Soybeans production
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Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\\n\\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
\\n"}]',published:!0,mainMedia:{caption:"Highly Cited",originalUrl:"/media/original/117"}},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 191 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\nThroughout the years, the list has named a total of 261 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\nReleased this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
\n'}],latestNews:[{slug:"webinar-introduction-to-open-science-wednesday-18-may-1-pm-cest-20220518",title:"Webinar: Introduction to Open Science | Wednesday 18 May, 1 PM CEST"},{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"}]},book:{item:{type:"book",id:"55",leadTitle:null,fullTitle:"Advances in Photodiodes",title:"Advances in Photodiodes",subtitle:null,reviewType:"peer-reviewed",abstract:"Photodiodes, the simplest but most versatile optoelectronic devices, are currently used in a variety of applications, including vision systems, optical interconnects, optical storage systems, photometry, particle physics, medical imaging, etc. Advances in Photodiodes addresses the state-of-the-art, latest developments and new trends in the field, covering theoretical aspects, design and simulation issues, processing techniques, experimental results, and applications. Written by internationally renowned experts, with contributions from universities, research institutes and industries, the book is a valuable reference tool for students, scientists, engineers, and researchers.",isbn:null,printIsbn:"978-953-307-163-3",pdfIsbn:"978-953-51-4512-7",doi:"10.5772/588",price:139,priceEur:155,priceUsd:179,slug:"advances-in-photodiodes",numberOfPages:480,isOpenForSubmission:!1,isInWos:1,isInBkci:!0,hash:"6cdd5e9ee86489b07d6841bf4e4a2eb7",bookSignature:"Gian Franco Dalla Betta",publishedDate:"March 22nd 2011",coverURL:"https://cdn.intechopen.com/books/images_new/55.jpg",numberOfDownloads:72773,numberOfWosCitations:193,numberOfCrossrefCitations:70,numberOfCrossrefCitationsByBook:14,numberOfDimensionsCitations:138,numberOfDimensionsCitationsByBook:19,hasAltmetrics:0,numberOfTotalCitations:401,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 11th 2010",dateEndSecondStepPublish:"June 8th 2010",dateEndThirdStepPublish:"September 13th 2010",dateEndFourthStepPublish:"November 12th 2010",dateEndFifthStepPublish:"January 26th 2011",currentStepOfPublishingProcess:5,indexedIn:"1,2,3,4,5,6,7,8",editedByType:"Edited by",kuFlag:!1,featuredMarkup:null,editors:[{id:"19896",title:"Dr.",name:"Gian-Franco",middleName:null,surname:"Dalla Betta",slug:"gian-franco-dalla-betta",fullName:"Gian-Franco Dalla Betta",profilePictureURL:"https://mts.intechopen.com/storage/users/19896/images/1566_n.jpg",biography:"Gian-Franco Dalla Betta received his M.S. degree in Electronics Engineering from the University of Bologna, Italy, in 1992, and the Ph.D. degree in Microelectronics from the University of Trento, Italy, in 1997. Since 1997 to 2002, he was with the Centre for Scientific and Technological Research (ITC-irst) of Trento, Italy. Since 2002, he has been an Associate Professor of Electronics at the University of Trento, Italy. Since 1994, he has been mainly involved in the development of silicon radiation detectors and optical sensors for high-energy physics experiments and medical imaging applications. On these subjects, he has coauthored more than 230 papers published in international journals and conference proceedings.\nProf. Dalla Betta is a Senior Member of the IEEE. In 2004, he has received a “Certificate for outstanding contributions in the field of nuclear radiation measurements” from the Radiation Instrumentation Steering Committee of the IEEE Nuclear & Plasma Science Society. Since 2008, he has served as an Associate Editor of the IEEE Transactions on Nuclear Science.",institutionString:null,position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"1",institution:null}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"754",title:"Optical Engineering",slug:"optical-engineering"}],chapters:[{id:"14333",title:"Spectral Properties of Semiconductor Photodiodes",doi:"10.5772/15300",slug:"spectral-properties-of-semiconductor-photodiodes",totalDownloads:7664,totalCrossrefCites:5,totalDimensionsCites:7,hasAltmetrics:0,abstract:null,signatures:"Terubumi Saito",downloadPdfUrl:"/chapter/pdf-download/14333",previewPdfUrl:"/chapter/pdf-preview/14333",authors:[{id:"20250",title:"Dr.",name:"Terubumi",surname:"Saito",slug:"terubumi-saito",fullName:"Terubumi Saito"}],corrections:null},{id:"14334",title:"Noise in Electronic and Photonic Devices",doi:"10.5772/15223",slug:"noise-in-electronic-and-photonic-devices",totalDownloads:3320,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:null,signatures:"K. 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They are rich in nutrients such as rich proteins, lipids, and others. Furthermore, soybeans can be eaten after processing in various ways.
Eastern Asian people and particularly Japanese people have eaten soybeans after various stages of processing. Soybean seedlings are eaten in many dishes as bean sprouts. Furthermore, soybeans are eaten as green beans in the pod after boiling, as
After hard tissues in boiled soybeans are crushed and ground physically, the soluble fraction is extracted as soy milk. Soy milk is processed as
Theories about the origin of soybean use and cultivation remain controversial in their details. By some accounts, soybeans used as food originated in the area of Manchuria in China and Siberia in Russia. Alternatively, their use as food originated in southern China [1]. Yet another possible history holds that soybeans were bred from wild soybeans as
In China, the first literal record can be found in a Chinese dictionary published in 100 B.C. The dictionary inserted “
In Japan also, “
Soybeans were produced only in eastern Asia for a long time. In contrast, other cereals such as rice, barley, wheat, and corn have diffused throughout the world. Moreover, it is considered that some other endemic bean or pea or pulse had become cultivated in each area already [1].
For instance, in central Asia, broad beans were cultivated, as were chick peas in India, shell peas in western Asia, and kidney beans and ground peas in North America. Nevertheless, soybeans have been cultivated in the United States as oil seed crops since the 1920s. Furthermore, the crop has begun to be cultivated in Canada and South America. In 2012, approximately 82 million tons of soybeans were harvested, with the United States accounting for 34% of the world production. Brazil harvested approximately 66 million tons that year, accounting for 27% of world production. Argentina harvested approximately 40 million tons, or 17% of world production. Therefore, most soybeans (over 80%) consumed worldwide are now produced and harvested in North and South America [2] (Table 1).
In Japan, soybean production was sufficient to provide for domestic consumption until the Taisho Era [1]. Soybean consumption in Japan has been high, but it decreased after the Taisho Era. In 2013, 30 million tons were consumed, but only 240 thousand tons were harvested domestically. That figure is less than 0.1% of the world production amount. Soybeans used domestically account for 104 thousand tons for feed, 6 thousand tons for seed, and 1.9 million tons for oilseeds, all together accounting for 70% of the 30 million tons consumed. Furthermore, those figures indicate that only 30% of soybeans are used as food. The self-sufficiency ratio of soybeans was 97% in 1947. It decreased gradually to 28% in 1959, 11% in 1965, and 7% in 2013 [3]. The ratios of soybeans used for food are 49% used for
\n\t\t\t\t | \n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t
United States | \n\t\t\t8205 | \n\t\t\t33.9 | \n\t\t
Brazil | \n\t\t\t6585 | \n\t\t\t27.2 | \n\t\t
Argentina | \n\t\t\t4010 | \n\t\t\t16.6 | \n\t\t
India | \n\t\t\t1467 | \n\t\t\t6.1 | \n\t\t
China | \n\t\t\t1305 | \n\t\t\t5.4 | \n\t\t
Canada | \n\t\t\t509 | \n\t\t\t2.1 | \n\t\t
Paraguay | \n\t\t\t434 | \n\t\t\t1.8 | \n\t\t
Uruguay | \n\t\t\t300 | \n\t\t\t1.2 | \n\t\t
Ukraine | \n\t\t\t241 | \n\t\t\t1.0 | \n\t\t
Bolivia | \n\t\t\t206 | \n\t\t\t0.9 | \n\t\t
Russia | \n\t\t\t181 | \n\t\t\t0.7 | \n\t\t
Indonesia | \n\t\t\t84 | \n\t\t\t0.3 | \n\t\t
South Africa | \n\t\t\t65 | \n\t\t\t0.3 | \n\t\t
Nigeria | \n\t\t\t58 | \n\t\t\t0.2 | \n\t\t
North Korea | \n\t\t\t35 | \n\t\t\t0.1 | \n\t\t
Japan | \n\t\t\t24 | \n\t\t\t0.1 | \n\t\t
Myanmar | \n\t\t\t21 | \n\t\t\t0.1 | \n\t\t
Others | \n\t\t\t454 | \n\t\t\t1.9 | \n\t\t
World total | \n\t\t\t24,184 | \n\t\t\t100 | \n\t\t
Soybeans production
Source: http://www.maff.go.jp/j/seisan/ryutu/daizu/d_data/pdf/014.pdf
\n\t\t\t\t | \n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t
Miso paste | \n\t\t\t138 | \n\t\t\t123 | \n\t\t
Soy sauce | \n\t\t\t38 | \n\t\t\t33 | \n\t\t
\n\t\t\t\t | \n\t\t\t494 | \n\t\t\t454 | \n\t\t
Natto | \n\t\t\t137 | \n\t\t\t125 | \n\t\t
Frozen | \n\t\t\t30 | \n\t\t\t20 | \n\t\t
Soy milk | \n\t\t\t19 | \n\t\t\t40 | \n\t\t
Delicatessen of soybean | \n\t\t\t33 | \n\t\t\t30 | \n\t\t
Kinako soy powder | \n\t\t\t17 | \n\t\t\t18 | \n\t\t
Other | \n\t\t\t128 | \n\t\t\t93 | \n\t\t
Total | \n\t\t\t1034 | \n\t\t\t936 | \n\t\t
Changes in amount of soybeans for applications
(Unit: thousand tons)
Ref. http://www.maff.go.jp/j/seisan/ryutu/daizu/d_data/
Soybeans contain 35% protein as storage protein, which is used for nutrition during germination. That storage protein is stored in granules, called protein bodies, of about 5–8 μm diameter. Soluble soy protein is extracted from insoluble protein bodies that are burst during soy milk and
Protein digestibility-corrected amino acid score (PDCAAS) values are used to evaluate the protein quality based on the amino acid requirements of humans and their ability to digest it. It was long thought that the amount of amino acid requirements of humans dictate a low score for soybeans because methionine and cysteine residues, sulfur amino acids, in soybean storage proteins have a low composition. The score was only 86 points based on the amino acid requirements of a developing rat. However, in 1985, the score was modified to 100 points, the same as milk and eggs, based on the amino acid requirements of humans. Soy storage proteins are rich in nutrition for human needs [4].
