infections are common and recurrent in poor communities and usually result in long-lasting complications making them a significant health threat to the populations who are continuously at risk for infection [6].
Over the years, many highly effective chemotherapeutic agents have been developed for treating helminth infections. Unfortunately in the setting of rural poverty where these diseases are mostly prevalent, access to healthcare facilities and the cost of medications are a challenge [7, 8]. Additionally, environmental factors and unavoidable domestic or occupational exposures, strongly favor the process of re-infection even after a successful therapy [9, 10]. Given that these infections also require lengthy treatment regimens with related costs which cannot be afforded by the affected victims, many patients seek for alternative treatment options especially the use of herbal medicines which are readily available and less expensive [9, 11].
Herbal extracts have been used in traditional medicines since ancient times for the effective treatment of human diseases [12]. Ethnobotanical studies in various regions of the world have documented medicinal plants used for the treatment of various parasitic infections. Scientific investigations of selected plants have also revealed remarkable activity of medicinal plants against specific human parasites [13, 14]. In Ghana, numerous medicinal plants play an important role in the healthcare system of rural communities. The Ghanaian flora provides a ready source for new therapeutic interventions for the local population [15, 16, 17]. This chapter provides a review with special focus on medicinal plants collected from Ghana with anthelmintic and anti-schistosomal activity.
1.1 Soil transmitted helminthiasis (STH)-the disease burden and current chemotherapy
Soil transmitted helminth (STH) infections are a group of infections which are acquired by the ingestion of, or contact with, soil containing infectious worm eggs or larvae [18]. STHs have been reported as the most common parasitic infections encountered in humans with an estimation of more than 1 billion people infected with at least one or more helminth parasites. They constitute an important global health challenge in resource deprived parts of the world and are prevalent in areas of poor sanitary conditions [19].
The main species of clinical importance are the intestinal roundworm (Ascaris lumbricoides), the whipworm (Trichuris trichiura) and the hookworms (Necator americanus and Ancylostoma duodenale) [18]. Common symptoms of intestinal helminthiasis include abdominal pains, nausea, itching and diarrhea and in severe cases, anemia, pneumonia, eosinophilia and malnutrition. School-aged children and preschool children are the most vulnerable group who harbor the greatest numbers of intestinal worms. As a result, they experience growth stunting and diminished physical fitness as well as impaired memory and cognition [20]. Although helminth infections are not known to be lethal as compared to other infections, they are recurrent among poor people and pose an enormous impact on the socio-economic status of the society affected [21].
Anthelmintics are a group of antiparasitic drugs that expel worms and other internal parasites out of the body by either stunting or killing them. For the treatment of STHs, the benzimidazoles specifically albendazole and mebendazole are the current treatment drugs of choice [19]. The main challenge with these anthelminthics is the development of resistance due to the intensive use of drugs in both human and live-stock [22]. With few new drugs evolving against helminth infections over the years, the fight against these parasites could become a losing battle, thus the need to search for new alternatives.
1.2 Schistosomiasis—the disease burden and current chemotherapy
Schistosomiasis, widely known as bilharzia, is caused by infection with blood flukes of the genus Schistosoma which is transmitted through contact with infected fresh-water snail vectors. Schistosomiasis is reported to be the 2nd leading endemic parasitic disease in the world after malaria. The disease affects more than 240 million people in tropical and subtropical areas with about 90% cases reported from sub Saharan Africa [23, 24].
Five species of the schistosome parasite namely: Schistosoma mansoni, Schistosoma haematobium, Schisosoma japonicum, Schistosoma mekongi, and Schistosoma intercalatum usually affect humans [25]. In sub-Saharan Africa the main burden of disease is usually attributed to S. mansoni and S. haematobium which cause intestinal and urinary schistosomiasis respectively [10]. The infection is mainly characterized by painful bloody urination in urinary schistosomiasis or blood stained diarrhea in intestinal schistosomiasis. Long term effects include liver fibrosis, renal failure, cancer of the bladder, infertility and increased risk of contracting HIV. In children, schistosomiasis results in malnutrition, growth retardation, cognitive defects and chronic anemia [6, 26].
For the eradication of schistosomiasis, control programmes have been based on preventive chemotherapy. The WHO endorsed and advocated for mass drug administration (MDA) especially among school children utilizing a single oral dose of 40 mg/kg praziquantel [27]. Unfortunately, the unavailability of the drugs due to cost, poor drug coverage, inequity of access to chemotherapy and non-compliance to therapy due to adverse side effects have impeded the progress of this approach [7, 28]. The expansion of preventive chemotherapy has also raised concerns about the potential development of resistance to praziquantel (PZQ) which remains the only commercially readily available drug for the control of schistosomiasis [29]. Some studies have reported low cure rates of PZQ attributing this to possible mutation of the schistosome parasite as well as inactivity of PZQ against early stages of the worms [30, 31]. It is thus not a satisfactory situation to have only one single effective treatment. Ideally, other anti-schistosome drugs should be developed so that the classical strategy of avoiding development of resistance could be followed.
1.3 Methods used in this review for identifying medicinal plants with anthelminthic and anti-schistosomal activities
Reported anthelmintic and anti-schistosomal activities of medicinal plants collected from various parts of Ghana were obtained from electronic databases including PubMed, SciFinder and Google Scholar. The inclusion criteria were that: (i) plants should be used in Ghanaian traditional medicine for treatment of worm infestations or expulsion of worms and schistosomiasis (urinary and intestinal) or other condition characterized by the symptoms of the above diseases (ii) plant should have been investigated for anthelmintic or anti-schistosomal (cercarididal) activity using one or more validated in vitro or in vivo models (iii) the right botanical names, plant parts used, types of extracts prepared, active constituents and mechanisms of action if investigated were mentioned. Consideration was also given to plants with significant activity differences with reference to control groups.
2. Plants with anthelminthic activity identified from Ghana
The anthelmintic activity of plant extracts was mostly studied by evaluating their effect on worms after direct exposure for a period of time. Earthworms including Pheretima posthuma, Lumbricus terrestris, Eudrilus eugeniae and Caenorhabditis elegans were employed as target organisms due to their anatomical and physiological similarity to the human intestinal round worm, ease of availability, adaptability to laboratory conditions and ease of handling.
Alchornea cordifolia, commonly called the Christmas bush is a straggling, laxly branched evergreen dioecious shrub growing up to about 8 m tall. It is locally known as ‘agyama’ in the Ghanaian Akan language and an essential medicinal plant in traditional medicine. Various parts of the plant are used to treat jaundice, diarrhea, rheumatic pains, malaria, fever, wounds, colds, asthma, amoebic dysentery and worm infections. Other literatures report its use in the treatment of urinary and gastrointestinal infections, leprosy, yaws, filariasis as an antidote to snake venom [32].
The anthelminthic potency of the petroleum ether, chloroform and methanol extracts of A. cordifolia leaves were investigated by evaluating its effect on the gross motility and mortality of earthworms (Pheretima posthuma). The extracts displayed significant (p < 0.001) concentration-dependent anthelminthic activity at concentration range of 0.75 to 12.00 mg/mL. At the highest concentration, worm paralysis was effectuated between 10 and 26 mins whiles death occurred between 57 to 93 min. The effect of the extracts in reducing the paralysis and death times of the worms was significantly higher than the effect on albendazole-treated worms [33].
2.2 Alstonei boonei De Wild (Apocynaceae)
Alstonia boonei is an indigenous African tree mostly distributed in the evergreen rain forest of tropical West Africa. In Ghana it is locally called ‘Nyame dua’ meaning God’s tree in the Akan language. In the western coastal regions of Africa, this plant is well known for its extensive use in traditional medicine for treating rheumatism, general body pains, worm infestation and diabetes. A cold infusion of the fresh or dried bark is used as a vermifuge to expel intestinal worms and other intestinal parasites in children [34].
The methanol extracts (50–150 mg/mL) of the stem bark and roots of A. boonei were investigated in vitro for anthelmintic effects against the adult Indian earthworm, Pheretima posthuma by direct exposure of worms to the extracts. The stem bark extract exhibited a concentration dependent anthelmintic activity causing paralysis of worms within 15–55 mins and death within approximately 100 mins which was significant (p < 0.01) compared to the untreated group. The stem bark extract had a better anthelmintic effect than the root bark [35].
In another study, the aqueous and ethanolic stem bark extracts (50–200 mg/mL) of A. boonei demonstrated significant anthelmintic activity against Lubricus terretris. While worms in the untreated group saw no paralysis or death after 120 mins of exposure, the extract-treated worms were paralyzed within 8–16 minutes of exposure and died within approximately 21–27 minutes of exposure [36].
2.3 Azadirachta indica A. Juss. (Meliaceae)
Azadirachta indica, commonly known as neem, is a fast-growing and long lived evergreen tree which grows up to about 15 m tall with long, spreading branches that form a dense, large rounded crown. The plant is a multipurpose medicinal plant which also provides food and timber and is widely distributed in several regions of Asia and Africa. It is well known for its insecticidal and insect-repelling property. Various parts of the plants are reported to be used for the treatment of many ailments in traditional medicine including malaria, fever, upper respiratory tract infections, wound healing, sexually transmitted infections and skin diseases [37].
The anthelmintic activity of the ethanolic extract of A. indica seeds was investigated in vivo using albino rats (Rattus norvegicus) infected with helminth species including: Hymenolepsis diminuta, Enterbius vermicularis and hookworm. The rats were treated with the alcoholic extracts (20–60%) over a 3-week period and fecal samples were examined for eggs. The extract treated groups showed declining levels of egg count by the 3rd week and complete elimination of worms by the end of 21 days when treated with 40–60% of neem seed extract. Weight loss and death were however recorded at 60% concentration of extract raising some concern about the toxicity of the seed extract [38].
2.4 Carica papaya Linn. (Caricaceae)
The pawpaw tree is well known for its nutritional and medicinal values. The leaf decoction is used as a galactogogue and in the treatment of tonsillitis, ulcerative stomatitis, hemorrhoids, asthma, urinary tract infections, as poultice for sores and gingivitis and in the treatment of helminth infections. The roots are used as antidote to various poisons. The fruits are used to treat indigestion, chronic diarrhea, ringworm infections, bleeding piles, and amoebic dysentery [39]. Almost all parts of the plant are documented to be used for managing helminth infections. In Ghana, 74% traditional healers used this plant for treating helminth infections [40].
In a comparative assessment of the anthelminthic activity of various parts of the plant, the hydroethanolic extracts of the leaves, stem bark, and seeds of Carica papaya were tested against P. posthuma as the target organism. The results indicated that all crude extracts prepared were more effective than albendazole in reducing paralysis (p < 0.0001) and death times (p < 0.0001) of worms. Extracts from the seeds at 2.5 mg/mL were the most effective causing worm paralysis and death at 9.26 ± 0.03 and 20.12 ± 0.01 mins respectively. This was more potent than the standard anthelmintic albendazole at the same concentration which gave paralysis and death times of 19.45 ± 0.57 and 31.43 ± 0.28 mins respectively [41].
Ethnopharmacological reports from parts of Ghana revealed the extensive use of the leaves of Combretum mucronatum for treatment of human and livestock helminth infection [40]. The leaves from this plant species is monographed in the Ghana Herbal Pharmacopeia for the treatment of infections with worms [42].
In a previous study, the alcoholic leaf extract of C. mucronatum was assayed in vitro for anthelmintic activity against free-living nematode, Caenorhabditis elegansusing levamisole as a positive control. The extract demonstrated anthelmintic activity with a worm survival rate of 89.2% at 0.1 mg/mL and 58.1% at 1 mg/mL [40].
In another study, fractions and purified compounds from C. mucronatum leaves were tested in vitro for their anthelmintic activity against C. elegans. Unsubstituted oligomeric proanthocyanidins (PACs) mainly composed of epicatechin units were identified as the active compounds of the hydroethanolic leaf extracts. The compounds demonstrated a dose-dependent anthelmintic activity ranging from 1 to 1000 mM and activity was found to increase with increasing molecular size. The anthelmintic activity was suggested to be by interaction of the PACs with some unidentified proteins of the target organism [43]. Further, the mechanism of anthelmintic activity of the PACs was determined by transcriptome analysis. PACs were found to interact with proteins within the worm’s intestinal membrane as well as enzymes and peptides to elicit anthelmintic effects [44]. Another proposed mechanism was interaction of the tannins with cuticular proteins, particularly proline-rich collagen in the worm cuticle [45].
2.6 Cyperus difformis Linn. (Cyperaceae)
Cyperus difformis is an annual plant with smooth leaves and fibrous reddish roots. It is native to the subtropical and tropical areas but also distributed and widespread in South Europe, Asia and Americas. It is regarded as one of the world’s commonest weeds found growing in wet swampy soils among rice plantation. It is very common in Ghana and traditionally used for the management of scorpion bites and malaria [46].
The anthelmintic and helminth resistance modifying activities of methanol extract of C. difformis was investigated against the adult Indian worm, P. posthuma using albendazole, mebendazole and levamisole as reference anthelmintics. The extract exhibited a concentration dependent anthelmintic activity against P. posthuma with significant (p < 0.001) paralysis and death times of 66.67 ± 1.8 and 140.7 ± 2.3 mins respectively at extract concentration of 20 mg/mL [47].
Further the extract at 1, 2 and 5 mg/mL significantly potentiated the activity of albendazole, mebendazole and levamisole against the test organism. In the presence of 2 mg/mL of the extract the paralysis and death times of albendazole (8 mg/mL) against P. posthuma were reduced from 41.33 ± 0.33 and 106.67 ± 0.88 min respectively to 33.33 ± 0.88 and 85.67 ± 1.2 min, respectively. Similar results were obtained for mebendazole and levamisole [47].
2.7 Garcinia cola Heckel (Guttiferae)
Garcinia cola also known as “bitter cola” is a valuable medicinal plant in African traditional medicine widely accepted for its numerous medicinal properties. It is usually called the wonder plant due to the usefulness of every part of the plant. The seeds are chewed as an aphrodisiac and used to cure cough, dysentery and upper respiratory tract infections [48, 49]. The latex from the stem is used against sexually transmitted infections and applied externally to heal wounds. The sap is used in curing parasitic diseases. Chewing sticks produced from the stems are used as masticatory for nervous alertness and for treating coughs and throat infections [50].
In a previous study, the methanol stem bark extract of G. cola (1—50 mg/mL) demonstrated a concentration dependent anthelmintic activity, decreasing paralytic and death times of P. posthuma with increasing extract concentrations. At 50 mg/mL, the extract had a paralytic time of 39.29 ± 0.12 min and death time of 54.29 ± 0.01 [51].
2.8 Morinda lucida Benth. (Rubiaceae)
Morinda lucida is an evergreen shrub growing from about 3 m to 18 m tall. It has a dense crown with slim, crooked branches. The plant is occasionally grown in home gardens. It is locally called ‘konkroma’ in the Ghanaian Akan language. It is a multipurpose species yielding dyes, timber, fuel and traditional medicines. The plant is reported to be used in managing diabetes, hypertension, dysentery, stomach-ache, leprosy and gonorrhea. Traditionally, the stems are used to treat piles while the leaves are used to treat fever. A decoction of the bark or leaf is used in the treatment of jaundice and against itch and ringworm. The leaves and twigs are sold as a medicinal tonic for young children [52].
In a previous study, the methanol stem bark extract of M. lucida (10–50 mg/mL) reduced worm motility and caused death of the adult Indian earth worm, P. posthuma with a paralytic time of 18.17 ± 0.03 min and death time of 24.34 ± 0.21 min at 50 mg/mL [51].
2.9 Moringa oleifera Lam. (Moringaceae)
Moringa oleifera is a fast growing perennial evergreen or deciduous plant which grows up to a maximum height of 7–12 m. It has an open crown of drooping fragile branches bearing feathery foliage of opposite pinnate leaves, a crooked bole and dark gray stem bark. M. oleifera has been naturalized in many tropical and subtropical regions of the world including Africa, Arabia, South Asia, South America and India where it is commonly referred to as horseradish tree and drumstick tree [53]. Various parts of the plant are used in traditional medicine to treat various diseases including skin infections, anemia, asthma, bronchitis, catarrh, chest congestion, cholera, diabetes, hypertension and many other illnesses [54].
The foliage of M. oleifera was investigated for anthelmintic activity in wild caught Achatina achatina Linnaeus (edible snails). After feeding the snails on the foliage for 10 weeks, the proportion of parasitic infection in the treated group was estimated using dissecting and microscopic techniques. At the end of the treatment period, 96% of snails in the untreated group were observed to have their kidneys infected with roundworms as opposed to 24% of snails in the treated group. The percentage prevalence of parasitic infection in the treated and control groups was significantly different (p < 0.0001). Similar results were recorded for the infection of the lungs highlighting the anthelmintic value of M. oleifera in the control of worm infection in edible snails [55].
2.10 Ocimum basilicum Linn (Lamiaceae)
Ocimum basilicum is a tender-growing aromatic annual herb indigenous to West Africa and India. It is commonly called basil or sweet basil and locally known in the Ghanaian Akan language as ‘Nunum’. The herb is ubiquitously known for its therapeutic potentials in African folk medicine. In Ghana, basil is used in its fresh form as spice and flavoring in soups and sauces due to its strong spicy aroma. The whole plant is used to treat worm infestation, inflammation, pain, diarrhea, gastrointestinal infections and eye-related diseases [56].
In vitro anthelmintic activity of the hexane and ethanolic extracts of the fruits of O. basilicum was investigated against Eudrilus eugeniae. At a concentration range of 0.25–5 mg/mL, the extracts displayed a concentration dependent anthelmintic activity which was observed to be significantly (p < 0.001) higher compared to mebendazole-treated worms. At 5 mg/mL, paralysis was observed at 11.85 ± 0.71, 27.90 ± 0.42 and 94.04 ± 2.57 mins for the ethanol extract, hexane extracts and mebendazole-treat worms respectively. Similarly, death of worms was recorded at 24.74 ± 0.42, 85.18 ± 0.07 and 522.77 ± 1.53 mins respectively for the ethanol extract, hexane extracts and mebendazole [57].
2.11 Paullinia pinnata L. (Euphorbiaceaae)
Paullinia pinnata is a woody climber growing in tropical regions worldwide. In Ghana, it is locally called ‘toantini’ in the Akan language. Preparations from the whole plant is used to treat dysentery. The mashed roots are used as poultice to heal chronic wounds and to treat leprosy. The root decoction is also used to cure coughs, pneumonia, gonorrhea, fractures, bacterial infections and abscesses. It is popularly known for its aphrodisiac property and used to treat erectyle dysfunction [58]. In addition, extracts of leaves and roots have been described for the treatment of helminth infestations particularly ancylostomiasis [40].
The hydroethanolic extract of the roots of P. pinnata was investigated in an in vitro mortality assay against the free-living nematode Caenorhabditis elegans as well as the larval stages of the parasitic helminths: Ancylostoma caninum, Haemonchus contortus, Toxocara cati and Trichuris vulpis. From the assay, the extract showed lethal activity against T. cati (LC50 = 112 μg/mL), T. vulpis (LC50 = 17 μg/mL), and C. elegans (LC50 = 2.5 of mg/mL), but not against A. caninum. Additionally, the effects of the extract on egg hatching and larval migration of the sheep parasite, Haemonchus contortus were investigated in vitro, but no inhibitory activity was observed [59].
In another study, the 70% aqueous acetone extract, solvent fractions and isolated compounds from the roots of P. pinnata were investigated for anthelmintic against C. elegans. From the results, the ethyl acetate fraction showed the highest anthelmintic effects with an LC50 of 1.1 mg/mL followed by the crude extract (LC50 = 1.9 mg/mL) and the aqueous fraction (LC50 = 2.9 mg/mL). Oligomeric proanthocyanidins were identified as the main active compounds. A mortality rate of at least 70% was observed for all proanthocyanidin containing fractions at 1 mg/mL [60].
2.12 Plumbago zeylanica Linn. (Plumbaginaceae)
Plumbago zeylanica is a perennial shrub with semi woody stems and numerous branches. It is a valuable medicinal plant widely used in Africa and Asia for the treatments of common ailments like hemorrhoids, diarrhea, leprosy, arthritic pains, toothache and as aphrodisiac and wound healing [61].
In a previous, observations were made for the time taken for different solvent extracts of the leaves of P. zeylanicum at concentrations of 300, 100 and 30 mg/mL to paralyze and kill Pheretima posthuma. The ethyl acetate extracts showed significant (p < 0.0001) concentration-dependent anthelminthic activity with the highest effect at 300 mg/mL causing paralysis at 7.39 ± 0.94 min and death at 11.81 ± 1.10 min. The methanol extract at 300 mg/mL demonstrated slightly lower anthelmintic effect with paralysis at 17.23 ± 1.68 min and death at 21.83 ± 2.60 min [62].
2.13 Rauwolfia vomitoria Afzel. (Apocynaceae)
Rauwolfia vomitoria commonly called the African Snakeroot or African Serpent root is a small tree or shrub that grows up to about 20 m tall in tropical Africa. It is locally called ‘kakapenpen’ in the Asante dialect of Ghana. In traditional medicine, the plant is recorded to be used in the treatment of convulsions, malaria fever, insomnia, arthritis, pain, high blood pressure, diabetes, stomach problems and as an emetic. The leaves are applied topically for skin infections, swelling and snake bites. It is placed in the rectum for the expulsion of worms and for dysmenorrhea [46].
The leaves and stem bark of R. vomitoria demonstrated significant (p < 0.001) anthelmintic activity against the Indian adult earthworm P. posthuma. The methanol extracts of the stem bark caused paralysis of worms at 11.17 ± 0.088 min and reduced the death time to 21.67 ± 0.733 similar to the effect of albendazole at 10 mg/mL which had a worm death time of 21.03 ± 0.258 min [63].
Sclerocarya birrea is a dioecious small to medium sized tree growing up to about 20 m high and 1.2 m in diameter. The plant is distributed from Gambia, Ghana and Nigeria in West Africa, across Cameroon in Central Africa, to Ethiopia and Sudan in East Africa and to South Africa, usually found growing in open farm lands and natural vegetation [64]. The stem-bark, roots and leaves are used to treat several ailments including diabetes mellitus, diarrhea, dysentery, proctitis, ulcers, inflammation, arthritis, hypertension, skin diseases, and malaria [65].
The anthelmintic activity of the aqueous and ethanolic extracts of the roots of S. birrea were evaluated against earth worms. The extracts displayed significant (p < 0.001) concentration-dependent anthelmintic activity at 12.00 to 0.1875 mg/mL. The observed effect was higher compared to albendazole-treated worms [66].
2.15 Vernonia amygdalina Del. (Asteraceae)
Vernonia amygdalina is tropical shrub which grows up to about 3 m high. The plant is distributed throughout tropical Africa and has been domesticated in some parts of West Africa including Nigeria and Ghana where it is commonly called the bitter leaf. It is a highly valuable vegetable in West and Central Africa which is consumed as part of various dishes. In traditional medicine the leaf decoction is used to treat fever, malaria, diarrhea, dysentery, hepatitis and cough, as a laxative and as a fertility inducer [67]. The root extracts are also used for treating malaria and gastrointestinal disorders. One of the most common medicinal uses of V. amygdalina is as a treatment against intestinal worms including nematode infections [68]. The use of the leave decoctions against intestinal worms, especially pinworms was confirmed in an ethnobotanical survey in the Ashanti Region of Ghana [40].
In a previous study, the anthelmintic activity of V. amygdalina leaves were investigated against Lumbricus terrestris (earth worm). Unlike the negative control groups which remained alive and active after 6 hours of exposure to normal saline, all worms treated with the aqueous and ethanol leaf extracts (50–200 mg/mL) of V. amygdalina were noted to be paralyzed within 4.05 ± 1.06 to 59.94 ± 8.25 and 3.56 ± 0.37 to 33.18 ± 12.4 mins respectively (p < 0.0001). The effect was concentration dependent [36].
In another study, the stem bark extracts (ethanol and chloroform extracts) of V. amygdalina were observed to produce a synergistic anthelmintic effect when combined with the seeds of Carica papaya [69].
2.16 Voacanga Africana Stapf. (Apocynaceae)
Voacanga africana is a small tree or shrub, reaching up to 6 m tall in height with a low widely spreading crown. In Ghana, it is locally known as ‘ofruma’ in the Asante language. Various plant parts are used medicinally throughout its distribution area [70]. The leaf decoction is used to treat dysentery, diarrhea, cutaneous and sub-cutaneous parasitic infections, leprosy, oedema, gout, paralysis and convulsion. The stem bark or roots decoctions are used as wound healing agents and used to treat boils, malaria, sexually transmitted diseases like gonorrhea, and skin diseases such as eczema and scabies. They are also taken to treat cardiovascular diseases and rheumatoid arthritis. The leaf latex is put in the teeth to treat dental caries or dripped in the eye to cure ophthalmia [46].
The methanol extracts of the leaves and stem bark V. africana were evaluated for in vitro anthelmintic activity by determining the effects of the extracts on the paralytic and death time of P. posthuma using albendazole as reference. The bark extract (20–50 mg/mL) demonstrated a significant (p < 0.001) concentration dependent anthelmintic effect by decreasing the paralysis and death times of worms. At 50 mg/mL, the stem bark extract caused worm paralysis within 7.03 ± 0.491 min and death at 14.77 ± 0.117 min [63].