Throughout the world, the recently improving healthy image of soy protein is interesting. In particular, the health benefits of soy foods attract attention in the United States. Health claims are authorized by the Food and Drug Administration (FDA) in the United States: foods containing 6.25 g of soy protein or more can be said by manufacturers to reduce the risk of heart disease if a consumer ingests 25 g/day of soy protein [5]. In Japan, some soybean containing foods are manufactured as
The taxonomy of soybean storage protein has been conducted according to the sedimentation coefficient by an ultracentrifugal fraction as 2S globulin, 7S globulin, 11S globulin, and 15S globulin. Yamauchi [1] reported details of soybean proteins: 2S globulin contained α-conglycinin, 7S globulin composed with β-conglycinin and γ-conglycinin, and 11S globulin-containing glycinin. In addition, the 11S globulin composes hexamer. It is a 350,000 Da protein. Furthermore, their proteins are composed with five subunits as G1–G5; their subunit was 10 polypeptides as A1a, A2, A1b, A3, A5A4, A4, B2, B1b, B4, and B3. Their polypeptides are combined specifically as A1aB1b, A1bB2, A2B1a, A3B4, and A5A4B3. In fact, β-conglycinin, called 7S globulin, combines a dimer protein and a monomer protein, which are 150,000–200,000 Da, or an average of 180,000 Da. They are composed of three subunits: an α-subunit of 63,000 Da, an α′-subunit of 67,000 Da, and a β-subunit of 48,000 Da. The protein has a low concentration of sulfur amino acids. In particular, the β-subunit does not contain methionine, cysteine, and tryptophan [6].
Soybeans have 20% lipids. The lipid concentration varies among harvested regions. Soybeans harvested in the United States have more lipids than those in China [1]. A main reason is that soybeans there have long been bred and modified to contain high oil concentrations as oilseed.
\n\t\t\t\t | \n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t
Pork fat | \n\t\t\t26.2 | \n\t\t\t13.5 | \n\t\t\t42.9 | \n\t\t\t9 | \n\t\t\t0.3 | \n\t\t
Beef fat | \n\t\t\t38.7 | \n\t\t\t3.8 | \n\t\t\t42.1 | \n\t\t\t2.3 | \n\t\t\t2.4 | \n\t\t
Milk lipid | \n\t\t\t31.1 | \n\t\t\t9.2 | \n\t\t\t21.7 | \n\t\t\t1.6 | \n\t\t\t0.4 | \n\t\t
Soybean oil | \n\t\t\t10.5 | \n\t\t\t3.2 | \n\t\t\t22.3 | \n\t\t\t54.5 | \n\t\t\t8.3 | \n\t\t
Sunflower oil | \n\t\t\ttrace | \n\t\t\t4 | \n\t\t\t27.6 | \n\t\t\t58.3 | \n\t\t\ttrace | \n\t\t
Cotton oil | \n\t\t\t27.3 | \n\t\t\t3.1 | \n\t\t\t16.7 | \n\t\t\t50.4 | \n\t\t\ttrace | \n\t\t
Safflower oil | \n\t\t\t6 | \n\t\t\t3.4 | \n\t\t\t12.2 | \n\t\t\t77 | \n\t\t\t0.3 | \n\t\t
Components of fatty acids in foods (%)
Components of fatty acids in foods shows Table 3. Soy oil comprises a small amount of saturated fatty acids, such as palmitic acid and stearic acid, and large amount of unsaturated fatty acids such as oleic acid, linoleic acid, and linolenic acid. Polyunsaturated fatty acids (PUFAs) containing more than unsaturated bonds are important nutrition as necessary lipids for humans. Soybeans have over 60% PUFA. In particular, one kind of PUFA as linoleic acid contained approximately 54.5%.
Actually, PUFAs in animal lipids have low concentration. Therefore, they are insufficient nutritionally. Saturated fats and unsaturated fats are ideally in the following ratio: saturated–unsaturated (1:2) [1]. Soybean lipids were well known to be much stable against oxidation because they are covered as oil body particle by oleosin and other proteins.
Isoflavone is one kind of flavonoid (Fig. 1). Fabaceae sp. contain high concentrations (Fig. 1).
Isoflavone structure.
Generally, soybeans have totally 12 isoflavones in 3 aglycones, and they have three types of glycosides as glucoside, acetyl-glycoside and malonyl-glycosides: genistein, daidzein, glystein, genistin, daidzin, glycitin, acetyl-genistin, acetyl-daidzin, acetyl-glycitin, malonyl-genistin, malonyl-daidzin and malonyl-glycitin [7]. After soybean consumption, glycoside isoflavone, which is contained in food as soy milk or
Many Japanese and throughout eastern Asia intake isoflavone from soybeans. Some researchers have reported negative opinions about plant estrogen [8]. Isoflavones are produced via phenyl–propanoid pathway from phenylalanine in plants. Two intermediate substances, naringenins, are converted to genistein by two specific enzymes in soybeans: isoflavone synthetase and dehydrogenase. Chalcones are converted to daidzein by three specific enzymes in soybean: chalcone reductase, chalcone isomerase, and isoflavone synthetase. Isoflavone and a similar substance, phytoalexin, are used as antibacterial substances against phytopathogenic fungi and bacteria. In addition, they grow well as root nodule bacteria at the root for nitrogen fixation [9, 10].
Other beans and peas, legumes, have isoflavones: chickpeas have biochanin A [11]; alfalfa has formononetin and coumestrol [12]; and ground peas have genistein [13].
Isoflavones in many plants store glucosyl, malonyl-glucosyl, and acetyl-glucosyl conjugate as hydrophilic substances. After invasion of phytopathogenic fungus and bacteria, the glucosyl conjugate isoflavone is transferred to infested wounds, where it hydrolyzes for phytoalexin [14]. Isoflavone has health functions against climacteric disturbances and type 2 diabetes. In Japan, soybean isoflavones are a
Soy proteins have properties that produce curd to add specific metal ions. The property is applied for
Formation of
Soy milk is an emulsion composing lipid and soy protein, mainly glycinin and β-conglycinin. Actually, 60% of the protein in soy milk protein is composed of these two proteins, and a large size of the protein body was constructed with their proteins and others. Lipid is a triacylglyceride composed of linoleic acid, oleic acid, and phospholipids. Before treating, triacylglyceride is stored in oil bodies in soybeans. During soy milk production, and of course during
This phenomenon induces the charge of protein to dissipate by a combination of phytic acid and bivalent ion. Repulsion among their proteins is decreased. Moreover, the immobilized protein combines with outside layer protein easily around an oil drop [18]. Consequently, the steric network structure of soy protein is formed to gather oil drops with intermediary soy protein. Becoming low pH in soy milk, soluble soy protein becoming dissoluble is taken into the network. The curd produces a hard gel that is water retentive, such that moisture is trapped in the network.
As discussed above, soybean proteins provide rich nutrition [4, 19]. In fact, soymilk consumption is increasing quickly throughout the world because of its health benefits. Moreover, differently from bovine milk, it contains no cholesterol. Yogurt-like foods and cheese-like foods made from soybeans can be consumed by people who are concerned about health issues or allergies related to bovine milk.
It is not yet a viable alternative to dairy foods. For that reason, the commercial use of enzymes such as bromelain, ficin, and papain for the curdling of soybean milk has been unsuccessful [20–22]. The authors have reported that physical properties of soy protein modified by enzyme reactions such as germinated proteolysis in soybeans. Therefore, in this section, along with a report of yeast containing soybean curdling enzyme [23], this investigation was undertaken to screen and identify specific food yeast strains (
The yeast strains (1345 strains) stored in the laboratory were screened using soybean milk agar plate medium. The strains were inoculated by streaking on a plate surface. Then they were incubated at 30°C for 7 days. After cultivation, the clear zone diameter was measured using calipers. Yeast strains that produced a clear zone were selected. Results show that 1242 yeast strains among all 1345 yeast strains produced no clear zone on the plate medium. The yeast strains (42 strains) produced less than 1 mm of a clear zone. Also, 57 yeast strains produced 1.0–5.0 mm; 4 yeast strains produced more than 6 mm.
In the second screening of curdling soybean milk enzyme-producing yeast, the screened strains (103 strains) were inoculated to the soybean milk liquid medium. Purchased soybean milk was added to them aseptically.
The soybean milk medium was incubated at 30°C for 24 h. When curdling occurred, the pH of whey was measured using a pH meter (Horiba Ltd.). Results show that three yeasts curdled at pH greater than 5.90. The media were pH 5.90 (SCY 001), pH 6.05 (SCY 002), and pH 6.38 (SCY003) (Table 4).
\n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t | ||
(++) | \n\t\t\t\t(+) | \n\t\t\t\t(–) | \n\t\t\t\t\n\t\t\t | |
≥6.50 | \n\t\t\t0 | \n\t\t\t0 | \n\t\t\t7 | \n\t\t\t\n\t\t |
6.49–5.90 | \n\t\t\t1 | \n\t\t\t2 | \n\t\t\t43 | \n\t\t\t\n\t\t |
5.89–5.50 | \n\t\t\t0 | \n\t\t\t17 | \n\t\t\t17 | \n\t\t\t\n\t\t |
5.49–5.00 | \n\t\t\t2 | \n\t\t\t11 | \n\t\t\t0 | \n\t\t\t\n\t\t |
≤4.99 | \n\t\t\t3 | \n\t\t\t0 | \n\t\t\t0 | \n\t\t\t\n\t\t |
Curdling soybean milk condition by screened yeast
Initial pH was 6.70. ++, coagulating very well; +, coagulating; –, noncoagulating.
The curd activity of strain SCY003 was the highest among the strains. Therefore, the SCY003 strain was finally screened. Isolated yeasts were classified taxonomically and were identified according to methods described in earlier studies [24].
The morphology was observed by microscope. Their 1.5- to 6.5-μm-long cells were short and ovaloid. The yeast, which buds by multibudding reproduction, does not form pseudomycelia or pellicles on the liquid medium. It forms ascospores. It was identified as
For researching physiological characteristics of the strain, the yeast was inoculated into a yeast nitrogen base medium (Difco Laboratories) adding 0.5% of each carbon source: sugar or organic acid as glucose, galactose, sucrose, maltose, raffinose, trehalose, lactose, melibiose, cellobiose, melezitose, starch, D-xylose, L-arabinose, D-ribose, L-rhamnose, erythritol, D-mannitol, salicin, inositol, dulcitol, ethanol, D-sorbitol, disodium succinate, and trisodium citrate. The yeast was inoculated into yeast carbon base medium (Difco Laboratories) adding sodium nitrate solution.
The glucose, galactose, sucrose, maltose, and raffinose in the medium were fermented as carbon sources using strain SCY003. The yeasts grew in a vitamin-free medium. Furthermore, the strain did not grow in 0.01% cycloheximide. According to the morphological, physiological, and molecular characteristics, it was identified as
For researching molecular biological characteristics of the strain, primers were used for amplification and sequencing of 18S-rRNA-encoding genes. The PCR products were sequenced using a kit (ABI Prism Big Dye Terminator Cycle Sequencing Ready Reaction; Applied Biosystems). Analyses of DNA sequence reactions were performed using a sequencer (3130; Applied Biosystems). The 18S rRNA coding DNA was sequenced. Homology was assessed using the Basic Local Alignment Search Tool (BLAST; http://www.ncbi.nlm.nih.gov/BLAST/).
As a result, the yeast showed homology of 99% with
Enzyme extraction, intercellular, in
Generally, commercial soy milk has dispersion stability attributable to the presence of oleosomes or forming aggregate formation of soy proteins on it [28, 29]. Therefore, no precipitate is produced from commercial soybean milk by low centrifugal gravity as 400×
The precipitation ratio was related with the reaction period, and with the enzyme solution volume. They are mutually correlated:
Curdling soybean milk enzyme activity.
After crude extraction of the enzyme, the enzyme protein was purified using chromatography. After crushing cells and extracting the enzyme, the enzyme was precipitated to between 30% and 40% saturation of ammonium sulfate. After redissolving the precipitate, the solution was dialyzed overnight at 4°C, and they carried out ion-exchange chromatography using a column (25 mm × 300 mm) of DEAE gel. The protein was eluted using a 0- to 1-M NaCl linear gradient. Proteolytic activity and curdling were assayed each fraction. Proteolytic activity was measured in duplicate using a commercial kit fluorescein isothiocyanate-labeled casein (FTC). Fluorescence was measured using a 485-nm excitation wave and a 535-nm emission wave. The proteolytic activity was decided for one unit expressed equal amount of trypsin (1 ng⋅mL–1) doing proteolysis of FTC solution.
After ion chromatography, fractions containing the highest level of activity were pooled and reprecipitated using 80% saturation of ammonium sulfate. After redissolving the precipitate, gel filtration chromatography (10 mm × 350 mm, P-100 gel; Bio-Rad Laboratories Inc., CA, USA) was carried out. Then the molecular weight of the enzyme was analyzed using also the chromatography as various molecular weight standards (myosin, 200 kDa; serum albumin, 66.2 kDa; ovalbumin, 45.0 kDa; trypsin inhibitor, 21.5 kDa).
The results are portrayed in Figs. 4a and 4b. One main curdling activity peak was identified using ion-exchange chromatography. The peak (fraction no. 49) agreed with protein and activity. Furthermore, curdling activity agreed with the same fractions presenting protease activity (fraction no. 49).
(a). Ion-exchange chromatography of soybean milk curdling.
As a result, the larger peak of proteolysis activity was found around fraction number 25, and a small peak was found at fraction number 49. The fraction of the proteolysis enzyme around number 25 was not representative of curdling activity. It is considered that the former fractions are attributable to intense proteolysis enzymes and that the latter fractions are attributable to soybean milk-curdling enzymes.
After reprecipitation, the sample was analyzed using gel filtration chromatography. A peak was found at fraction numbers 11–14. Their fractions agreed with soybean milk curdling activity, proteolytic activity, and protein. This result on their chromatograms demonstrates that protease and soybean milk curdling enzyme have some mutual relation of activity.
After purification, the enzyme protein band was approximately 45 kDa (Fig. 5a), which agrees with data of other proteases. The protease molecular weight was measured using gel filtration chromatography (Fig. 5b). The molecular mass is about 45 kDa. The protease was inferred.
(a). Photograph of SDS-PAGE of soybean curding enzyme. (b). Measurement of molecular weight.
The soy milk curdling enzyme has proteolytic activity. Results suggest that the soy milk curdling enzyme was a proteolysis enzyme. Many researchers have reported protease produced by yeasts as
By contrast, few reports describe intracellular protease producing
Optimum pH, temperature, and stability of the enzyme are presented in Figs. 6a and 6b. Optimum pH was assayed at pH 4.0–8.0 using 50 mM phosphate-citric buffer or phosphate-NaOH. For optimum pH of the enzyme assaying, 0.1 mL of a fluorescein isothiocyanate-labeled casein (FTC) solutions, which dissolved in each phosphate buffer (50 mM, pH 4.0–8.0), and 20 μL of enzyme solution were reacted at 40°C for 60 min. For optimum temperature of the enzyme assaying, FTC solution at pH 7.5 (0.1 mL) and 20 μL of enzyme solution were reacted at 15°C–70°C for 60 min to find optimum temperature. After reaction, fluorescence was measured using a 485-nm excitation wave and a 535-nm emission wave.
The optimum pH for the protease activity as curdling was pH 7.5; the optimum temperature was 50°C. The optimum pH of a bovine milk curdling protease,
(a). Optimum pH of soybean curdling enzyme. (b). Optimum temperature of soybean curdling enzyme.
Park
Effects of metal ions and inhibitors on protease are presented in Table 5. In fact, zinc, copper, and mercury all inhibit protease activity. The amino acid of the active site contains cysteine residue because of inhibition by mercury [39]. Furthermore, EGTA (10 mM) inhibited protease activity (62.0% of relative activity).
\n\t\t\t\t\t \n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t\t\n\t\t\t\t\t | \n\t\t\t
Na+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t101.5 | \n\t\t
K+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t105.9 | \n\t\t
Mn2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t101.9 | \n\t\t
Mg2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t46.2 | \n\t\t
Fe2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t95.4 | \n\t\t
Zn2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t23.6 | \n\t\t
Co2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t47.9 | \n\t\t
Cu2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t17.9 | \n\t\t
Ca2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t100.9 | \n\t\t
Iodo acetate | \n\t\t\t1 mM | \n\t\t\t74.1 | \n\t\t
Hg2+\n\t\t\t | \n\t\t\t1 mM | \n\t\t\t34.1 | \n\t\t
EGTA | \n\t\t\t1 mM | \n\t\t\t101.6 | \n\t\t
EGTA | \n\t\t\t10 mM | \n\t\t\t62.0 | \n\t\t
EDTA | \n\t\t\t1 mM | \n\t\t\t96.1 | \n\t\t
EDTA | \n\t\t\t10 mM | \n\t\t\t89.8 | \n\t\t
NEM | \n\t\t\t1 mM | \n\t\t\t98.5 | \n\t\t
Azid | \n\t\t\t1 mM | \n\t\t\t100.4 | \n\t\t
NBS | \n\t\t\t1 mM | \n\t\t\t97.6 | \n\t\t
Cont. | \n\t\t\t– | \n\t\t\t100.0 | \n\t\t
Effects of metal ion and inhibitor of the protease
The activity was not activated by metal ions, but it was inactivated by mercury. Soybean milk-curdling enzyme [38] was inhibited by zinc ions and mercury ions. These results agree with our data related to zinc and mercury. Its survival activity was 18% by mercury. The protease was not activated by metal ions, which indicates that the protease is not a metalloprotease: a metal-dependent enzyme. The amino acid of active site contains cysteine residue.
The mechanisms of curdling soybean milk protease were investigated. At first, The curdled soybean milk samples with added protease and without protease were treated with sample buffer solution.
Soybean milk was poured into a glass vessel (inner diameter 32 mm, height 45 mm). After 0.1 mL of enzyme solution adding to the soybean milk, or without enzyme 0.1 mL D.W., the mixtures were incubated at 40°C, and they were sampled sequentially; between 4- and 24-h. samples (0.01 mL) were added to 0.01 mL of sample buffer and then heated at 100°C for 3 min. Then samples (10 µl) were added in each well. The samples were electrophoresed on a 12.5% uniform gel at 20 mA.
They were subsequently examined using SDS–PAGE (Fig. 7) of curdled soybeans. The left side lane shows the standard of protein size. The next lane (0 h.) shows soybean milk protein without reaction of protease. The other lanes show soybean milk protein decomposed for 4, 8, 12, 16, and 24 h. Lane 0 h shows the α′- and α-subunits of β-conglycinin (approximately 84–73 kDa), the A3 acidic subunit (approximately 40 kDa), other acidic subunits as A4, A1a, A1b, and A2 (approximately 30–42 kDa) of glycinin, the β subunit (approximately 50 kDa), and basic subunits as B3, B1a, B1b, and B4 (approximately 20 kDa) [40, 41].
Digestion of soy protein during curding by soybean milk curdling enzyme.
The two bands shown as α′ and α disappeared gradually after the reaction, showing the protein band from curd making the protease. In the glycinin subunits, the band of the A3 acidic subunit disappeared completely after 4 h. Furthermore, A4, A1a, A1b, and A2 disappeared to a partial degree same as A3 acidic subunit. Peptides smaller than 20 kDa were detected on the gel. The β-conglycinin as α, α′, and part of glycinin as A3 A4, A1b, and A2 were decomposed. Soybean protein became loosely curdled with the addition of other proteases from microorganisms or plants. The protein was decomposed. The low-molecular-weight peptides increased on the polyacrylamide gel. Generally, 11S glycinin was related to the formation of a stiffer gel. Furthermore, Ono
According to our data, after the curdling soy milk by enzyme, α- and α′-subunits cleaved by the protease easily, whereas basic and β-subunit remained. It is considered that surface proteins as α- and α′-subunits were decomposed easily. Some decomposed subunits such as α, α′, A3, acidic, and basic subunits are regarded as related to the curdling soybean milk.
The enzyme of mechanisms for proteolysis was searched that the enzyme had the peptidase activity as exotype proteolysis activity and protease as endotype proteolysis activity. The synthesis peptide substrates, Z-glutamyl-tyrosine, and casein, FTC, were reacted by the enzymes. Peptidase (carboxypeptidase) activity was determined by the increase in ninhydrin after hydrolysis of benzyloxycarbonyl-glutamyl-tyrosine (pH 8.0) at 40°C.