2.17 Xylopia aethiopica (Dunal) A. Rich. (Apocynaceae)
Xylopia aethiopica is popularly known as the African pepper and locally called ‘Hwentia’ in the Ghanaian Akan language meaning slender nose, referring to the shape of the fruit. X. aethiopica is known for its numerous medicinal properties in African traditional medicine. The bark infusion is used in the treatment of asthma, stomach aches and rheumatism. The bark powder is also applied topically on ulcerous wounds and used locally for the treatment of cancer and stomach ulcers. The root powder is known to relief toothache and pyorrhea [71].
The ethanolic extract of the dried fruits and leaves (300–300 mg/mL) were investigated for anthelmintic activity against earth worms. The anthelmintic activity of the fruit extract was more potent that the leaf extract. Both extracts demonstrated a concentration dependent activity with the fruit extract demonstrating significant paralytic and death times (p < 0.001) at 100 and 300 mg/mL [72].
3. Plants with cercaricidal and anti-schistosomal activities identified from Ghana
Anthelmintic activity against Pheretima posthuma [33]
Alstonia boonei
Apocynaceae
Alstonia
Roots, stem bark
Anthelmintic activity against Pheretima posthuma, Lubricus terretris [35, 36]
Azadirachta indica
Meliaceae
Neem
Seeds Leaves
Anthelmintic activity against Hymenolepsis diminuta, Enterbius vermicularis and hookworm [38] Cercaricidal and adulticidal activity against Schistosoma mansoni [73]
Carica papaya
Caricaceae
Pawpaw
Leaves, stem bark, seeds
Anthelmintic activity against Pheretima posthuma [41]
Combretum mucronatum
Combretaceae
—
Leaves
Anthelmintic activity against Caenorhabditis elegans [40, 43, 45]
Cyperus difformis
Cyperaceae
—
Whole plant
Anthelmintic activity against Pheretima posthuma [47]
Dichapetalum crassifolium
Dichapeltaceae
—
Stems, roots
Anti-schistosomal activity against eggs obtained from clinical isolates of Schistosoma haematobium [75]
Erythrophloem ivorense
Euphorbiaceae
—
Leaves, stem bark Roots
Cercaricidal activity against post-infective larvae (schistosomule) and adult parasite of Schistosoma mansoni [77] Cercaricidal activity against freshly shed cercariae from Schistosoma haematobium [78]
Garcinia cola
Gutifferae
Bitter kola
Stem bark
Anthelmintic activity against Pheretima posthuma [51]
Holarrhena floribunda
Apocynaceae
—
Stem bark
Cercariae from Schistosoma haematobium
Morinda lucida
Rubiaceae
—
Stem bark
Anthelmintic activity against Pheretima posthuma [51] Cercaricidal activity against Schistosoma mansoni cercariae Adulticidal effect against S. mansoni adult worms [73]
Moringa oleifera
Moringaceae
Moringa
Foliage
Anthelmintic activity against round worms in wild edible snails (Achatina achatina) [55]
Nauclea latifolia
Rubiaceae
African peach
Stem bark
Cercaricidal activity against Schistosoma mansoni cercariae Adulticidal effect against S. mansoni adult worms [73]
Ocimum basilicum
Lamiaceae
Basil
Fruits
Anthelmintic activity against Eudrilus eugeniae [57]
Paullinia pinnata
Euphorbiaceae
—
Roots
Anthelmintic activity against the free-living nematode Caenorhabditis elegans and larval stages of the parasitic helminths: Ancylostoma caninum, Haemonchus contortus, Toxocara cati and Trichuris vulpis [60]
Plumbago zeylanica
Plumbaginaceae
—
Leaves
Anthelmintic activity against Pheretima posthuma [62]
Phyllanthus amarus
Euphorbiaceae
—
Leaves
Cercaricidal activity against Schistosoma mansoni cercariae
Rauwolfia vomitoria
Apocynaceae
Snakeroot
Leaves, roots Roots, stem bark
Anthelmintic activity against Pheretima posthuma [63] Cercaricidal activity against Schistosoma mansoni cercariae Adulticidal effect against S. mansoni adult worms [73]
Sclerocarya birrea
Anacardiaceae
Roots
Anthelmintic activity against Lumbricus terrestris [66]
Vernonia amygdalina
Asteraceae
Bitter leaf
Leaves, stem bark Leaves
Anthelmintic activity against Lumbricus terrestris [36] Cercaricidal activity against Schistosoma mansoni cercariae Adulticidal effect against S. mansoni adult worms [73]
Voacanga africana
Apocynaceae
—
Leaf, stem bark
Anthelmintic activity against Pheretima posthuma [63]
Xylopia aethiopica
Apocynaceae
African black pepper
Fruits, leaves
Anthelmintic activity against Lumbricus terrestris [72]
Table 1.
Medicinal plants from Ghana with anthelmintic and anti-schistosomal activity.
3.1 Azadirachta indica A. Juss (Meliaceae)
[Refer to Section 2.3 for plant description].
The methanol leaf extract of A. indica was investigated for cercaricidal activity against freshly shed cercariae of Schistosoma mansoni. At a concentration range of 31.2–1000 μg/mL, the leaf extract caused a steady increase in the number of dead cercariae during an observation period of 15 to 180 mins. At 60 mins, 250 μg/mL of extract was found to cause 100% mortality of cercariae. At the end of the observation period (180 mins) the leaf extract recorded an IC50 of 27.62 μg/mL which was about four times lower than the effect of the positive control Balanites aegyptiaca (IC50 of 5.95 μg/mL) [73].
The effect of A. indica leaf extract on the viability of adult schistosome worms (i.e. adulticidal effect) was further investigated. At the end of 120 h, the extract at 62.5–1000 μg/mL was found to be lethal to the incopula adult worms. Further in an in vivo study, the ability of the leaf extract (500 mg/kg p.o.) to reduce the worm recovery and worm burden in S. mansoni infected mice was investigated. After a two-week period of treatment, the mean number of worms recovered from A. indica-treated mice was 19.80 ± 8.194 which was significantly lesser than that of the untreated mice (40.20 ± 3.072) [73].
The effect of the extract on the weight of spleen and liver of infected mice were all significantly lesser in the A. indica-treated group than that of the untreated group (p < 0.05). Organ histology also revealed only few granulomas which were smaller in diameter in the treatment groups whereas those in the untreated were severe (p < 0.05). Treated cercariae-infected mice group also had relatively less severe inflammatory cell infiltration compared with untreated group [73].
Dichapetalum crassifolium is a scandent shrub, about 1.5 m tall usually found growing in the rain forest, shady places, primitive woods and rocky areas of African countries including Ghana, Angola, Benin, Cameroon, Ivory Coast, Liberia, Nigeria, Sierra Leone, Tanzania, Togo and Zambia [74].
Crude extracts (pet-ether, ethyl acetate and methanol) and isolated triterpenoids from the stems and roots of D. crassifolium were investigated for anti-schistosomal activity against eggs obtained from clinical isolates of Schistosoma haematobium using the 96-well plate-egg hatch assay [75].
For the stem extracts, the ovicidal potency was in the following order petroleum ether (IC50 = 443.70) > EtOAc (IC50 = 638.00) > MeOH (IC50 = 893.70 μg/mL). The IC50 values for the root extracts were 248.60, 546.40, and 566.30 μg/mL respectively for the EtOAc, pet-ether and MeOH extracts.
The isolated compounds (Friedelan-3-one, β-Sitosterol/stigmasterol, Dichapetalin M and Dichapetalin A) showed higher ovicidal activity than the extracts though activities for both extracts and compounds were lower compared to the standard drug, praziquantel. The highest ovicidal potency was exhibited by β-sitosterol/stigmasterol mixture with an IC50 of 177.90 μg/mL which was about 11 times less potent than praziquantel (15.47 ± 0.06 μg/mL). The next highest was dichapetalin A (151.10 μg/mL) whiles friedelan-3-one showed the least potency with IC50 of 378.10 μg/mL. From the root extract, Dichapetalin M showed ovicidal effect with IC50 of 191.00 μg/mL [75].
3.3 Erythrophleum ivorense Afzel (Euphorbiaceae)
E. ivorense is a large tree which grows to about 40 m tall, with a cylindrical bole, sometimes fluted at the base. It is widely distributed in the evergreen primary and secondary forests of tropical Africa where it is commonly called by names like ‘forest ordeal tree’, ‘red water tree’ and ‘sasswood tree’. Among the Akan tribe in Ghana, it is known as ‘potrodum’. The stem-bark and roots are usually employed in the treatment of epilepsy, emesis, pain, oedema, constipation and worm infestations [76].
The cercaricidal activity of the leaf and stem bark extracts of E. ivorense was investigated against two developmental stages of Schistosoma mansoni namely: the post-infective larvae (schistosomule) and the adult parasite. Various solvent fractions were assayed against the schitosomules at a concentration range of 0.31–100 μg/mL and against adult parasites at 1.25 mg/mL. The acetone fractions of both leaf and bark demonstrated the highest anti-schistosomal activity causing severe phenotypic alterations (immobility/inactivity, change in shape, translucence, surface disintegration) and death of schistosomules at all dilutions (except 0.31 𝜇g/mL) at 24 h and 48 h. For adult parasites, severe phenotypic changes specifically damage to the adult parasite’s tegument (surface) was observed for the acetone fraction of the stem bark extract. The adult worms were observed to be uncoordinated by 5 h, darkened in color by 24 h and died at 48 h exhibiting tegumental damage [77].
In another study, the in vitro cercaricidal activity of solvent fractions and isolated compounds from the root bark of E. ivorense was investigated against freshly shed cercariae from Schistosoma haematobium. Whereas the cercariae showed normal viability without any morphological changes (tail loss) throughout the entire duration of the experiment in the untreated group, exposure of cercariae to the crude hydro-ethanolic extract, its fractions and compounds caused a concentration and time-dependent decrease in viability of cercariae. Within two hours of incubation, all cercariae died at the various concentrations of test compounds and extracts. Eriodictyol, was the most potent compound with an IC50 of 1.23 ± 0.05 μg/mL. All test samples exhibited a much higher cercaricidal activity than the standard drug praziquantel which caused only 40% mortality of cercariae at the highest concentration tested (IC50 = 695.50 ± 0.05 μg/mL) [78].
3.4 Holarrhena floribunda (G. Don) Dur. & Schinz. (Apocynaceae)
Holarrhena floribunda is native to West Africa and is known in Ghana as ‘osese’ among the Akans. The plant is traditionally used in the treatment of malaria, fever and bareness in females. It has antifungal, antibacterial and antidiabetic properties [79, 80].
The hydroethanolic and alkaloidal extracts from the stem bark of H. floribunda were tested on cercariae from Schistosoma haematobium at concentrations between 15.625 and 500.00 μg/mL. After 180 mins of contact with test samples, the ethanolic extract exhibited the highest cercaricidal potency with an IC50 of 20.09 ± 1.11 μg/mL higher than the effect of paraziquantel (IC50 = 695.50 ± 1.12). The alkaloidal extract also exhibited cercaricidal potency with an IC50 of 53.20 ± 1.33 μg/mL. The isolated compounds: holonamine, holadienine and conessine exhibited cercaricidal potency with IC50 values of 53.24 ± 1.28, 470.80 ± 1.00 and 33.28 ± 1.04 respectively. The results confirmed the activity of Holarrhena floribunda against S. heamatobium ceracriae [81].
3.5 Morinda lucida Benth (Rubiaceae)
[Refer to Section 2.8 for plant description].
In a previous study, the cercaricidal activity of the methanol stem bark extract of M. lucida was carried out. The extract at a concentration of 500 μg/mL elicited 100% mortality of S. mansoni cercariae within 120 mins of exposure giving an IC50 value of 262.3 μg/mL, which was however lower than the effect of the positive control Balanites aegyptiaca (IC50 of 5.95 μg/mL). Further, the in vitro adulticidal effect of the stem bark extract on adult schistosome worms revealed that at a concentration of 125–1000 μg/mL, the extract was found to be lethal to the adult worms within 120 h of exposure [73].
3.6 Nauclea latifolia Carl Lin. (Rubiaceae)
Nauclea latifolia, commonly called the African peach, is a deciduous shrub with an open canopy distributed throughout tropical and savanna regions of Africa and Asia. It varies widely in height from around 10–30 m according to soil and moisture conditions. The plant is used against various medical conditions such as diabetes, fever, indigestion and cough [82].
Previous studies on the cercaricidal activity the methanolic extract of stem bark of N. latifolia revealed 100% mortality of S. mansoni cercariae at a concentration of 250 μg/mL at 120 min (IC50 = 195.9 μg/mL). Further the extract was found to exhibit schistomicidal effect being lethal to the adult incopula worms at a concentration range of 500–1000 μg/mL within 120 mins of exposure [73].
3.7 Phyllanthus amarus Schum. and Thonn. (Euphorbiaceae)
P. amarus is a small herb bearing ascending herbaceous branches normally found around coastal and muddy areas. The whole plant is used in the treatment of gonorrhea, menorrhagia and other urinary and sexually transmitted infections. It is useful in gastropathy, diarrhea, dysentery, intermittent fevers, ophthalmopathy, scabies, ulcers and wounds [83].
The methanolic extract (250 μg/mL) of P. amarus leaves exhibited moderate cercaricidal activity on freshly shed S. mansoni cercariae causing 100% mortality of cercariae within 180 mins of exposure (IC50 = 250.4 μg/mL). It was further established that at 125–1000 μg/mL, the extract caused a drastic reduction in the viability of adult worms [73].
3.8 Rauwolfia vomitoria Afzel. (Apocynaceae)
[Refer to Section 2.13 for plant description].
The root and stem bark of Rauwolfia vomitoria were evaluated for schistosomicidal effect on two different parasitic stages of Schistosoma mansoni i.e. cercariae and adult worms [84].
The ethanolic extract of the root and stem bark were both found to be active against the cercariae and adult worms. At a concentration range of 62.5–1000 𝜇g/mL the stem bark extract exhibited significant anti-cercarial activity (p < 0.05) with an LC50 of 207.4 and 61.18 𝜇g/mL after 1 and 2 h of exposure respectively. At the highest concentration (1000 𝜇g/mL), there was 100% mortality of cercariae within 90 min of exposure. The roots were less active than the stem bark showing activity at a higher concentration range of 250–1000 𝜇g/mL. The schistomicidal activity of the stem bark and roots were further determined against adult worms. All adult worms exposed to the concentrations range of 250–1000 𝜇g/mL for both plant parts died within 120 h of incubation [84].
3.9 Vernonia amygdalina Del. (Asteraceae)
[Refer to Section 2.15 for plant description].
In a previous study, the evaluation of the cercaricidal and schistosomicidal activities of the methanol extract of the leaves of V. amygdalina revealed significant potency response. At 250 μg/mL, the extract exhibited cercaricidal activity with an IC50 of 35.84 μg/mL within 180 min of exposure. Further, the extract was found to reduce the viability of adult schistosome worms in vitro at 250–1000 μg/mL.
The ability of the leaf extract (500 mg/kg p.o.) to reduce the worm recovery and worm burden in S. mansoni infected mice was further investigated in an in vivo study. After a two-week period of treatment, the mean number of worms recovered from V. amygdalina-treated mice was 12.00 ± 1.549, indicating 48.9%, worm burden which was significantly lower than that of the untreated group (40.20 ± 3.072). While there was significant increase in the weight of the liver and spleen of the untreated infected mice with marked formation of granuloma, V. amygdalina-treat infected mice showed no increase in liver or spleen size and had few granulomas which were smaller in diameter with relatively less severe inflammatory cell infiltration compared [73].
4. Conclusion
The anthelmintic and anti-schistosomal activities of some medicinal plants employed in Ghanaian traditional medicine have been validated. For most of these plants however, the specific bioactive constituents are not yet identified. It is therefore imperative that further studies to isolate and verify the constituents responsible for the observed activities be performed. Further, the evaluation of safety profiles will add substantial value to the reported bioactivities and make these plants attractive for adaptation to pharmaceutical companies for further development.
Conflict of interest
Authors have no conflict of interest to declare.
\n',keywords:"schistosomiasis, worms, parasite, helminth, Ghana, herbal medicine",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/76353.pdf",chapterXML:"https://mts.intechopen.com/source/xml/76353.xml",downloadPdfUrl:"/chapter/pdf-download/76353",previewPdfUrl:"/chapter/pdf-preview/76353",totalDownloads:191,totalViews:0,totalCrossrefCites:0,dateSubmitted:"February 24th 2021",dateReviewed:"March 25th 2021",datePrePublished:"April 20th 2021",datePublished:"May 11th 2022",dateFinished:"April 20th 2021",readingETA:"0",abstract:"Parasitic infections including schistosomiasis and soil transmitted helminthiasis are the most commonly encountered Neglected Tropical Diseases (NTDs) in the world. These diseases remain a major public health concern affecting millions of people especially those living in poor regions where access to effective conventional health care is a challenge. Interventions to control these infections in endemic areas have not been successful due to the high cost of drugs, limited availability as well as inequity of access to preventive chemotherapies. Another problem is the development resistance to the limited number of recommended medications due to their intensive use in both human and live-stock. There is an increasing awareness of the potential of natural products as chemotherapeutic agents to combat parasitic infections. Natural products may offer an unlimited source of chemically diverse drug molecules which may be safe, efficient, less toxic, less expensive and readily available for use especially in low-income countries. The Ghanaian flora provides such a ready source for new therapeutic interventions for the local population. Several researches have provided evidence of the anti-parasitic activity of Ghanaian medicinal plants. This chapter provides a review with special focus on medicinal plants collected from Ghana with anthelmintic and anti-schistosomal activity. Evidence of pharmacological activities of crude extracts, fractions and bioactive phytoconstituents as well as possible mechanisms of action where investigated are discussed.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/76353",risUrl:"/chapter/ris/76353",signatures:"Evelyn Asante-Kwatia, Abraham Yeboah Mensah, Lord Gyimah and Arnold Donkor Forkuo",book:{id:"10356",type:"book",title:"Natural Medicinal Plants",subtitle:null,fullTitle:"Natural Medicinal Plants",slug:"natural-medicinal-plants",publishedDate:"May 11th 2022",bookSignature:"Hany A. El-Shemy",coverURL:"https://cdn.intechopen.com/books/images_new/10356.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",isbn:"978-1-83969-276-5",printIsbn:"978-1-83969-275-8",pdfIsbn:"978-1-83969-277-2",isAvailableForWebshopOrdering:!0,editors:[{id:"54719",title:"Prof.",name:"Hany",middleName:null,surname:"El-Shemy",slug:"hany-el-shemy",fullName:"Hany El-Shemy"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}},authors:[{id:"217045",title:"Dr.",name:"Arnold Forkuo",middleName:null,surname:"Donkor",fullName:"Arnold Forkuo Donkor",slug:"arnold-forkuo-donkor",email:"forkuo3@gmail.com",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:null},{id:"303360",title:"Dr.",name:"Evelyn",middleName:null,surname:"Asante-Kwatia",fullName:"Evelyn Asante-Kwatia",slug:"evelyn-asante-kwatia",email:"emireku@yahoo.com",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:null},{id:"309974",title:"Prof.",name:"Abraham Yeboah",middleName:null,surname:"Mensah",fullName:"Abraham Yeboah Mensah",slug:"abraham-yeboah-mensah",email:"aymensah@yahoo.com",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:{name:"Kwame Nkrumah University of Science and Technology",institutionURL:null,country:{name:"Ghana"}}},{id:"347910",title:"Mr.",name:"Lord",middleName:null,surname:"Gyimah",fullName:"Lord Gyimah",slug:"lord-gyimah",email:"lordgyimah36@gmail.com",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:{name:"Kwame Nkrumah University of Science and Technology",institutionURL:null,country:{name:"Ghana"}}}],sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_1_2",title:"1.1 Soil transmitted helminthiasis (STH)-the disease burden and current chemotherapy",level:"2"},{id:"sec_2_2",title:"1.2 Schistosomiasis—the disease burden and current chemotherapy",level:"2"},{id:"sec_3_2",title:"1.3 Methods used in this review for identifying medicinal plants with anthelminthic and anti-schistosomal activities",level:"2"},{id:"sec_5",title:"2. Plants with anthelminthic activity identified from Ghana",level:"1"},{id:"sec_5_2",title:"2.1 Alcornea cordifolia (Schumach & Thonn) Müll. Arg. Euphorbiaceae",level:"2"},{id:"sec_6_2",title:"2.2 Alstonei boonei De Wild (Apocynaceae)",level:"2"},{id:"sec_7_2",title:"2.3 Azadirachta indica A. Juss. (Meliaceae)",level:"2"},{id:"sec_8_2",title:"2.4 Carica papaya Linn. (Caricaceae)",level:"2"},{id:"sec_9_2",title:"2.5 Combretum mucronatum Schumach & Thonn. (Combretaceae)",level:"2"},{id:"sec_10_2",title:"2.6 Cyperus difformis Linn. (Cyperaceae)",level:"2"},{id:"sec_11_2",title:"2.7 Garcinia cola Heckel (Guttiferae)",level:"2"},{id:"sec_12_2",title:"2.8 Morinda lucida Benth. (Rubiaceae)",level:"2"},{id:"sec_13_2",title:"2.9 Moringa oleifera Lam. (Moringaceae)",level:"2"},{id:"sec_14_2",title:"2.10 Ocimum basilicum Linn (Lamiaceae)",level:"2"},{id:"sec_15_2",title:"2.11 Paullinia pinnata L. (Euphorbiaceaae)",level:"2"},{id:"sec_16_2",title:"2.12 Plumbago zeylanica Linn. (Plumbaginaceae)",level:"2"},{id:"sec_17_2",title:"2.13 Rauwolfia vomitoria Afzel. (Apocynaceae)",level:"2"},{id:"sec_18_2",title:"2.14 Sclerocarya birrea (A. Rich) Hochst (Anacardiaceae)",level:"2"},{id:"sec_19_2",title:"2.15 Vernonia amygdalina Del. (Asteraceae)",level:"2"},{id:"sec_20_2",title:"2.16 Voacanga Africana Stapf. (Apocynaceae)",level:"2"},{id:"sec_21_2",title:"2.17 Xylopia aethiopica (Dunal) A. Rich. (Apocynaceae)",level:"2"},{id:"sec_23",title:"3. Plants with cercaricidal and anti-schistosomal activities identified from Ghana",level:"1"},{id:"sec_23_2",title:"3.1 Azadirachta indica A. Juss (Meliaceae)",level:"2"},{id:"sec_24_2",title:"3.2 Dichapetalum crassifolium Chodat (Dichapetalaceae)",level:"2"},{id:"sec_25_2",title:"3.3 Erythrophleum ivorense Afzel (Euphorbiaceae)",level:"2"},{id:"sec_26_2",title:"3.4 Holarrhena floribunda (G. Don) Dur. & Schinz. (Apocynaceae)",level:"2"},{id:"sec_27_2",title:"3.5 Morinda lucida Benth (Rubiaceae)",level:"2"},{id:"sec_28_2",title:"3.6 Nauclea latifolia Carl Lin. (Rubiaceae)",level:"2"},{id:"sec_29_2",title:"3.7 Phyllanthus amarus Schum. and Thonn. (Euphorbiaceae)",level:"2"},{id:"sec_30_2",title:"3.8 Rauwolfia vomitoria Afzel. (Apocynaceae)",level:"2"},{id:"sec_31_2",title:"3.9 Vernonia amygdalina Del. (Asteraceae)",level:"2"},{id:"sec_33",title:"4. Conclusion",level:"1"},{id:"sec_37",title:"Conflict of interest",level:"1"}],chapterReferences:[{id:"B1",body:'Hotez PJ, Kamath A. 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African Journal of Traditional, Complementary and Alternative Medicines. 2017; 14(2):227-233'},{id:"B81",body:'Amponsah IK, Armah FA, Alake J, Harley BK, Ampofo EK, Asante-Kwatia E, Clinton B, Amoani B, Henneh TI. In-vitro Anti-cercarial activity of extracts and steroidal alkaloids from the stem bark of Holarrhena floribunda (G. Don) Dur. & Schinz International Journal of Phytomedicine. 2020; 12(3):069-073'},{id:"B82",body:'Abdel-Rahman NA-G, Nauclea latifolia (Karmadoda): Distribution, Composition and Utilization. In: Mariod A. editor. Wild Fruits: Composition, Nutritional Value and Products. Springer Cham; 2019. pp. 435-445'},{id:"B83",body:'Patel JR, Tripathi P, Sharma V, Chauhan NS, Dixit VK. Phyllanthus amarus: ethnomedicinal uses, phytochemistry and pharmacology: A Review. Journal of Ethnopharmacology. 2011; 138(2):286-313'},{id:"B84",body:'Tekwu EM, Bosompem KM, Anyan WK, Appiah-Opong R, Owusu KB-A, Tettey MD, et al. In vitro assessment of anthelmintic activities of Rauwolfia vomitoria (Apocynaceae) stem bark and roots against parasitic stages of Schistosoma mansoni and cytotoxic study. Journal of Parasitology Research. 2017; 2017:1-11'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"Evelyn Asante-Kwatia",address:"emireku@yahoo.com",affiliation:'
Department of Pharmacognosy, Faculty of Pharmacy and Pharmaceutical Sciences, College of Health Sciences, Kwame Nkrumah University of Science and Technology, Ghana
Department of Pharmacognosy, Faculty of Pharmacy and Pharmaceutical Sciences, College of Health Sciences, Kwame Nkrumah University of Science and Technology, Ghana
Department of Pharmacognosy, Faculty of Pharmacy and Pharmaceutical Sciences, College of Health Sciences, Kwame Nkrumah University of Science and Technology, Ghana
Department of Pharmacology, Faculty of Pharmacy and Pharmaceutical Sciences, College of Health Sciences, Kwame Nkrumah University of Science and Technology, Ghana