The results show that the enzyme had 0.14 U⋅mg–1 protein as peptidase activity and 0.55 U⋅mg–1 protein protease as endotype proteolysis activity (data not shown). Results also show that the soybean milk-curdling enzyme as a proteolysis enzyme had endotype proteolysis activity.
Jones
As mechanisms that are closely involved in curdling soybeans, curdled soybean milk by enzyme and glucono-δ-lactone (GDL, 3.0% solution) as control samples were dissolved in chemical solutions. The enzyme solution (0.1 mL) was added to the soybean milk. The mixture was incubated at 40°C for 4 h., or 0.1 mL of glucono-δ-lactone (GDL, 3.0% solution) was added to the soybean milk (1.0 g) and incubated at 80°C for 1 h as control sample. To each of the two curdled soybean milk samples, 9 mL of chemical solution as 2% SDS solution, 4 M urea solution, and 10 mM 2-mercaptoethanol were added. They were held for 1 h at room temperature and were then centrifuged at 4000×
Results show the relative ratio of protein (%); that is, 100% relative ratio represents the amount of protein dissolving no-curdling soy milk in each solution (Fig. 8).
Curdled soy bean milk dissolved in chemical solutions. SCE shows soymilk curdled by enzymes; GDL shows soymilk curdled by glucono δ-lactone.
After dissolving the solutions, curd produced by the enzyme dissolved 47.3% of relative ratio from curd to the 2-mercaptoethanol solutions. That curdled by GDL dissolved 41.6% of relative ratio from the curd to the urea solutions. With urea solution, the curd making the enzyme dissolved 93.8% of relative ratio and GDL dissolved 40.3% of relative ratio. The curd produced by the enzyme can dissolve with urea. Both the curd produced by the enzyme and GDL dissolved with SDS solution. Actually, 2-mercaptoethanol solution cleaves the disulfide bond in protein. The urea solution cleaves the hydrogen bond, and the SDS solution cleaves the hydrophobic bond. That inference agrees with results reported by Yasuda
Next, the effects of the proteolysis enzyme against two protein in soybean, glycinin and β-conglycinin, were researched. Glycinin and β-conglycinin were extracted from commercial soy protein according a process described by Nagano
The data agree with reports in the relevant literature [45, 46, 47]. Bromelain decomposes 11S globulin to curdling. The entire band of acidic subunits and most basic subunits disappeared [46]. Glycinin-rich soybean milk was curdled strongly [47]. However, the enzyme made glycinin curdle without metal ion or GDL. Generally, glycinin is known to contain more sulfur amino acid than β-conglycinin does. According to Fig. 7, soymilk was curdled by a hydrogen bond or hydrophobic bond. Furthermore, some alkaline protease as subtilisin and chymotrypsin cleaves hydrophobic amino acid residue.
Curdling activity against two soy protein as glycinin and β-conglycinin.
The enzyme made curd from soymilk mainly by an enzyme reaction against glycinin. Choi
Soybean milk (10 mL) with 0.01 mL of anti-foam (KM-72F) was poured into a glass cup (32 mm inner diameter, 45 mm height). Then 1.5 mL of enzyme solution was added to the soybean milk. The mixture was incubated at 40°C for 4 h. As a control sample, glucono-δ-lactone (GDL, 0.3%) was added to soybean milk (10 mL) with 0.01 mL of anti-foam (KM-72F) added. Then the mixture was incubated at 80°C for 1 h. The curdled soybean milk samples were held at room temperature for 30 min. The rheological characteristics of enzyme curdling soybean milk were measured directly using a creep meter with a 16-mm-diameter plunger compressing 1 mm s–1 with 80.0%. As a control sample, soybean milk was curdled by GDL, 0.3% at 80°C for 1 h.
The rupture strength of the curdled soybean milk in the cups was measured directly using a creep meter (RE-3305; Yamaden Co. Ltd., Tokyo, Japan) with a 16-mm-diameter plunger compressing 1 mm s–1 with 80.0%.
The stress–strain curves of curdled soybean milk are presented in Fig. 10. The vertical axis shows stress (N⋅m–2), which represents internal forces of the sample curd pushing back against the strain. The horizontal axis shows the strain of the curd. The sample curd strained by the plunger is broken by a force that exceeds a certain force: the breaking point. The breaking load represents the hardness or softness of the curd sample. The breaking strain represents the resilience of the sample curd: a large value signifies a high-resilience sample. Pressure by the plunger was loaded more. Then the curd was broken more heavily. After strain loading, the stress value decreased partly. The brittleness shows a different breaking point with the local minimal value. A large brittleness load shows brittle sample curd. The soybean milk was poured into a glass vessel and then curdled using the respective methods. After curdling, rheological analysis of the sample was conducted using a creep meter without taking out.
Stress–strain curves of curdled soybean milk.
The breaking point of curd curdled using GDL, which is used by many Japanese
By contrast, the breaking point of curd curdled by soy curdling enzymes (SCE) was 58.4% strain. Their breaking stress was 10,930 (N⋅m–2). The brittleness point is 81.2% and 10,200 (N⋅m–2). The brittleness of this curd produced using the enzyme was 730 (N⋅m–2). The curd that used SCE had 1.4 times greater breaking point, shown hardness, than that of the curd produced using the GDL same as the Japanese
Heretofore, Yasuda
It is considered that the curd produced using yeast enzymes was not like
Guo and Ono [47] and Toyokawa
According to this report, the new protease from
Soybeans are a traditional food in eastern Asia, particularly in Japan and China. They were eaten in 100 BC in China. The beans can be processed into
Soy storage proteins mainly comprise two proteins as 7S globulin composed of β-conglycinin and γ-conglycinin and 11S globulin containing glycinin composed of 5 subunits. β-Conglycinin, included in 7S globulin, is composed of three subunits.
To modify the physical properties of soy protein, a new type of enzyme for curdling soybean milk enzyme was purified as an extract from yeast. Yeast producing curdling soybean milk enzyme, the SCY003 strain, was isolated from 1345 yeast strains. According to the morphology, physiology, and molecular and characteristics, SCY003 was identified as
The enzyme cleaved the β-conglycinin as α and α′, and part of glycinin as A3 A4, A1b, and A2 in soy protein by endoproteolysis. Soybean protein became loosely curdled with the addition of other proteases from microorganisms or plants. Soybean milk curdled after cleaving endoproteolysis enzyme in SCY003 strain. The rheological characteristics of enzyme curdling soybean milk, the breaking point, was 58.4% strain; their breaking stress was 10,900 (N⋅m–2); the brittleness point is 81.2% and 10,200 (N⋅m–2). The brittleness of the curd produced using the enzyme was 727 (N⋅m–2). The curd had a sticky and chewy texture and did not resemble
In this way, some properties of soy protein were modified by enzymes, such as decomposing specific subunits in soybeans and making soy milk curdle, which are expected to be applicable for new healthy foods, anti-milk allergy foods, and others.
We thank A-STEP, Adaptable and Seamless Technology, Transfer Program through Target Driven R&D by Japan Science and Technology Agency (JST) (AS231Z00291E) for financial support.
Decontamination is a fundamental requirement for research facilities where pathogen elimination is critical, and laboratory facility managers routinely employ various methods of fumigation or fogging disinfection in the never-ending battle against contamination. Historically, technologies such as chlorine dioxide and formaldehyde gas systems have been applied in these areas for pathogen disinfection. Likewise, high concentration vaporized hydrogen peroxide has also been relied on to achieve similar outcomes. A large percentage of these methods follow a familiar pattern of solution injection, dwell (contact time), evacuation, and validation; however, not every system delivers the same functionality or efficacy. Differences in formula and design influence personnel hours, material compatibility, and risk management.
While effective, these high concentration solutions come with inherent risks to health and safety. A recent innovation significantly lowers the risk of exposure to high-concentration chemicals— an HHP™ system which combines a 7% hydrogen peroxide solution with a calibrated fogging device to deliver a mixture of gaseous and micro aerosolized particles. Studies performed with this technology demonstrate high level pathogen disinfection across a variety of tested viruses, bacteria, and substrates. This chapter will provide readers with a deeper understanding of essential components and considerations when implementing systems for viral decontamination. This chapter introduces the latest evolution in hydrogen peroxide disinfection of viral pathogens to address these challenges: an HHP system using patented Pulse™ technology.
A dichotomy of virology work is the need for both viral presence within the confines of research and the equally consistent need to establish pathogen-free research spaces. Throughout the world, contagious disease through viral contamination is an ever-present concern, and SARS-CoV-2 has brought the need to decontaminate to the forefront of virtually every industry. Scientific industries performing research, manufacturing pharmaceuticals, or providing healthcare services, all employ protocols for the disinfection of their environments in order for safe, successful, timely work to take place. These industries depend upon disinfection chemicals, and perhaps just as importantly the chemical delivery systems, that ensure the integrity of their work, personnel safety, and efficient transition from one research project or product type to the next.