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Morrell"}]},{id:"16100",doi:"10.5772/16592",title:"Artificial Insemination in Pigs",slug:"artificial-insemination-in-pigs",totalDownloads:15223,totalCrossrefCites:7,totalDimensionsCites:15,abstract:null,book:{id:"185",slug:"artificial-insemination-in-farm-animals",title:"Artificial Insemination in Farm Animals",fullTitle:"Artificial Insemination in Farm Animals"},signatures:"Maes Dominiek, Lopez Rodriguez Alfonso, Rijsselaere Tom, Vyt Philip and Van Soom Ann",authors:[{id:"25704",title:"Prof.",name:"Dominiek",middleName:null,surname:"Maes",slug:"dominiek-maes",fullName:"Dominiek Maes"},{id:"41076",title:"Dr.",name:"Alfonso",middleName:null,surname:"Lopéz Rodriguez",slug:"alfonso-lopez-rodriguez",fullName:"Alfonso Lopéz Rodriguez"},{id:"41077",title:"Dr.",name:"Tom",middleName:null,surname:"Rijsselaere",slug:"tom-rijsselaere",fullName:"Tom Rijsselaere"},{id:"41078",title:"Dr.",name:"Philip",middleName:null,surname:"Vyt",slug:"philip-vyt",fullName:"Philip Vyt"},{id:"41079",title:"Prof.",name:"Ann",middleName:null,surname:"Van Soom",slug:"ann-van-soom",fullName:"Ann Van Soom"}]},{id:"68173",doi:"10.5772/intechopen.86799",title:"A Review on the Influence of Climate Change on Sheep Reproduction",slug:"a-review-on-the-influence-of-climate-change-on-sheep-reproduction",totalDownloads:1237,totalCrossrefCites:10,totalDimensionsCites:13,abstract:"Increasing food and natural fibre production ensure food security for nearly 10 billion people, the projected global population in 2050, without causing further environmental damage can be achieved by transforming systems and adopting sustainable agriculture practices within a changing climate. Globally, climate change effects are having both direct and indirect effects on agricultural productivity including changing rainfall patterns, drought, flooding and the geographical redistribution of pests and diseases. Climate change induced heat stress is thus one of the complex factors making sheep management and husbandry challenging in many geographical locations in the world. Within the sheep industry, reproductive wastage (RW) is a major challenge throughout the varying breeding landscapes. Reproductive wastage is defined as the early losses of embryos undergoing natural and/or artificial breeding programs. Our previous research showed that heat stress (THI > 75) and elevated glucocorticoid levels (indexed using faecal glucocorticoid metabolites) are linked to embryo loss in Merino ewes. This mini review discusses how extreme variation in climate such as heat stress affects the maternal reproductive performance in the Merino sheep and the impacts on the wool industry. 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The normal duration of estrus cycle is 21 days in cow, sow, and mare, 17 days in ewe, and 20 days in doe. The species which exhibit a single estrus cycle are known as monstrous and species which come into estrus twice or more are termed polyestrous animals. Among them some species have estrus cycles in a particular season and defined as seasonal polyestrous. It includes goats, sheep, and horses. On the other hand, cattle undergo estrus throughout the year. The estrus inducers can grossly be divided into two parts, that is, non-hormonal and hormonal. Non-hormonal treatments include plant-derived heat inducers, mineral supplementation, uterine and ovarian massage, and use of Lugol’s iodine. The hormones that are used in estrus induction are estrogen, progesterone, GnRH, prostaglandin, insulin, and anti-prolactin-based treatment. Synchronization can shorten the breeding period to less than 5 days, instead of females being bred over a 21-day period, depending on the treatment regimen. The combination of GnRH with the prostaglandin F2α (PGF2α)- and progesterone-based synchronization program has shown a novel direction in the estrus synchronization of cattle with the follicular development manipulation.",book:{id:"8545",slug:"animal-reproduction-in-veterinary-medicine",title:"Animal Reproduction in Veterinary Medicine",fullTitle:"Animal Reproduction in Veterinary Medicine"},signatures:"Prasanna Pal and Mohammad Rayees Dar",authors:[{id:"299126",title:"Dr.",name:"Mohammad Rayees",middleName:null,surname:"Dar",slug:"mohammad-rayees-dar",fullName:"Mohammad Rayees Dar"},{id:"311663",title:"Dr.",name:"Prasanna",middleName:null,surname:"Pal",slug:"prasanna-pal",fullName:"Prasanna Pal"}]},{id:"16102",title:"Sperm Preparation Techniques for Artificial Insemination - Comparison of Sperm Washing, Swim Up, and Density Gradient Centrifugation Methods",slug:"sperm-preparation-techniques-for-artificial-insemination-comparison-of-sperm-washing-swim-up-and-den",totalDownloads:29983,totalCrossrefCites:8,totalDimensionsCites:8,abstract:null,book:{id:"185",slug:"artificial-insemination-in-farm-animals",title:"Artificial Insemination in Farm Animals",fullTitle:"Artificial Insemination in Farm Animals"},signatures:"Ilaria Natali",authors:[{id:"27026",title:"Dr.",name:"Ilaria",middleName:null,surname:"Natali",slug:"ilaria-natali",fullName:"Ilaria Natali"}]},{id:"71105",title:"Understanding Sow Sexual Behavior and the Application of the Boar Pheromone to Stimulate Sow Reproduction",slug:"understanding-sow-sexual-behavior-and-the-application-of-the-boar-pheromone-to-stimulate-sow-reprodu",totalDownloads:1135,totalCrossrefCites:2,totalDimensionsCites:2,abstract:"In this chapter, we review the sexual behavior of domestic pigs, and the visible or measurable anatomical features of the pig that will contribute to detecting sows in estrus. We also summarize olfactory organs, and the effects of a sexual pheromone on pig’s biology and sow reproductive performance. We discuss the role of a live boar in the heat detection where the female is in breeding crates. However, there is an increasing interest in being able to breed sows without a boar present. Farm workers must be trained on the fine points of estrus detection so that they can work in a safe and productive setting. After a review of olfactory biology of the pig, the chapter explains how new pheromonal technology, such as BOARBETTER®, aids in the process of heat detection with or without a live boar. To achieve reproductive success, the persons breeding must assimilate all fine points of pig sexual behavior and possess a clear understanding of what they should be looking for in each sow they expect to breed.",book:{id:"8545",slug:"animal-reproduction-in-veterinary-medicine",title:"Animal Reproduction in Veterinary Medicine",fullTitle:"Animal Reproduction in Veterinary Medicine"},signatures:"John J. McGlone, Edgar O. Aviles-Rosa, Courtney Archer, Meyer M. Wilson, Karlee D. Jones, Elaina M. Matthews, Amanda A. 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Mastitis is responsible for great economic losses to the dairy producer and to the milk processing industry resulting from reduced milk production, alterations in milk composition, discarded milk, increased replacement costs, extra labor, treatment costs, and veterinary services. Economic losses due to bovine mastitis are estimated to be $2 billion in the United States, $400 million in Canada (Canadian Bovine Mastitis and Milk Quality Research Network-CBMQRN) and $130 million in Australia per year. Many factors can influence the development of mastitis; however, inflammation of the mammary gland is usually a consequence of adhesion, invasion, and colonization of the mammary gland by one or more mastitis pathogens such as Staphylococcus aureus, Streptococcus uberis, and Escherichia coli.",book:{id:"8545",slug:"animal-reproduction-in-veterinary-medicine",title:"Animal Reproduction in Veterinary Medicine",fullTitle:"Animal Reproduction in Veterinary Medicine"},signatures:"Oudessa Kerro Dego",authors:[{id:"283019",title:"Dr.",name:"Oudessa",middleName:null,surname:"Kerro Dego",slug:"oudessa-kerro-dego",fullName:"Oudessa Kerro Dego"}]}],onlineFirstChaptersFilter:{topicId:"1379",limit:6,offset:0},onlineFirstChaptersCollection:[],onlineFirstChaptersTotal:0},preDownload:{success:null,errors:{}},subscriptionForm:{success:null,errors:{}},aboutIntechopen:{},privacyPolicy:{},peerReviewing:{},howOpenAccessPublishingWithIntechopenWorks:{},sponsorshipBooks:{sponsorshipBooks:[],offset:8,limit:8,total:0},allSeries:{pteSeriesList:[{id:"14",title:"Artificial Intelligence",numberOfPublishedBooks:8,numberOfPublishedChapters:87,numberOfOpenTopics:6,numberOfUpcomingTopics:0,issn:"2633-1403",doi:"10.5772/intechopen.79920",isOpenForSubmission:!0},{id:"7",title:"Biomedical Engineering",numberOfPublishedBooks:12,numberOfPublishedChapters:98,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2631-5343",doi:"10.5772/intechopen.71985",isOpenForSubmission:!0}],lsSeriesList:[{id:"11",title:"Biochemistry",numberOfPublishedBooks:27,numberOfPublishedChapters:286,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2632-0983",doi:"10.5772/intechopen.72877",isOpenForSubmission:!0},{id:"25",title:"Environmental Sciences",numberOfPublishedBooks:1,numberOfPublishedChapters:9,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2754-6713",doi:"10.5772/intechopen.100362",isOpenForSubmission:!0},{id:"10",title:"Physiology",numberOfPublishedBooks:11,numberOfPublishedChapters:139,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2631-8261",doi:"10.5772/intechopen.72796",isOpenForSubmission:!0}],hsSeriesList:[{id:"3",title:"Dentistry",numberOfPublishedBooks:8,numberOfPublishedChapters:129,numberOfOpenTopics:0,numberOfUpcomingTopics:2,issn:"2631-6218",doi:"10.5772/intechopen.71199",isOpenForSubmission:!1},{id:"6",title:"Infectious Diseases",numberOfPublishedBooks:13,numberOfPublishedChapters:105,numberOfOpenTopics:3,numberOfUpcomingTopics:1,issn:"2631-6188",doi:"10.5772/intechopen.71852",isOpenForSubmission:!0},{id:"13",title:"Veterinary Medicine and Science",numberOfPublishedBooks:9,numberOfPublishedChapters:101,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2632-0517",doi:"10.5772/intechopen.73681",isOpenForSubmission:!0}],sshSeriesList:[{id:"22",title:"Business, Management and Economics",numberOfPublishedBooks:1,numberOfPublishedChapters:11,numberOfOpenTopics:2,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100359",isOpenForSubmission:!0},{id:"23",title:"Education and Human Development",numberOfPublishedBooks:0,numberOfPublishedChapters:0,numberOfOpenTopics:2,numberOfUpcomingTopics:0,issn:null,doi:"10.5772/intechopen.100360",isOpenForSubmission:!1},{id:"24",title:"Sustainable Development",numberOfPublishedBooks:0,numberOfPublishedChapters:9,numberOfOpenTopics:4,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100361",isOpenForSubmission:!0}],testimonialsList:[{id:"6",text:"It is great to work with the IntechOpen to produce a worthwhile collection of research that also becomes a great educational resource and guide for future research endeavors.",author:{id:"259298",name:"Edward",surname:"Narayan",institutionString:null,profilePictureURL:"https://mts.intechopen.com/storage/users/259298/images/system/259298.jpeg",slug:"edward-narayan",institution:{id:"3",name:"University of Queensland",country:{id:null,name:"Australia"}}}},{id:"13",text:"The collaboration with and support of the technical staff of IntechOpen is fantastic. The whole process of submitting an article and editing of the submitted article goes extremely smooth and fast, the number of reads and downloads of chapters is high, and the contributions are also frequently cited.",author:{id:"55578",name:"Antonio",surname:"Jurado-Navas",institutionString:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRisIQAS/Profile_Picture_1626166543950",slug:"antonio-jurado-navas",institution:{id:"720",name:"University of Malaga",country:{id:null,name:"Spain"}}}}]},series:{item:{id:"24",title:"Sustainable Development",doi:"10.5772/intechopen.100361",issn:null,scope:"
\r\n\tTransforming our World: the 2030 Agenda for Sustainable Development endorsed by United Nations and 193 Member States, came into effect on Jan 1, 2016, to guide decision making and actions to the year 2030 and beyond. Central to this Agenda are 17 Goals, 169 associated targets and over 230 indicators that are reviewed annually. The vision envisaged in the implementation of the SDGs is centered on the five Ps: People, Planet, Prosperity, Peace and Partnership. This call for renewed focused efforts ensure we have a safe and healthy planet for current and future generations.
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\r\n\tThis Series focuses on covering research and applied research involving the five Ps through the following topics:
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\r\n\t1. Sustainable Economy and Fair Society that relates to SDG 1 on No Poverty, SDG 2 on Zero Hunger, SDG 8 on Decent Work and Economic Growth, SDG 10 on Reduced Inequalities, SDG 12 on Responsible Consumption and Production, and SDG 17 Partnership for the Goals
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\r\n\t2. Health and Wellbeing focusing on SDG 3 on Good Health and Wellbeing and SDG 6 on Clean Water and Sanitation
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\r\n\t3. Inclusivity and Social Equality involving SDG 4 on Quality Education, SDG 5 on Gender Equality, and SDG 16 on Peace, Justice and Strong Institutions
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\r\n\t4. Climate Change and Environmental Sustainability comprising SDG 13 on Climate Action, SDG 14 on Life Below Water, and SDG 15 on Life on Land
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\r\n\t5. Urban Planning and Environmental Management embracing SDG 7 on Affordable Clean Energy, SDG 9 on Industry, Innovation and Infrastructure, and SDG 11 on Sustainable Cities and Communities.
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\r\n\tThe series also seeks to support the use of cross cutting SDGs, as many of the goals listed above, targets and indicators are all interconnected to impact our lives and the decisions we make on a daily basis, making them impossible to tie to a single topic.
",coverUrl:"https://cdn.intechopen.com/series/covers/24.jpg",latestPublicationDate:"April 24th, 2022",hasOnlineFirst:!0,numberOfPublishedBooks:0,editor:{id:"262440",title:"Prof.",name:"Usha",middleName:null,surname:"Iyer-Raniga",slug:"usha-iyer-raniga",fullName:"Usha Iyer-Raniga",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRYSXQA4/Profile_Picture_2022-02-28T13:55:36.jpeg",biography:"Usha Iyer-Raniga is a professor in the School of Property and Construction Management at RMIT University. Usha co-leads the One Planet Network’s Sustainable Buildings and Construction Programme (SBC), a United Nations 10 Year Framework of Programmes on Sustainable Consumption and Production (UN 10FYP SCP) aligned with Sustainable Development Goal 12. The work also directly impacts SDG 11 on Sustainable Cities and Communities. She completed her undergraduate degree as an architect before obtaining her Masters degree from Canada and her Doctorate in Australia. Usha has been a keynote speaker as well as an invited speaker at national and international conferences, seminars and workshops. Her teaching experience includes teaching in Asian countries. She has advised Austrade, APEC, national, state and local governments. She serves as a reviewer and a member of the scientific committee for national and international refereed journals and refereed conferences. She is on the editorial board for refereed journals and has worked on Special Issues. Usha has served and continues to serve on the Boards of several not-for-profit organisations and she has also served as panel judge for a number of awards including the Premiers Sustainability Award in Victoria and the International Green Gown Awards. Usha has published over 100 publications, including research and consulting reports. Her publications cover a wide range of scientific and technical research publications that include edited books, book chapters, refereed journals, refereed conference papers and reports for local, state and federal government clients. She has also produced podcasts for various organisations and participated in media interviews. She has received state, national and international funding worth over USD $25 million. Usha has been awarded the Quarterly Franklin Membership by London Journals Press (UK). Her biography has been included in the Marquis Who's Who in the World® 2018, 2016 (33rd Edition), along with approximately 55,000 of the most accomplished men and women from around the world, including luminaries as U.N. Secretary-General Ban Ki-moon. In 2017, Usha was awarded the Marquis Who’s Who Lifetime Achiever Award.",institutionString:null,institution:{name:"RMIT University",institutionURL:null,country:{name:"Australia"}}},editorTwo:null,editorThree:null},subseries:{paginationCount:9,paginationItems:[{id:"91",title:"Sustainable Economy and Fair Society",coverUrl:"https://cdn.intechopen.com/series_topics/covers/91.jpg",editor:{id:"181603",title:"Dr.",name:"Antonella",middleName:null,surname:"Petrillo",slug:"antonella-petrillo",fullName:"Antonella Petrillo",profilePictureURL:"https://mts.intechopen.com/storage/users/181603/images/system/181603.jpg",biography:"Antonella Petrillo is a Professor at the Department of Engineering of the University of Naples “Parthenope”, Italy. She received her Ph.D. in Mechanical Engineering from the University of Cassino. Her research interests include multi-criteria decision analysis, industrial plant, logistics, manufacturing and safety. 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His research interest focuses on computational chemistry and molecular modeling of diverse systems of pharmacological, food, and alternative energy interests by resorting to DFT and Conceptual DFT. He has authored a coauthored more than 255 peer-reviewed papers, 32 book chapters, and 2 edited books. He has delivered speeches at many international and domestic conferences. He serves as a reviewer for more than eighty international journals, books, and research proposals as well as an editor for special issues of renowned scientific journals.",institutionString:"Centro de Investigación en Materiales Avanzados",institution:{name:"Centro de Investigación en Materiales Avanzados",country:{name:"Mexico"}}},{id:"76477",title:"Prof.",name:"Mirza",middleName:null,surname:"Hasanuzzaman",slug:"mirza-hasanuzzaman",fullName:"Mirza Hasanuzzaman",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/76477/images/system/76477.png",biography:"Dr. Mirza Hasanuzzaman is a Professor of Agronomy at Sher-e-Bangla Agricultural University, Bangladesh. He received his Ph.D. in Plant Stress Physiology and Antioxidant Metabolism from Ehime University, Japan, with a scholarship from the Japanese Government (MEXT). Later, he completed his postdoctoral research at the Center of Molecular Biosciences, University of the Ryukyus, Japan, as a recipient of the Japan Society for the Promotion of Science (JSPS) postdoctoral fellowship. He was also the recipient of the Australian Government Endeavour Research Fellowship for postdoctoral research as an adjunct senior researcher at the University of Tasmania, Australia. Dr. Hasanuzzaman’s current work is focused on the physiological and molecular mechanisms of environmental stress tolerance. Dr. Hasanuzzaman has published more than 150 articles in peer-reviewed journals. He has edited ten books and written more than forty book chapters on important aspects of plant physiology, plant stress tolerance, and crop production. According to Scopus, Dr. Hasanuzzaman’s publications have received more than 10,500 citations with an h-index of 53. He has been named a Highly Cited Researcher by Clarivate. He is an editor and reviewer for more than fifty peer-reviewed international journals and was a recipient of the “Publons Peer Review Award” in 2017, 2018, and 2019. He has been honored by different authorities for his outstanding performance in various fields like research and education, and he has received the World Academy of Science Young Scientist Award (2014) and the University Grants Commission (UGC) Award 2018. He is a fellow of the Bangladesh Academy of Sciences (BAS) and the Royal Society of Biology.",institutionString:"Sher-e-Bangla Agricultural University",institution:{name:"Sher-e-Bangla Agricultural University",country:{name:"Bangladesh"}}},{id:"187859",title:"Prof.",name:"Kusal",middleName:"K.",surname:"Das",slug:"kusal-das",fullName:"Kusal Das",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSBDeQAO/Profile_Picture_1623411145568",biography:"Kusal K. Das is a Distinguished Chair Professor of Physiology, Shri B. M. Patil Medical College and Director, Centre for Advanced Medical Research (CAMR), BLDE (Deemed to be University), Vijayapur, Karnataka, India. Dr. Das did his M.S. and Ph.D. in Human Physiology from the University of Calcutta, Kolkata. His area of research is focused on understanding of molecular mechanisms of heavy metal activated low oxygen sensing pathways in vascular pathophysiology. He has invented a new method of estimation of serum vitamin E. His expertise in critical experimental protocols on vascular functions in experimental animals was well documented by his quality of publications. He was a Visiting Professor of Medicine at University of Leeds, United Kingdom (2014-2016) and Tulane University, New Orleans, USA (2017). For his immense contribution in medical research Ministry of Science and Technology, Government of India conferred him 'G.P. Chatterjee Memorial Research Prize-2019” and he is also the recipient of 'Dr.Raja Ramanna State Scientist Award 2015” by Government of Karnataka. He is a Fellow of the Royal Society of Biology (FRSB), London and Honorary Fellow of Karnataka Science and Technology Academy, Department of Science and Technology, Government of Karnataka.",institutionString:"BLDE (Deemed to be University), India",institution:null},{id:"243660",title:"Dr.",name:"Mallanagouda Shivanagouda",middleName:null,surname:"Biradar",slug:"mallanagouda-shivanagouda-biradar",fullName:"Mallanagouda Shivanagouda Biradar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/243660/images/system/243660.jpeg",biography:"M. S. Biradar is Vice Chancellor and Professor of Medicine of\nBLDE (Deemed to be University), Vijayapura, Karnataka, India.\nHe obtained his MD with a gold medal in General Medicine and\nhas devoted himself to medical teaching, research, and administrations. He has also immensely contributed to medical research\non vascular medicine, which is reflected by his numerous publications including books and book chapters. Professor Biradar was\nalso Visiting Professor at Tulane University School of Medicine, New Orleans, USA.",institutionString:"BLDE (Deemed to be University)",institution:{name:"BLDE University",country:{name:"India"}}},{id:"289796",title:"Dr.",name:"Swastika",middleName:null,surname:"Das",slug:"swastika-das",fullName:"Swastika Das",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/289796/images/system/289796.jpeg",biography:"Swastika N. Das is Professor of Chemistry at the V. P. Dr. P. G.\nHalakatti College of Engineering and Technology, BLDE (Deemed\nto be University), Vijayapura, Karnataka, India. She obtained an\nMSc, MPhil, and PhD in Chemistry from Sambalpur University,\nOdisha, India. Her areas of research interest are medicinal chemistry, chemical kinetics, and free radical chemistry. She is a member\nof the investigators who invented a new modified method of estimation of serum vitamin E. She has authored numerous publications including book\nchapters and is a mentor of doctoral curriculum at her university.",institutionString:"BLDEA’s V.P.Dr.P.G.Halakatti College of Engineering & Technology",institution:{name:"BLDE University",country:{name:"India"}}},{id:"248459",title:"Dr.",name:"Akikazu",middleName:null,surname:"Takada",slug:"akikazu-takada",fullName:"Akikazu Takada",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/248459/images/system/248459.png",biography:"Akikazu Takada was born in Japan, 1935. After graduation from\nKeio University School of Medicine and finishing his post-graduate studies, he worked at Roswell Park Memorial Institute NY,\nUSA. He then took a professorship at Hamamatsu University\nSchool of Medicine. In thrombosis studies, he found the SK\npotentiator that enhances plasminogen activation by streptokinase. He is very much interested in simultaneous measurements\nof fatty acids, amino acids, and tryptophan degradation products. By using fatty\nacid analyses, he indicated that plasma levels of trans-fatty acids of old men were\nfar higher in the US than Japanese men. . He also showed that eicosapentaenoic acid\n(EPA) and docosahexaenoic acid (DHA) levels are higher, and arachidonic acid\nlevels are lower in Japanese than US people. By using simultaneous LC/MS analyses\nof plasma levels of tryptophan metabolites, he recently found that plasma levels of\nserotonin, kynurenine, or 5-HIAA were higher in patients of mono- and bipolar\ndepression, which are significantly different from observations reported before. In\nview of recent reports that plasma tryptophan metabolites are mainly produced by\nmicrobiota. He is now working on the relationships between microbiota and depression or autism.",institutionString:"Hamamatsu University School of Medicine",institution:{name:"Hamamatsu University School of Medicine",country:{name:"Japan"}}},{id:"137240",title:"Prof.",name:"Mohammed",middleName:null,surname:"Khalid",slug:"mohammed-khalid",fullName:"Mohammed Khalid",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/137240/images/system/137240.png",biography:"Mohammed Khalid received his B.S. degree in chemistry in 2000 and Ph.D. degree in physical chemistry in 2007 from the University of Khartoum, Sudan. He moved to School of Chemistry, Faculty of Science, University of Sydney, Australia in 2009 and joined Dr. Ron Clarke as a postdoctoral fellow where he worked on the interaction of ATP with the phosphoenzyme of the Na+/K+-ATPase and dual mechanisms of allosteric acceleration of the Na+/K+-ATPase by ATP; then he went back to Department of Chemistry, University of Khartoum as an assistant professor, and in 2014 he was promoted as an associate professor. In 2011, he joined the staff of Department of Chemistry at Taif University, Saudi Arabia, where he is currently an assistant professor. His research interests include the following: P-Type ATPase enzyme kinetics and mechanisms, kinetics and mechanisms of redox reactions, autocatalytic reactions, computational enzyme kinetics, allosteric acceleration of P-type ATPases by ATP, exploring of allosteric sites of ATPases, and interaction of ATP with ATPases located in cell membranes.",institutionString:"Taif University",institution:{name:"Taif University",country:{name:"Saudi Arabia"}}},{id:"63810",title:"Prof.",name:"Jorge",middleName:null,surname:"Morales-Montor",slug:"jorge-morales-montor",fullName:"Jorge