Today, a number of distinct categories are used to classify and understand disinfection methods. Disinfection chemicals are tested with established protocols and classified according to their relative success at eliminating specific pathogens. The
Decontamination | The use of physical and/or chemical means to remove, inactivate, or destroy microbial pathogens (e.g., bloodborne or aerosolized) on a surface or item to the point where they are no longer capable of transmitting infectious particles and the item or surface is rendered safe to handle: however, this definition has been broadened by infection control specialists to include all pathogens and physical spaces (e.g., patient rooms, laboratories, buildings). |
Disinfectant | A substance, or mixture of substances, that destroys or irreversibly inactivates bacteria, fungi, and viruses, but not necessarily bacterial spores or prions, in the inanimate environment. |
Disinfection | A process that destroys pathogens and other microorganisms, except prions, by physical or chemical means. |
High-Level Disinfection | A lethaI process utilizing a sterilant under less than sterilizing conditions (e.g., 10–30 min contact time instead of 6–10 h needed for sterilization). The process kills all forms of microbiaI life except for large numbers of bacterial spores. |
lnactivation | A procedure to render a pathogen non-viable, viral nucleic acid sequences non-infectious, or a toxin non-toxic whiIe retaining characteristic(s) of interest for future use. Methods targeting tropism may be host-specific. |
Sterilization | A physical or chemical process that kills or inactivates all microbial life forms including highly resistant bacterial spores. |
Sterilant | A substance or mixture of substances that destroys or eliminates all forms of microbial life in the inanimate environment including all forms of vegetative bacteria, bacterial spores, fungi, fungal spores, and viruses. |
Validation | Establishment of the performance characteristics of a method and provision of objective evidence that the performance requirements for a specified intended use are fulfilled. |
Aerosol | Particulate matter, solid or liquid, larger than a molecule but small enough to remain suspended in the atmosphere [4]. |
Gas | A substance or matter in a state in which it will expand freely to fill the whole of a container, having no fixed shape (unlike a solid) and no fixed volume (unlike a liquid) [5]. |
Hybrid H2O2 | A mixture of gaseous and micro aerosolized substance which remain suspended in the air to fill the whole container [6] |
Vapor | A substance diffused or suspended in the air, especially one normally Iiquid or solid [7]. |
One growing understanding is that the application method of a disinfectant plays a critical role in the success of the disinfection results. While some of the most common spray and wipe surface disinfectants have been in use for decades, there are challenges to their application which can result in inconsistent or ineffective results. Adequate distribution and required contact time are difficult to achieve on a consistent basis by hand application methods, especially in large spaces with high ceilings and complex surface profiles. These accessibility issues and failures may result in inconsistent and incomplete elimination of surface contamination [13]. To address inherent inconsistencies in manual disinfection and to provide alternative methods of delivery, various technologies have been applied. Those technologies include fumigation with formaldehyde, chlorine dioxide gas, fogging of hydrogen peroxide as vapor, silver hydrogen peroxide systems, and hybrid hydrogen peroxide systems. Their gaseous and vaporous form allows access to, and contact with, surfaces that spray and wipe methods alone often cannot access. Automated systems have taken these chemicals with known disinfectant action and paired them with dispersion devices, aiming to deliver an appropriate contact time and maximize surface exposure. These systems automate much of the disinfection process, helping to remove human error and mitigate safety concerns from contact with potentially caustic chemicals. In particular, H2O2-based systems have become a front-runner among automated high-level disinfection technologies due to H2O2’s effectiveness, material compatibilities, lack of chemical residues, and increased safety over other technologies such as formaldehyde or chlorine dioxide gas [14, 15, 16, 17, 18]. When applied in multiple life science environments, H2O2 fogging is well documented to have efficacy against numerous viral pathogens and has seen a rise in use in environments where thorough efficacy and decontamination of a room and its contents are needed [19, 20, 21, 22].
Anyone who has skinned their knee and poured hydrogen peroxide on the wound to stave off infection is familiar with the use of H2O2 as an antiseptic and anti-bacterial agent. Indeed, hydrogen peroxide is produced naturally in the body, acting as a beacon triggering the accumulation of white blood cells of the immune response [23]. Hydrogen Peroxide was first discovered in 1818 by Louis Jacque Theénard, who described it as ‘eau oxygénéé or water oxygen for its composition containing one more oxygen atom than water [24]. This single oxygen–oxygen or peroxide bond is naturally unstable and prone to decomposition with or without the presence of a catalyst [25]. During decomposition, the active oxygen atom cleaves off, releasing energy and resulting in water and oxygen molecules [26]. The oxidizing activity, resulting from the presence of the extra oxygen atom, is what makes hydrogen peroxide an effective disinfectant. It is the reactive formulation of hydrogen peroxide which causes destruction of pathogens by breaking apart structures, interrupting key functions, causing damage to DNA, and eliminating infectious particles.
One of the biggest challenges to any disinfectant application is ensuring a thorough and consistent disinfectant exposure to contaminated surfaces for an effective contact time. To achieve success, fogging technologies must perform a complicated dance between the amount of chemical injected, temperature, humidity, dew point, and method, all of which can affect efficacy from one application to the next. To answer this need, CURIS System designed and patented the concept of replenishing any naturally decomposing solution and called it Pulse technology, simplifying the complicated balance of a successful disinfection. Combining a 7% hydrogen peroxide solution with a calibrated fogging device, this HHP system delivers hybrid hydrogen peroxide, a mixture of gaseous and micro aerosol particles. While effective in a liquid solution, fogging with hydrogen peroxide in this hybrid form increases the availability of each H2O2 molecule, maximizing oxidation opportunities and leading to the destruction of pathogens on surfaces. Beyond just inactivating pathogens, this oxidation causes a physical destructive action of pathogen components, which further delineates this substance as a decontaminant as defined by the BMBL.
A fundamental distinction of this system is its ability to disperse a lower concentration of 7% hydrogen peroxide at calibrated intervals, maximizing contact time while using less H2O2 to achieve microbicidal efficacy. The HHP device operates by delivering the HHP mixture in a two-part process. First, it fills an enclosure with disinfecting fog to an optimal level for killing pathogens. Second, it maintains the fog at the optimal level without oversaturation by periodically injecting more solution into the space being treated, and thereby prolonging the active contact time of the H2O2 (Figure 1). This not only helps to keep surfaces dry, it also reduces sensitivity to variations in temperature and other factors. One might consider this similar to cruise control in a vehicle—the initial phase continuously revs the engine to get the vehicle up to speed, while the second phase uses the engine just enough to keep it at the cruising speed without exceeding the limit. In the case of disinfection, it means keeping the fog concentration at the optimum “kill” level to achieve efficacy in a relatively short time, yet without exceeding this optimum level to the point where the fog condenses on surfaces in the treatment area.
With a concentration of 7% H2O2, the solution, known as CURoxide™, is below the 8% hazard threshold [27, 28]. Being below the threshold means special shipping considerations are not required. Moreover, this enables safer handling for personnel than the 35–59% H2O2 solutions traditionally employed for fogging applications [18, 29, 30, 31]. Likewise, the 7% solution is safer for laboratory materials than the 28.1–52% concentration of corrosive industrial strength grade hydrogen peroxide [27, 32]. This material safety (compatibility) is perhaps most evident when considering how the hydrogen peroxide concentration of a solution will evolve when the solution transitions through states of matter. Hydrogen peroxide is more resistant to leaving the liquid state and more likely to return to it than the water in the solution. When transitioning from vapor back into liquid, this can result in surface condensation at more than double the initial liquid concentration (Figure 2). At 7% H2O2, the HHP solution remains below the 45% known level of material incompatibility [33].
The levels of particle concentration used in typical high-level disinfection are of particular concern to facility managers. These concerns may be lessened by employing lower particle-producing products. Technologies utilizing formaldehyde, chlorine dioxide, and high concentration H2O2 operate at concentrations as high as 1,400 parts per million (ppm) [34, 35, 36]. By contrast, the HHP 7% solution has a lower operating concentration of approximately 138 ppm [37]. Traditional vaporized approaches require a concentration that is up to 10× higher than the lower 7% H2O2 concentration enables, which accordingly may result in a greater risk to personnel from leakage with typical high concentration systems [38]. This is particularly important because, according to the National Library of Medicine, “Inhalation of vapors from concentrated (greater than 10%) solutions may result in severe pulmonary irritation” [39]. This may be why there is a substantial safety concern among facility managers when it comes to typical fogging approaches, as these approaches utilize caustic chemicals at very high concentrations which are known to penetrate through gaps as small as a keyhole [38, 40].
Roughly the size of a small suitcase, the 36-pound (16 kg) HHP system fogs enclosures from an adjustable stainless-steel nozzle at the top of the unit. It can be wheeled or carried throughout a facility to disinfect a wide variety of spaces, large or small, and its Rotomold design provides durability for long-term use and sturdiness during transport. A push-button design allows users to input area dimensions through the device’s manual digital interface, or users may operate the device remotely via a tablet for touchless disinfection from outside the treatment space. The system self-calculates the cubic footage of the space to be fogged to determine the amount of disinfectant needed, and an indicator light shows users when the appropriate amount of solution has been added to the reservoir. An electronically sequenced A/C electrical outlet provides optional connection for any desired additional equipment.
In a world where everything is documented to defend, reinforce, train, and track information, technologies with the ability to employ these methods are invaluable to present and future decontamination applications. The HHP system incorporates patented smart technology, allowing operation not only from a device interface but also remotely through its control app for phones and tablets (Figure 3). For larger spaces, multiple devices may simultaneously work together via wireless communication to combine their capacities to fill the larger volume without the added complications of cables. Whether used alone or in a network, the fogging device(s) self-calculates the dosage required for a space once dimensions are provided. For each disinfection cycle, a job report is wirelessly generated and saved into a secure data system, providing the facility with trackable records in support of risk management protocols. On-demand training, reference materials, and technical support are also available through this secure data storage system, which includes security codes, usernames, and password protection against unauthorized operation and modifications. These smart technology components give laboratory personnel the ability to remotely operate and monitor the system, lessening concerns affiliated with exposure to high concentrations of H2O2.
The HHP device offers the ability to decontaminate enclosed spaces as large as 14,000 ft3 (396 m3) by itself or wirelessly pair up to 25 devices together to treat spaces as large as 350,000 ft3 (9,911 m3) at once. Although the EPA approvals are for 3,682 ft3 (103 m3) due to the size limitation of the testing laboratory, efficacy of bacterial spores are documented in much larger spaces [41]. The small, compact design also reaches tall ceilings efficaciously, as noted in studies where 6-log10 reductions of
Since many life science facilities are made up of diversely sized spaces and needs, the next generation of Pulse technology device was developed. Retaining the core fogging unit’s design, the new attachment model offers the ability to fog, hand spray, or port in, all from the same unit. This fogging model can disinfect large open spaces with a hand sprayer (with proper personal protective equipment). The device can also port into enclosed spaces, such as labs or mobile equipment, with extension nozzles, or it can connect to various enclosures found within laboratories.
To enable decontamination of small enclosures, the HHP system pairs with a mobile cart designed to attach to biological safety cabinets, isolators, incubators, filters, and filter housings (Figure 4a) [42]. This modular pairing delivers low concentration H2O2 solution to the closed system environment, extracts vapor once decontamination has been achieved, and conditions the space to return it to its normal operating environment. No disassembly of lab equipment is required. The system achieves decontamination of the entire chamber, including filters, and contents. The rolling cart weighs approximately 50 pounds (22 kg) and includes a pullout tray to house the HHP fogging device. For scalable applications, the fogging device can fog a whole laboratory or be coupled to the mobile cart as needed for smaller enclosures.