Morales-Montor",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/63810/images/system/63810.png",biography:"Dr. Jorge Morales-Montor was recognized with the Lola and Igo Flisser PUIS Award for best graduate thesis at the national level in the field of parasitology. He received a fellowship from the Fogarty Foundation to perform postdoctoral research stay at the University of Georgia. He has 153 journal articles to his credit. He has also edited several books and published more than fifty-five book chapters. He is a member of the Mexican Academy of Sciences, Latin American Academy of Sciences, and the National Academy of Medicine. He has received more than thirty-five awards and has supervised numerous bachelor’s, master’s, and Ph.D. students. Dr. Morales-Montor is the past president of the Mexican Society of Parasitology.",institutionString:"National Autonomous University of Mexico",institution:{name:"National Autonomous University of Mexico",country:{name:"Mexico"}}},{id:"217215",title:"Dr.",name:"Palash",middleName:null,surname:"Mandal",slug:"palash-mandal",fullName:"Palash Mandal",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/217215/images/system/217215.jpeg",biography:null,institutionString:"Charusat University",institution:null},{id:"49739",title:"Dr.",name:"Leszek",middleName:null,surname:"Szablewski",slug:"leszek-szablewski",fullName:"Leszek Szablewski",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/49739/images/system/49739.jpg",biography:"Leszek Szablewski is a professor of medical sciences. He received his M.S. in the Faculty of Biology from the University of Warsaw and his PhD degree from the Institute of Experimental Biology Polish Academy of Sciences. He habilitated in the Medical University of Warsaw, and he obtained his degree of Professor from the President of Poland. Professor Szablewski is the Head of Chair and Department of General Biology and Parasitology, Medical University of Warsaw. Professor Szablewski has published over 80 peer-reviewed papers in journals such as Journal of Alzheimer’s Disease, Biochim. Biophys. Acta Reviews of Cancer, Biol. Chem., J. Biomed. Sci., and Diabetes/Metabol. Res. Rev, Endocrine. He is the author of two books and four book chapters. He has edited four books, written 15 scripts for students, is the ad hoc reviewer of over 30 peer-reviewed journals, and editorial member of peer-reviewed journals. Prof. Szablewski’s research focuses on cell physiology, genetics, and pathophysiology. He works on the damage caused by lack of glucose homeostasis and changes in the expression and/or function of glucose transporters due to various diseases. He has given lectures, seminars, and exercises for students at the Medical University.",institutionString:"Medical University of Warsaw",institution:{name:"Medical University of Warsaw",country:{name:"Poland"}}},{id:"173123",title:"Dr.",name:"Maitham",middleName:null,surname:"Khajah",slug:"maitham-khajah",fullName:"Maitham Khajah",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/173123/images/system/173123.jpeg",biography:"Dr. Maitham A. Khajah received his degree in Pharmacy from Faculty of Pharmacy, Kuwait University, in 2003 and obtained his PhD degree in December 2009 from the University of Calgary, Canada (Gastrointestinal Science and Immunology). Since January 2010 he has been assistant professor in Kuwait University, Faculty of Pharmacy, Department of Pharmacology and Therapeutics. His research interest are molecular targets for the treatment of inflammatory bowel disease (IBD) and the mechanisms responsible for immune cell chemotaxis. He cosupervised many students for the MSc Molecular Biology Program, College of Graduate Studies, Kuwait University. Ever since joining Kuwait University in 2010, he got various grants as PI and Co-I. He was awarded the Best Young Researcher Award by Kuwait University, Research Sector, for the Year 2013–2014. He was a member in the organizing committee for three conferences organized by Kuwait University, Faculty of Pharmacy, as cochair and a member in the scientific committee (the 3rd, 4th, and 5th Kuwait International Pharmacy Conference).",institutionString:"Kuwait University",institution:{name:"Kuwait University",country:{name:"Kuwait"}}},{id:"195136",title:"Dr.",name:"Aya",middleName:null,surname:"Adel",slug:"aya-adel",fullName:"Aya Adel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/195136/images/system/195136.jpg",biography:"Dr. Adel works as an Assistant Lecturer in the unit of Phoniatrics, Department of Otolaryngology, Ain Shams University in Cairo, Egypt. Dr. Adel is especially interested in joint attention and its impairment in autism spectrum disorder",institutionString:"Ain Shams University",institution:{name:"Ain Shams University",country:{name:"Egypt"}}},{id:"94911",title:"Dr.",name:"Boulenouar",middleName:null,surname:"Mesraoua",slug:"boulenouar-mesraoua",fullName:"Boulenouar Mesraoua",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/94911/images/system/94911.png",biography:"Dr Boulenouar Mesraoua is the Associate Professor of Clinical Neurology at Weill Cornell Medical College-Qatar and a Consultant Neurologist at Hamad Medical Corporation at the Neuroscience Department; He graduated as a Medical Doctor from the University of Oran, Algeria; he then moved to Belgium, the City of Liege, for a Residency in Internal Medicine and Neurology at Liege University; after getting the Belgian Board of Neurology (with high marks), he went to the National Hospital for Nervous Diseases, Queen Square, London, United Kingdom for a fellowship in Clinical Neurophysiology, under Pr Willison ; Dr Mesraoua had also further training in Epilepsy and Continuous EEG Monitoring for two years (from 2001-2003) in the Neurophysiology department of Zurich University, Switzerland, under late Pr Hans Gregor Wieser ,an internationally known epileptologist expert. \n\nDr B. Mesraoua is the Director of the Neurology Fellowship Program at the Neurology Section and an active member of the newly created Comprehensive Epilepsy Program at Hamad General Hospital, Doha, Qatar; he is also Assistant Director of the Residency Program at the Qatar Medical School. \nDr B. Mesraoua's main interests are Epilepsy, Multiple Sclerosis, and Clinical Neurology; He is the Chairman and the Organizer of the well known Qatar Epilepsy Symposium, he is running yearly for the past 14 years and which is considered a landmark in the Gulf region; He has also started last year , together with other epileptologists from Qatar, the region and elsewhere, a yearly International Epilepsy School Course, which was attended by many neurologists from the Area.\n\nInternationally, Dr Mesraoua is an active and elected member of the Commission on Eastern Mediterranean Region (EMR ) , a regional branch of the International League Against Epilepsy (ILAE), where he represents the Middle East and North Africa(MENA ) and where he holds the position of chief of the Epilepsy Epidemiology Section; Dr Mesraoua is a member of the American Academy of Neurology, the Europeen Academy of Neurology and the American Epilepsy Society.\n\nDr Mesraoua's main objectives are to encourage frequent gathering of the epileptologists/neurologists from the MENA region and the rest of the world, promote Epilepsy Teaching in the MENA Region, and encourage multicenter studies involving neurologists and epileptologists in the MENA region, particularly epilepsy epidemiological studies. \n\nDr. Mesraoua is the recipient of two research Grants, as the Lead Principal Investigator (750.000 USD and 250.000 USD) from the Qatar National Research Fund (QNRF) and the Hamad Hospital Internal Research Grant (IRGC), on the following topics : “Continuous EEG Monitoring in the ICU “ and on “Alpha-lactoalbumin , proof of concept in the treatment of epilepsy” .Dr Mesraoua is a reviewer for the journal \"seizures\" (Europeen Epilepsy Journal ) as well as dove journals ; Dr Mesraoua is the author and co-author of many peer reviewed publications and four book chapters in the field of Epilepsy and Clinical Neurology",institutionString:"Weill Cornell Medical College in Qatar",institution:{name:"Weill Cornell Medical College in Qatar",country:{name:"Qatar"}}},{id:"282429",title:"Prof.",name:"Covanis",middleName:null,surname:"Athanasios",slug:"covanis-athanasios",fullName:"Covanis Athanasios",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/282429/images/system/282429.jpg",biography:null,institutionString:"Neurology-Neurophysiology Department of the Children Hospital Agia Sophia",institution:null},{id:"190980",title:"Prof.",name:"Marwa",middleName:null,surname:"Mahmoud Saleh",slug:"marwa-mahmoud-saleh",fullName:"Marwa Mahmoud Saleh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/190980/images/system/190980.jpg",biography:"Professor Marwa Mahmoud Saleh is a doctor of medicine and currently works in the unit of Phoniatrics, Department of Otolaryngology, Ain Shams University in Cairo, Egypt. She got her doctoral degree in 1991 and her doctoral thesis was accomplished in the University of Iowa, United States. Her publications covered a multitude of topics as videokymography, cochlear implants, stuttering, and dysphagia. She has lectured Egyptian phonology for many years. Her recent research interest is joint attention in autism.",institutionString:"Ain Shams University",institution:{name:"Ain Shams University",country:{name:"Egypt"}}},{id:"259190",title:"Dr.",name:"Syed Ali Raza",middleName:null,surname:"Naqvi",slug:"syed-ali-raza-naqvi",fullName:"Syed Ali Raza Naqvi",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/259190/images/system/259190.png",biography:"Dr. Naqvi is a radioanalytical chemist and is working as an associate professor of analytical chemistry in the Department of Chemistry, Government College University, Faisalabad, Pakistan. Advance separation techniques, nuclear analytical techniques and radiopharmaceutical analysis are the main courses that he is teaching to graduate and post-graduate students. In the research area, he is focusing on the development of organic- and biomolecule-based radiopharmaceuticals for diagnosis and therapy of infectious and cancerous diseases. Under the supervision of Dr. Naqvi, three students have completed their Ph.D. degrees and 41 students have completed their MS degrees. He has completed three research projects and is currently working on 2 projects entitled “Radiolabeling of fluoroquinolone derivatives for the diagnosis of deep-seated bacterial infections” and “Radiolabeled minigastrin peptides for diagnosis and therapy of NETs”. He has published about 100 research articles in international reputed journals and 7 book chapters. Pakistan Institute of Nuclear Science & Technology (PINSTECH) Islamabad, Punjab Institute of Nuclear Medicine (PINM), Faisalabad and Institute of Nuclear Medicine and Radiology (INOR) Abbottabad are the main collaborating institutes.",institutionString:"Government College University",institution:{name:"Government College University, Faisalabad",country:{name:"Pakistan"}}},{id:"58390",title:"Dr.",name:"Gyula",middleName:null,surname:"Mozsik",slug:"gyula-mozsik",fullName:"Gyula Mozsik",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/58390/images/system/58390.png",biography:"Gyula Mózsik MD, Ph.D., ScD (med), is an emeritus professor of Medicine at the First Department of Medicine, Univesity of Pécs, Hungary. He was head of this department from 1993 to 2003. His specializations are medicine, gastroenterology, clinical pharmacology, clinical nutrition, and dietetics. His research fields are biochemical pharmacological examinations in the human gastrointestinal (GI) mucosa, mechanisms of retinoids, drugs, capsaicin-sensitive afferent nerves, and innovative pharmacological, pharmaceutical, and nutritional (dietary) research in humans. He has published about 360 peer-reviewed papers, 197 book chapters, 692 abstracts, 19 monographs, and has edited 37 books. He has given about 1120 regular and review lectures. He has organized thirty-eight national and international congresses and symposia. He is the founder of the International Conference on Ulcer Research (ICUR); International Union of Pharmacology, Gastrointestinal Section (IUPHAR-GI); Brain-Gut Society symposiums, and gastrointestinal cytoprotective symposiums. He received the Andre Robert Award from IUPHAR-GI in 2014. Fifteen of his students have been appointed as full professors in Egypt, Cuba, and Hungary.",institutionString:"University of Pécs",institution:{name:"University of Pecs",country:{name:"Hungary"}}},{id:"277367",title:"M.Sc.",name:"Daniel",middleName:"Martin",surname:"Márquez López",slug:"daniel-marquez-lopez",fullName:"Daniel Márquez López",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/277367/images/7909_n.jpg",biography:"Msc Daniel Martin Márquez López has a bachelor degree in Industrial Chemical Engineering, a Master of science degree in the same área and he is a PhD candidate for the Instituto Politécnico Nacional. His Works are realted to the Green chemistry field, biolubricants, biodiesel, transesterification reactions for biodiesel production and the manipulation of oils for therapeutic purposes.",institutionString:null,institution:{name:"Instituto Politécnico Nacional",country:{name:"Mexico"}}},{id:"196544",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/196544/images/system/196544.jpg",biography:"Angel Catalá studied chemistry at Universidad Nacional de La Plata, Argentina, where he received a Ph.D. in Chemistry (Biological Branch) in 1965. From 1964 to 1974, he worked as an Assistant in Biochemistry at the School of Medicine at the same university. From 1974 to 1976, he was a fellow of the National Institutes of Health (NIH) at the University of Connecticut, Health Center, USA. From 1985 to 2004, he served as a Full Professor of Biochemistry at the Universidad Nacional de La Plata. He is a member of the National Research Council (CONICET), Argentina, and the Argentine Society for Biochemistry and Molecular Biology (SAIB). His laboratory has been interested for many years in the lipid peroxidation of biological membranes from various tissues and different species. Dr. Catalá has directed twelve doctoral theses, published more than 100 papers in peer-reviewed journals, several chapters in books, and edited twelve books. He received awards at the 40th International Conference Biochemistry of Lipids 1999 in Dijon, France. He is the winner of the Bimbo Pan-American Nutrition, Food Science and Technology Award 2006 and 2012, South America, Human Nutrition, Professional Category. In 2006, he won the Bernardo Houssay award in pharmacology, in recognition of his meritorious works of research. Dr. Catalá belongs to the editorial board of several journals including Journal of Lipids; International Review of Biophysical Chemistry; Frontiers in Membrane Physiology and Biophysics; World Journal of Experimental Medicine and Biochemistry Research International; World Journal of Biological Chemistry, Diabetes, and the Pancreas; International Journal of Chronic Diseases & Therapy; and International Journal of Nutrition. He is the co-editor of The Open Biology Journal and associate editor for Oxidative Medicine and Cellular Longevity.",institutionString:"Universidad Nacional de La Plata",institution:{name:"National University of La Plata",country:{name:"Argentina"}}},{id:"186585",title:"Dr.",name:"Francisco Javier",middleName:null,surname:"Martin-Romero",slug:"francisco-javier-martin-romero",fullName:"Francisco Javier Martin-Romero",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSB3HQAW/Profile_Picture_1631258137641",biography:"Francisco Javier Martín-Romero (Javier) is a Professor of Biochemistry and Molecular Biology at the University of Extremadura, Spain. He is also a group leader at the Biomarkers Institute of Molecular Pathology. Javier received his Ph.D. in 1998 in Biochemistry and Biophysics. At the National Cancer Institute (National Institute of Health, Bethesda, MD) he worked as a research associate on the molecular biology of selenium and its role in health and disease. After postdoctoral collaborations with Carlos Gutierrez-Merino (University of Extremadura, Spain) and Dario Alessi (University of Dundee, UK), he established his own laboratory in 2008. The interest of Javier's lab is the study of cell signaling with a special focus on Ca2+ signaling, and how Ca2+ transport modulates the cytoskeleton, migration, differentiation, cell death, etc. He is especially interested in the study of Ca2+ channels, and the role of STIM1 in the initiation of pathological events.",institutionString:null,institution:{name:"University of Extremadura",country:{name:"Spain"}}},{id:"217323",title:"Prof.",name:"Guang-Jer",middleName:null,surname:"Wu",slug:"guang-jer-wu",fullName:"Guang-Jer Wu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/217323/images/8027_n.jpg",biography:null,institutionString:null,institution:null},{id:"148546",title:"Dr.",name:"Norma Francenia",middleName:null,surname:"Santos-Sánchez",slug:"norma-francenia-santos-sanchez",fullName:"Norma Francenia Santos-Sánchez",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/148546/images/4640_n.jpg",biography:null,institutionString:null,institution:null},{id:"272889",title:"Dr.",name:"Narendra",middleName:null,surname:"Maddu",slug:"narendra-maddu",fullName:"Narendra Maddu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/272889/images/10758_n.jpg",biography:null,institutionString:null,institution:null},{id:"242491",title:"Prof.",name:"Angelica",middleName:null,surname:"Rueda",slug:"angelica-rueda",fullName:"Angelica Rueda",position:"Investigador Cinvestav 3B",profilePictureURL:"https://mts.intechopen.com/storage/users/242491/images/6765_n.jpg",biography:null,institutionString:null,institution:null},{id:"88631",title:"Dr.",name:"Ivan",middleName:null,surname:"Petyaev",slug:"ivan-petyaev",fullName:"Ivan Petyaev",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Lycotec (United Kingdom)",country:{name:"United Kingdom"}}},{id:"423869",title:"Ms.",name:"Smita",middleName:null,surname:"Rai",slug:"smita-rai",fullName:"Smita Rai",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"424024",title:"Prof.",name:"Swati",middleName:null,surname:"Sharma",slug:"swati-sharma",fullName:"Swati Sharma",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"439112",title:"MSc.",name:"Touseef",middleName:null,surname:"Fatima",slug:"touseef-fatima",fullName:"Touseef Fatima",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"424836",title:"Dr.",name:"Orsolya",middleName:null,surname:"Borsai",slug:"orsolya-borsai",fullName:"Orsolya Borsai",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Agricultural Sciences and Veterinary Medicine of Cluj-Napoca",country:{name:"Romania"}}},{id:"422262",title:"Ph.D.",name:"Paola Andrea",middleName:null,surname:"Palmeros-Suárez",slug:"paola-andrea-palmeros-suarez",fullName:"Paola Andrea Palmeros-Suárez",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Guadalajara",country:{name:"Mexico"}}}]}},subseries:{item:{id:"93",type:"subseries",title:"Inclusivity and Social Equity",keywords:"Social contract, SDG, Human rights, Inclusiveness, Equity, Democracy, Personal learning, Collaboration, Glocalization",scope:"
\r\n\tThis topic is dedicated to the efforts and promotion of UNESCO SDG4, the UNESCO initiative on the future of education, and the need for a new social contract for education. It aims to disseminate knowledge on policies, strategies, methods, and technologies that increase the resilience and sustainability of the development of the future of education and the new social contract for education. It will also consider the global challenges such as globalization, demographic change, digital transformation, climate change, environment and the social pillars of sustainable development.
\r\n
\r\n\tResponses to the pandemic and the widespread discontent that preceded it must be based on a new social contract and a New Global Deal for education that ensures equal opportunities for all and respects all people’s rights and freedoms (UNESCO; 2021). Such a new social contract, as proposed by UNESCO, must be based on the general principles underlying human rights - inclusion and equality, cooperation and solidarity, and collective responsibility and interconnectedness - and be guided by the following fundamental principle: Ensure that everyone has access to quality education throughout their lives.
\r\n
\r\n\tWe face the dual challenge of delivering on the unfulfilled promise of ensuring the right to quality education for every child, youth, and adult, as well as fully realizing the transformative potential of education as a pathway to a more sustainable collective future. To achieve this, we need a new social contract for education that eliminates inequities while transforming the future. This new social contract must be based on human rights and the principles of non-discrimination, social justice, respect for life, human dignity, and cultural diversity. It must include an ethic of care, reciprocity and solidarity. The new social contract builds on inclusiveness, equity, lifelong learning, SDG, collaboration and personal learning in a global context for democracy.
\r\n
\r\n\tAt an international level, the adoption of the Open Educational Resources recommendation and the Open Science recommendation represents an important step towards building more open and inclusive knowledge societies as well as the achievement of the UN 2030 Agenda. Indeed, implementing the recommendations will help to achieve at least five more Sustainable Development Goals (SDGs) that are intertwined with the topic of this book series, namely SDG 5 (Gender equality), SDG 9 (Industry, innovation and infrastructure), SDG 10 (Reduced inequalities within and across countries), SDG 16 (Peace, justice and strong institutions) and SDG 17 (Partnerships for the goals).
",coverUrl:"https://cdn.intechopen.com/series_topics/covers/93.jpg",hasOnlineFirst:!1,hasPublishedBooks:!1,annualVolume:11977,editor:{id:"210060",title:"Prof. Dr.",name:"Ebba",middleName:null,surname:"Ossiannilsson",slug:"ebba-ossiannilsson",fullName:"Ebba Ossiannilsson",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002g6LkBQAU/Profile_Picture_2022-02-28T13:31:48.png",biography:'Professor Dr. Ebba Ossiannilsson is an independent researcher, expert, consultant, quality auditor and influencer in the fields of open, flexible online and distance learning (OFDL) and the "new normal". Her focus is on quality, innovation, leadership, and personalised learning. She works primarily at the strategic and policy levels, both nationally and internationally, and with key international organisations. She is committed to promoting and improving OFDL in the context of SDG4 and the future of education. Ossiannilsson has more than 20 years of experience in her current field, but more than 40 years in the education sector. She works as a reviewer and expert for the European Commission and collaborates with the Joint Research Centre for Quality in Open Education. Ossiannilsson also collaborates with ITCILO and ICoBC (International Council on Badges and Credentials). She is a member of the ICDE Board of Directors and has previously served on the boards of EDEN and EUCEN. Ossiannilsson is a quality expert and reviewer for ICDE, EDEN and the EADTU. She chairs the ICDE OER Advocacy Committee and is a member of the ICDE Quality Network. She is regularly invited as a keynote speaker at conferences. She is a guest editor for several special issues and a member of the editorial board of several scientific journals. She has published more than 200 articles and is currently working on book projects in the field of OFDL. Ossiannilsson is a visiting professor at several international universities and was recently appointed Professor and Research Fellow at Victoria University of Wellington, NZ. Ossiannilsson has been awarded the following fellowships: EDEN Fellows, EDEN Council of Fellows, and Open Education Europe. She is a ICDE OER Ambassador, Open Education Europe Ambassador, GIZ Ambassador for Quality in Digital Learning, and part of the Globe-Community of Digital Learning and Champion of SPARC Europe. On a national level, she is a quality developer at the Swedish Institute for Standards (SIS) and for ISO. She is a member of the Digital Skills and Jobs Coalition Sweden and Vice President of the Swedish Association for Distance Education. She is currently working on a government initiative on quality in distance education at the National Council for Higher Education. She holds a Ph.D. from the University of Oulu, Finland.',institutionString:"Swedish Association for Distance Education, Sweden",institution:null},editorTwo:null,editorThree:null,series:{id:"24",title:"Sustainable Development",doi:"10.5772/intechopen.100361",issn:null},editorialBoard:[{id:"320585",title:"Ph.D.",name:"Deborah",middleName:null,surname:"Young",slug:"deborah-young",fullName:"Deborah Young",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y00002vZLcTQAW/Profile_Picture_2022-05-10T08:30:47.jpg",institutionString:"Empowering Communities Globally",institution:null},{id:"348038",title:"Associate Prof.",name:"Feyza",middleName:null,surname:"Bhatti",slug:"feyza-bhatti",fullName:"Feyza Bhatti",profilePictureURL:"https://mts.intechopen.com/storage/users/348038/images/system/348038.jpg",institutionString:null,institution:{name:"Girne American University",institutionURL:null,country:{name:"Cyprus"}}},{id:"128665",title:"Prof.",name:"Man-Chung",middleName:null,surname:"Chiu",slug:"man-chung-chiu",fullName:"Man-Chung Chiu",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bR9OrQAK/Profile_Picture_2022-03-09T08:36:59.JPG",institutionString:null,institution:{name:"Beijing Normal University",institutionURL:null,country:{name:"China"}}}]},onlineFirstChapters:{paginationCount:9,paginationItems:[{id:"81493",title:"Rust Disease Classification Using Deep Learning Based Algorithm: The Case of Wheat",doi:"10.5772/intechopen.104426",signatures:"Shivani Sood, Harjeet Singh and Suruchi Jindal",slug:"rust-disease-classification-using-deep-learning-based-algorithm-the-case-of-wheat",totalDownloads:35,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Food Systems Resilience",coverURL:"https://cdn.intechopen.com/books/images_new/10897.jpg",subseries:{id:"91",title:"Sustainable Economy and Fair Society"}}},{id:"81428",title:"Observatory of Sustainable Development in Postgraduate Study Programs in Baja California",doi:"10.5772/intechopen.104641",signatures:"Rodolfo Martinez-Gutierrez, Maria Marcela Solis-Quinteros, Maria Esther Ibarra-Estrada and Angel Ernesto Jimenez-Bernardino",slug:"observatory-of-sustainable-development-in-postgraduate-study-programs-in-baja-california",totalDownloads:8,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Globalization and Sustainability - Recent Advances, New Perspectives and Emerging Issues",coverURL:"https://cdn.intechopen.com/books/images_new/11476.jpg",subseries:{id:"91",title:"Sustainable Economy and Fair Society"}}},{id:"81235",title:"Global Food System Transformation for Resilience",doi:"10.5772/intechopen.102749",signatures:"Jasper Okoro Godwin Elechi, Ikechukwu U. 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Behind these definitions are hidden all the aspects of normal and pathological functioning of all processes that the topic ‘Metabolism’ will cover within the Biochemistry Series. 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Thus proteomics, an area of research that detects all protein forms expressed in an organism, including splice isoforms and post-translational modifications, is more suitable than genomics for a comprehensive understanding of the biochemical processes that govern life. The most common proteomics applications are currently in the clinical field for the identification, in a variety of biological matrices, of biomarkers for diagnosis and therapeutic intervention of disorders. From the comparison of proteomic profiles of control and disease or different physiological states, which may emerge, changes in protein expression can provide new insights into the roles played by some proteins in human pathologies. Understanding how proteins function and interact with each other is another goal of proteomics that makes this approach even more intriguing. Specialized technology and expertise are required to assess the proteome of any biological sample. Currently, proteomics relies mainly on mass spectrometry (MS) combined with electrophoretic (1 or 2-DE-MS) and/or chromatographic techniques (LC-MS/MS). MS is an excellent tool that has gained popularity in proteomics because of its ability to gather a complex body of information such as cataloging protein expression, identifying protein modification sites, and defining protein interactions. 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