The HHP system also enables integration with a laboratory or stand-alone chamber. This modular design allows for custom installation into facilities—including integrated nozzles and touchscreen operation—to provide decontamination to these essential spaces (Figure 4b). For facilities requiring unified operation of environmental or electronic controls, the HHP system works in tandem with smart integration technology to provide remote operation, automation, and mounted disinfection for one or more enclosed spaces at a time. Decontamination chamber or washer integration includes cycles of less than 120 minutes, including aeration. This chamber integration enables users to operate the entire chamber from one common point, the display screen. It is suitable for coupling with chambers from a variety of manufacturers.
During the 2020–2021 COVID-19 pandemic, the HHP system was approved by the EPA for use against SARS-CoV-2 through the Emerging Viral Pathogen designation due to its sporicidal efficacy [37]. As a result, the HHP system was used in many different environments as a tool for mitigating risk to personnel, research, and equipment. Healthcare facilities faced with shortages of personal protective equipment (PPE) employed the system to decontaminate and safely reuse PPE until the supply could be reestablished. Life science facilities incorporated the HHP system for decontaminating manufacturing spaces where vaccine work was taking place. The HHP system was also instrumental in multiple military applications, significantly aided by the portable design and accessible use. Some prior and ongoing uses include disinfection of manufacturing facilities with a need for sterilization, sterile processing facilities, drug manufacturing facilities, vivariums, laboratory contents, laboratories with interstitial spaces, laboratory filter housings, compounding pharmacies, surgical suites, healthcare patient rooms, ambulances, equipment for service providers, biological safety cabinets, isolator filters, and gnotobiotics.
Studies performed with Pulse technology demonstrate high-level pathogen disinfection across a variety of tested viruses, bacteria, and bacterial spores. The data presented here include a mixture of peer-reviewed studies, Good Laboratory Practice (GLP)-regulated testing, and real-world applications where disinfection can be further complicated by condition-dependent factors such as biofilms, soil loads, and surface type (porous/non-porous), all of which can protect and harbor infectious pathogens [13, 43]. Across the body of this work, the target of high-level disinfection is not only to reduce the present contamination, but to reduce it sufficiently to prevent an infectious dose or the potential for colony regrowth. The work presented here demonstrates the HHP system’s ability to decontaminate, destroying microbial pathogens. This complete decontamination is critical as any surviving pathogens have the potential to interfere with or invalidate research, contaminate sterile products, and cause health hazards.
When targeting pathogens invisible to the eye, there must be some way to measure the efficacy of disinfection. Employing validation tools gives the ability to verify a disinfection process using living organisms and giving results rooted in science. Though several types of chemical and pH indicators exist, indicators of
Recognizing a disinfectant’s ability to kill less susceptible pathogens as an indicator of broader effectiveness, the EPA offers a variety of specific designations a chemical or system can claim. In 2018, the HHP system was approved for sporicidal classification by the EPA for a 6-log10 reduction of
Norovirus, a single stranded non-enveloped virus of the Caliciviridae family, is a leading cause of acute gastroenteritis in humans. The most common genogroup GII is responsible for 95% of infections, which can have severe and even fatal outcomes in at-risk populations such as young children or the elderly. Norovirus, once present, can become a pervasive problem due to the environmental stability of the virus, low infectious dose, resistance to alcohol and chlorine-based disinfectants, and the potential for prolonged asymptomatic shedding of infected individuals. Norovirus is also used as a target organism for testing, as it is considered to be a non-enveloped virus with relatively low susceptibility to disinfectants [48].
In 2018, a 1,600-bed assisted living facility had a norovirus outbreak affecting 1/4 of the residents within a 2-week period with an average of 40 new cases a day, despite protective measures such as the quarantine of afflicted individuals. A bio-decontamination company employing HHP technology was brought into the facility for outbreak response and control. HHP fogging was implemented as part of a 5-point process including continued quarantine and enhanced staff education. After a four-day implementation period, no new cases were reported, effectively ending the outbreak [49].
The HHP system was also tested under GLP conditions for efficacy against the norovirus testing surrogate feline calicivirus [20]. In this testing, 21 inoculated glass agar carrier plates were placed throughout the test room, ranging from floor level to 12 feet (3.6 m) in height, and exposed to the HHP fogging protocols. There was no recovered virus from the challenged plates for an overall reduction of 7.6 log10 (Table 1). Interestingly, efficacious results were also noted in GLP compliant testing when a carrier plate lid was accidentally left on during the HHP fogging cycle. This protocol deviation allowed for the observation that, even under these challenging conditions, the HHP fog migrated underneath the lid and achieved inactivation of viral particles [20].
HHP Efficacy | ||||
---|---|---|---|---|
Pathogen [reference] | Characteristics | Strain/Source | Carrier Type | Results |
Gram-positive, rod-shaped, endospore formation | 19615 | Dacron suture loop Porcelain Penicylinders (50% Tyvek/Tyvek) | 75 of 77 carriers negative 5.2 log10 reduction (Penicylinder) 6.2 log10 reduction (suture) | |
Gram-positive, rod-shaped, endospore formation | 3584 | Dacron suture loop Porcelain Penicylinders (50% Tyvek/Tyvek) | 73 of 74 carriers negative 6.1 log10 reduction (Penicylinder) 6.3 log10 reduction (suture) | |
Gram-positive, rod-shaped, endospore formation | ATCC 7953 | Tyvek/Tyvek stainless steel coupon | 206 carriers negative 6.2 log10 reduction | |
Gram-positive, rod-shaped, endospore formation | ATCC 43598 | Stainless Steel Disk | 90 carriers negative 6.6 log10 reduction | |
Enveloped, icosahedral | phi 6 | Porous N95 Mask | 36 of 37 ≥ 6.0 log10 reduction* | |
Non-enveloped, icosahedral | Unknown | Wild type | 100% reduction of cases | |
Non-enveloped, icosahedral | Strain F-9, ATCC VF-782 | Glass Petri Dish | 40 of 40 plates ≥7.58 log10 reduction | |
Enveloped, icosahedral | Strain F | Porous N95 Mask | 64 of 65 ≥ 5 log10 reduction* | |
Non-enveloped (naked), icosahedral | Strain B3 | Porous N95 Mask | 6o of 63 ≥ 4.3 log10 reduction* | |
Enveloped, no icosahedral capsid | Isolate USA-WA1/2020 | Porous N95 Mask | 48 of 48 reduced below LOD |
The combination of these two studies demonstrates that the HHP system effectively disinfects complex spaces contaminated with norovirus or its surrogates in both laboratory and real-world conditions. Though the assisted living facility case study did not measure a numerical reduction of viral burden, the effective outbreak control of 100% reduction in new cases leads to the conclusion that norovirus was reduced to levels less than the infectious dose.
In the spring/summer of 2020, the COVID-19 pandemic triggered a scarcity, and subsequent shortage of personal protective equipment (PPE) used by hospitals and other healthcare facilities. In an attempt to find ways to mitigate this emergency, researchers at Pennsylvania State University (Penn State) employed HHP to disinfect expired N95 respirators to assess the applicability of the HHP system for this use. Respirators were tested both for any physical degradation effects of the treatment on the respirator material and for efficacy of disinfection of respirator components via inoculation with three viral pathogens and one bacteriophage. Viral work performed at the Eva J Pell Biosafety Level 3 laboratory at Penn State used viruses of different characteristics, as well as a bacteriophage, to represent the range of physical characteristics of pathogens to which healthcare workers may be exposed (Table 1) [19]. Three viruses: herpes simplex virus (HSV-1; enveloped virus; family Herpesviridae), coxsackievirus (CVB3; non-enveloped virus; family Picornaviridae), and SARS-CoV-2 (isolate USA-WA1/2020; enveloped virus; family Coronaviridae), as well as pseudomonas bacteriophage (phi6; enveloped), were chosen for testing (Figure 6). The inside, outside, and strap materials of the respirators were used as inoculation sites. While the majority of these surfaces are made up of porous materials, at least one type of respirator had an outer layer of hydrophobic material which caused the inoculation droplet to dry into a ‘coffee ring’ pattern on the respirator. This testing of porous materials is significant because it presents a more difficult challenge to disinfection than non-porous surfaces, since the materials which absorb the pathogen may also provide a degree of protection, at least temporarily [51]. Disinfectant efficacy testing is commonly done on non-porous surfaces, which does not reflect the difficulty and variables that porous surfaces present.
Testing performed at Penn State also included the use of biological indicators as validation of the protocol for a successful HHP cycle. For each HHP cycle, 6 to 12 biological indicators (
The EPA and the Centers for Disease Control and Prevention (CDC) recognize that certain microorganisms can be ranked with respect to their tolerance to chemical disinfectants [7]. As a result, efficacy against less susceptible bacterial spores can be extrapolated to indicate efficacy against more susceptible microorganisms, including enveloped and non-enveloped viruses [8, 9, 52].
To assess efficacy within various Biosafety Level 3 Agricultural (BSL-3Ag) environments, Kansas State University challenged the HHP system within their Biosecurity Research Institute, a BSL-3Ag facility. Testing was performed in three laboratories representing a range of sizes: 2,281 ft3 (65 m3), 4,668 ft3 (132 m3), and 44,212 ft3 (1,252 m3). Each of the two smaller laboratories were tested over a series of three disinfection cycles with biological indicators of
Within the largest space tested, the 44,212 ft3 (1,252 m3) necropsy laboratory, four HHP devices were used for the disinfection cycle. The smart technology of the HHP system automated the connection of multiple Pulse fogging devices for a synchronized, custom-calibrated, HHP cycle. A total of 206 biological indicators were tested over two HHP cycles in locations throughout the laboratory, including at the 21-ft (6.4 m) ceiling height, soft-sided anteroom, walk-in cooler, and change rooms. All 206 challenged indicators were negative for spore growth, demonstrating a greater than 6-log10 reduction of
The BMBL (6th edition) defines sterilization as; “a physical or chemical process that kills or inactivates all microbial life forms including highly resistant bacterial spores.” The importance of sterilization is well understood in life science, pharmaceutical, and healthcare industries. Through the process of sterilization, researchers and physicians alike establish the basis for reliable and safe protocols and procedures. Standards for fogging sterilization testing are developed by the Association of Official Analytical Chemists (AOAC International), a globally recognized, third party not-for-profit, that provides education and facilitates the development of test methods and standards.
The HHP system was challenged with the Fogging Devices Sterilant Test (OCSPP 810.2100) for efficacy against
Formaldehyde is a naturally occurring compound consisting of hydrogen, oxygen, and carbon which is used as a disinfectant in both its liquid and gaseous states [55]. Used as a laboratory fumigant since the late 19th century, formaldehyde has remained in use due to its efficacy and low cost [56, 57]. For use as a disinfectant, formalin, the aqueous form of formaldehyde, is heated into a vapor producing formaldehyde gas [58]. When encountering microbes, this gas causes a cross-linking of molecules leading to protein clumping and loss of structure [59]. While an effective sterilant, formaldehyde must be handled with extreme care as exposure can cause asthma-like respiratory problems, cancer, or even be fatal to humans [55]. In gaseous form, formaldehyde is used at 8,000–10,000 ppm concentration and leaves behind a residue which must be removed through manual cleaning [56, 60]. Due to the potential health hazards and the required labor-intensive clean-up of residue, formaldehyde use is declining in favor of less hazardous and faster solutions. Indeed, the European Union lists formaldehyde as a substance of very high concern and has issued regulation calling for the progressive substitution when suitable alternatives have been identified [61]. While generally compatible with laboratory materials, formaldehyde can be absorbed into porous materials such as HEPA filters, off-gassing slowly and extending the time needed for safe re-entry [56, 62]. Formaldehyde production equipment ranges from as small as an electric fry pan requiring timers or externally controlled circuits to larger automated devices roughly the size of a household refrigerator and weighing approximately 396 pounds (180 kg) [63].
Chlorine dioxide (ClO2) is a synthetic, green-colored gas that gives off a bleach-like odor. Despite the familiar scent, chlorine dioxide gas is toxic and must be carefully contained when employed as a fumigant [64]. Consisting of unstable chlorine (Cl2) and oxygen molecules (O2), ClO2 disassociates when heated into chloride (Cl-), chlorite (ClO-) and chlorate ions (ClO3-). Some formulations can leave residues of sodium chlorite or inert salts, such as sodium chloride, on surfaces [65]. The disinfection cycle for ClO2 commonly consists of five steps: pre-conditioning, conditioning, charge (gas injection), exposure (contact time), and aeration [66]. The cycle is humidity-dependent, requiring a dosage increase of approximately 500 ppm for each 10% change in humidity, leading to an operating concentration range of 600–1550 ppm [66]. Similar to formaldehyde, ClO2 can be absorbed into porous surfaces and thus take longer to aerate than non-porous materials [65]. One consideration for system use is material compatibility with laboratory equipment. Some device manufacturers recommend that the ClO2-generating equipment remain outside the space being disinfected to prevent repeated exposure [34]. Instable in solution, chlorine dioxide must be mixed on-site by laboratory personnel. The effectiveness of ClO2 in penetrating treated spaces may also cause concern for personnel safety, as it can migrate out of seemingly enclosed spaces [38, 40]. As a result, facilities employing ClO2 systems must carefully monitor the disinfection cycle to ensure safety [64]. Roughly the size of an office bookcase and weighing approximately 230 pounds (104 kg), one system can treat up to 70,000 ft3 (2,000 m3) which may maximize the treatment space per device compared to other systems. ClO2 can also be dispensed from smaller devices which fit into a biological safety cabinet to treat that equipment [67, 68].
High concentration H2O2 devices are roughly the size of a medium file cabinet, wheeled around facilities on four castors and can be very heavy, weighing up to 500 pounds (227 kg). They are operated via touchscreen displays and the range of treatment area is between 8,800 to 20,000 ft3 (249 to 566 m3), depending on the device. One system can connect up to 10 devices via ethernet cables linking one device to another and enabling the treatment of larger spaces. Validation of these vaporous systems is determined using chemical and biological indicators, often
High concentration vaporous H2O2 systems traditionally employ a 35–59% H2O2 liquid solution, heated to a vaporous state [29]. These chemicals must be handled with care, since human contact with the liquid or vapor can be harmful and has been known to result in second- and third-degree burns [29, 30, 31]. Once heated, these chemicals are delivered to the treatment space, where vapor concentrations can reach peak levels of up to 1,400 ppm H2O2 [36], often necessitating precise operating conditions and continuous monitoring of the treatment cycle by the operator(s). A myriad of sensors precisely measures peak concentrations and these aid in delivering a specific combination of conditions to result in efficacy. These systems can be highly complex, accompanied by user manuals nearing a hundred pages of instructions. The four-part fogging process—dehumidification, conditioning, decontamination, and aeration—may require a technician to be present during the entire cycle of several hours [34, 69]. One reason for this vigilant monitoring may be to respond quickly should the system over or under deliver the high concentrations of H2O2 required. Another reason for persistent oversight may be a valid fear of escaped H2O2 vapor, which could migrate out of the treated space at high concentrations and affect personnel [38, 40].
Chemical solutions, even within the range of H2O2 technologies, differ not only in concentration, but also in their formulation. Some available H2O2 solutions contain additional active ingredients, such as the heavy metal silver nitrate [70]. Although silver has a long history of use in wound care, it is also known to cause a permanent retention of silver once in the body [71]. Silver ions are one of the most toxic known forms of heavy metal [70]. Accidental ingestion of these invisible silver residues can cause problems for the microbiome of the human digestive system, since these metals lack the ability to differentiate beneficial bacteria from pathogenic bacteria [72]. Silver persists not only in the body, but also in the environment, where it remains toxic and can be lethal to organisms [70]. As a result of a growing understanding of these unintended negative consequences, the use of silver for disinfection is regulated by the European Union (BPR, Regulation (EU) 528/2012) which states that “It may unnecessarily expose humans, animals and the environment to biocidal active substance, generate health and/or environmental risks and impacts, and may also contribute to the development of resistance to biocides leading to other health and/or environmental issues” [73]. Likewise the EPA acknowledges the potential health hazards related to exposure to silver, and has issued cautionary documents to this effect [74]. Due to the high level of potential exposure during residue cleanup, and the resulting inhalation or dermal absorption of this heavy metal, proper protocols and control should be always employed [74]. Devices for aerosolizing H2O2 with silver vary in size from toolbox-sized fixed systems in mobile transportation to large, stand-alone portable systems. Some of these systems spray in a mist, while others use a more wet delivery method which may impede the generation of floating aerosols [75].
There are several key elements to consider when deciding on a decontamination system. An ideal anti-microbial disinfectant should have the following characteristics: (1) is destructive to the greatest variety of pathogens, including bacterial spores, bacteria, viruses, molds, and fungi; (2) minimizes risks to personnel; (3) is non-corrosive and compatible with materials under normal application conditions; (4) is easy to implement; (5) imparts no harmful residue to the laboratory space or equipment; and (6) provides affordable decontamination. When comparing various disinfection systems, consider the most pertinent aspects below:
First and foremost, it is important for the system to not only be efficacious against more susceptible organisms, but efficacious against less susceptible organisms to the degree necessary to confidently implement the system as a regular component of the research cycle. Commensurate with the definitions of disinfection and decontamination [1], disinfection inactivates pathogens, while decontamination goes to the further degree of inactivating and denaturing them. In industries where pathogen-free environments form the foundational block for successful research, only decontamination will suffice. A detail-conscious manager should not only look for a decontaminant but select one which can demonstrate proof of efficacy with both porous and non-porous surfaces, most accurately representing the array found within life science sectors. Further supporting efficacy, laboratories should be able to validate their chosen system using biological indicators in adherence to international standards [44]. In support of risk management, the system should enable validation of sterilization through a 6-log10 sporicidal reduction that can be tracked and recorded [2]. With only the most efficacious systems under consideration, facility managers should evaluate each system’s impact on personnel safety, ideal laboratory operation, equipment material compatibility, and integrity of research.
Even more important than the safety of materials is the safety of personnel, which should be a top priority when implementing a decontamination system. Safety should be considered from the perspective of normal operation as well as in the event of an accidental exposure. Under normal conditions, devices which can be operated remotely create a layer of isolation between the decontamination system and the human operator, allowing for implementation without direct contact for personnel. In the unlikely event of an accidental exposure, higher concentration solutions may come with risks for exposure to high-consequence chemicals either from contact or inhalation [39]. Choosing a product with lower operating concentrations may likewise decrease the potential for risks associated with accidental exposure caused by unintended fog leakage [38, 40]. As with most gaseous systems, the Occupational Safety and Health Administration (OSHA) has defined a minimum reoccupation level, Permissible Exposure Limit (PEL), which must be considered: ClO2 = 0.1 ppm; H2O2 = 1 ppm; and formaldehyde = 0.75 ppm. Technologies employing lower operational ppm may reach reoccupation levels more quickly due to a lower peak threshold [15, 16, 76].
Decontamination within facilities is a recurring need, so both the physical devices as well as the chemicals or solutions used in them should be reviewed for the consequences of regular use. Devices with instructions requiring the operating machinery to remain outside of the room being disinfected may call into question the safety of exposed laboratory equipment within this space [34]. Likewise, systems with operating concentrations that can condense at levels beyond known material compatibility, such as 45% hydrogen peroxide, may also damage laboratory equipment [33].
Decision makers should critically examine the number of parts necessary for implementing a system. Multiple components may appear to create value but instead may only introduce complication and risks. Hosing laying on the floor add contamination risk in two ways: (1) hoses may impede a complete disinfection of any surfaces they touch and (2) those same hoses may contribute to cross contamination as they are moved throughout the facility. Additionally, a system with many components also comes with many opportunities to misplace or damage a critical element, potentially disrupting scheduled disinfection cycles. Quality and durability of the equipment is paramount as well.
While not strictly required, the degree of support available also contributes to the ease of use of a system. Whether creating new protocols, training personnel, or troubleshooting unique challenges, ensuring there is a commitment from the vendor to provide support can mean the difference between a quick phone call or time spent deciphering a 100-page manual.
Besides providing ease of use, the optimal disinfectant will also be free of byproducts which can leave precipitates or residues behind on the treated surfaces, or damage those surfaces [56, 65, 73, 74]. Additives such as metals are often marketed as beneficial catalysts, yet any benefit imparted can be overshadowed by what is left behind. Any disinfection system should benefit the facility by controlling contaminants, rather than introducing them to sensitive laboratory environments. It is essential for the integrity of research that no residual components be left in a space perceived sterile which can interfere with, invalidate, or otherwise impact the scientific work taking place.
As cost-cutting measures within laboratory spaces continue to be important, one way to save money is to choose a system that can readily be operated in-house by personnel who feel safe doing so. Outsourcing can be associated with significantly higher costs. Systems that are safer, scalable, trackable, easy to use, and modular can be employed for more than one application, resulting in even more cost savings.
When striving to meet strict viral disinfection requirements yet achieve balance with ease of use, timeliness, and safety requirements, facility managers should assess the disinfection needs of individual laboratory environments and the facility as a whole. Ideal disinfection systems should include technologies that have the ability to achieve validated decontamination with the lowest risk to equipment and personnel. We believe that the Hybrid Hydrogen Peroxide system introduced and discussed in detail here merits consideration as a versatile tool for viral disinfection. Pulse technology provides an unexpected efficacy with a 7% H2O2 solution equaling the best commercially available high-concentration H2O2 systems. The simplicity of one portable device with optional accessories and integration capabilities offers intriguing possibilities for reaching and decontaminating viral pathogens that may be found in the myriad of spaces within laboratory environments. Although conceived with sterilization efficacy in mind, its simplicity of use and safer operation enabled widespread adoption into multiple markets such as education and the military, with applicators ranging from entry level technicians to experienced personnel. As research continues to venture into unknown territories, awareness of potential viral threats has increased as well. Current adoption into the life sciences field is robust and underscores the value which can be added through implementing a targeted yet versatile system for facility decontamination. This chapter provides encouragement that innovations in disinfection technology, such as the HHP system, continue to keep pace with these viral threats with fact-based, science-driven results.
The authors would like to thank Jodi Woodson and Alyssa DeLotte for their invaluable contributions to this chapter.
This is a brief overview of the main steps involved in publishing with IntechOpen Compacts, Monographs and Edited Books. Once you submit your proposal you will be appointed a Author Service Manager who will be your single point of contact and lead you through all the described steps below.
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\n\nPlease complete the publishing proposal form. The completed form should serve as an overview of your future Compacts, Monograph or Edited Book. Once submitted, your publishing proposal will be sent for evaluation, and a notice of acceptance or rejection will be sent within 10 to 30 working days from the date of submission.
\n\n2. SUBMIT YOUR MANUSCRIPT
\n\nAfter approval, you will proceed in submitting your full-length manuscript. 50-130 pages for compacts, 130-500 for Monographs & Edited Books.Your full-length manuscript must follow IntechOpen's Author Guidelines and comply with our publishing rules. Once the manuscript is submitted, but before it is forwarded for peer review, it will be screened for plagiarism.
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\n\nExternal reviewers will evaluate your manuscript and provide you with their feedback. You may be asked to revise your draft, or parts of your draft, provide additional information and make any other necessary changes according to their comments and suggestions.
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\n\nIf the manuscript is formally accepted after peer review you will receive a formal Notice of Acceptance, and a price quote.
\n\nThe Open Access Publishing Fee of your IntechOpen Compacts, Monograph or Edited Book depends on the volume of the publication and includes: project management, editorial and peer review services, technical editing, language copyediting, cover design and book layout, book promotion and ISBN assignment.
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dioxide is a white metal oxide used in many food categories as food additives to provide a whitening effect. If its use complies with the five specifications including synthesis pathway, crystallographic phase, purity, amount and innocuousness, all other parameters are not defined and were hardly documented. However, in the last 3 years, two studies have deeply characterized food-grade TiO2 and converged to the fact that the size distribution of food-grade TiO2 spans over the nanoparticle range (<100 nm) and the surface is not pure TiO2 but covered by phosphate and eventually silicon species or aluminium species, which modify the surface chemistry of these particles. Until now, this material was considered as safe. However, the toxicological studies later to the last re-evaluation by the European Food Safety Agency reveal some concerns due to the ability of TiO2 particles to alter the intestinal barrier. 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He is also a faculty member in the Molecular Oncology Program. He obtained his MSc and Ph.D. at Oregon State University and Texas Tech University, respectively. He pursued his postdoctoral studies at Rutgers University Medical School and the National Institutes of Health (NIH/NIDDK), USA. His research focuses on biochemistry, biophysics, genetics, molecular biology, and molecular medicine with specialization in the fields of drug design, protein structure-function, protein folding, prions, microRNA, pseudogenes, molecular cancer, epigenetics, metabolites, proteomics, genomics, protein expression, and characterization by spectroscopic and calorimetric methods.",institutionString:"University of Health Sciences",institution:null},{id:"180528",title:"Dr.",name:"Hiroyuki",middleName:null,surname:"Kagechika",slug:"hiroyuki-kagechika",fullName:"Hiroyuki Kagechika",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/180528/images/system/180528.jpg",biography:"Hiroyuki Kagechika received his bachelor’s degree and Ph.D. in Pharmaceutical Sciences from the University of Tokyo, Japan, where he served as an associate professor until 2004. He is currently a professor at the Institute of Biomaterials and Bioengineering (IBB), Tokyo Medical and Dental University (TMDU). From 2010 to 2012, he was the dean of the Graduate School of Biomedical Science. Since 2012, he has served as the vice dean of the Graduate School of Medical and Dental Sciences. He has been the director of the IBB since 2020. Dr. Kagechika’s major research interests are the medicinal chemistry of retinoids, vitamins D/K, and nuclear receptors. He has developed various compounds including a drug for acute promyelocytic leukemia.",institutionString:"Tokyo Medical and Dental University",institution:{name:"Tokyo Medical and Dental University",country:{name:"Japan"}}},{id:"94311",title:"Prof.",name:"Martins",middleName:"Ochubiojo",surname:"Ochubiojo Emeje",slug:"martins-ochubiojo-emeje",fullName:"Martins Ochubiojo Emeje",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/94311/images/system/94311.jpeg",biography:"Martins Emeje obtained a BPharm with distinction from Ahmadu Bello University, Nigeria, and an MPharm and Ph.D. from the University of Nigeria (UNN), where he received the best Ph.D. award and was enlisted as UNN’s “Face of Research.” He established the first nanomedicine center in Nigeria and was the pioneer head of the intellectual property and technology transfer as well as the technology innovation and support center. Prof. Emeje’s several international fellowships include the prestigious Raman fellowship. He has published more than 150 articles and patents. He is also the head of R&D at NIPRD and holds a visiting professor position at Nnamdi Azikiwe University, Nigeria. He has a postgraduate certificate in Project Management from Walden University, Minnesota, as well as a professional teaching certificate and a World Bank certification in Public Procurement. Prof. Emeje was a national chairman of academic pharmacists in Nigeria and the 2021 winner of the May & Baker Nigeria Plc–sponsored prize for professional service in research and innovation.",institutionString:"National Institute for Pharmaceutical Research and Development",institution:{name:"National Institute for Pharmaceutical Research and Development",country:{name:"Nigeria"}}},{id:"268659",title:"Ms.",name:"Xianquan",middleName:null,surname:"Zhan",slug:"xianquan-zhan",fullName:"Xianquan Zhan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/268659/images/8143_n.jpg",biography:"Dr. Zhan received his undergraduate and graduate training in the fields of preventive medicine and epidemiology and statistics at the West China University of Medical Sciences in China during 1989 to 1999. He received his post-doctoral training in oncology and cancer proteomics for two years at the Cancer Research Institute of Human Medical University in China. In 2001, he went to the University of Tennessee Health Science Center (UTHSC) in USA, where he was a post-doctoral researcher and focused on mass spectrometry and cancer proteomics. Then, he was appointed as an Assistant Professor of Neurology, UTHSC in 2005. He moved to the Cleveland Clinic in USA as a Project Scientist/Staff in 2006 where he focused on the studies of eye disease proteomics and biomarkers. He returned to UTHSC as an Assistant Professor of Neurology in the end of 2007, engaging in proteomics and biomarker studies of lung diseases and brain tumors, and initiating the studies of predictive, preventive, and personalized medicine (PPPM) in cancer. In 2010, he was promoted to Associate Professor of Neurology, UTHSC. Currently, he is a Professor at Xiangya Hospital of Central South University in China, Fellow of Royal Society of Medicine (FRSM), the European EPMA National Representative in China, Regular Member of American Association for the Advancement of Science (AAAS), European Cooperation of Science and Technology (e-COST) grant evaluator, Associate Editors of BMC Genomics, BMC Medical Genomics, EPMA Journal, and Frontiers in Endocrinology, Executive Editor-in-Chief of Med One. He has\npublished 116 peer-reviewed research articles, 16 book chapters, 2 books, and 2 US patents. His current main research interest focuses on the studies of cancer proteomics and biomarkers, and the use of modern omics techniques and systems biology for PPPM in cancer, and on the development and use of 2DE-LC/MS for the large-scale study of human proteoforms.",institutionString:null,institution:{name:"Xiangya Hospital Central South University",country:{name:"China"}}},{id:"40482",title:null,name:"Rizwan",middleName:null,surname:"Ahmad",slug:"rizwan-ahmad",fullName:"Rizwan Ahmad",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/40482/images/system/40482.jpeg",biography:"Dr. Rizwan Ahmad is a University Professor and Coordinator, Quality and Development, College of Medicine, Imam Abdulrahman bin Faisal University, Saudi Arabia. Previously, he was Associate Professor of Human Function, Oman Medical College, Oman, and SBS University, Dehradun. Dr. Ahmad completed his education at Aligarh Muslim University, Aligarh. He has published several articles in peer-reviewed journals, chapters, and edited books. His area of specialization is free radical biochemistry and autoimmune diseases.",institutionString:"Imam Abdulrahman Bin Faisal University",institution:{name:"Imam Abdulrahman Bin Faisal University",country:{name:"Saudi Arabia"}}},{id:"41865",title:"Prof.",name:"Farid A.",middleName:null,surname:"Badria",slug:"farid-a.-badria",fullName:"Farid A. Badria",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/41865/images/system/41865.jpg",biography:"Farid A. Badria, Ph.D., is the recipient of several awards, including The World Academy of Sciences (TWAS) Prize for Public Understanding of Science; the World Intellectual Property Organization (WIPO) Gold Medal for best invention; Outstanding Arab Scholar, Kuwait; and the Khwarizmi International Award, Iran. He has 250 publications, 12 books, 20 patents, and several marketed pharmaceutical products to his credit. He continues to lead research projects on developing new therapies for liver, skin disorders, and cancer. Dr. Badria was listed among the world’s top 2% of scientists in medicinal and biomolecular chemistry in 2019 and 2020. He is a member of the Arab Development Fund, Kuwait; International Cell Research Organization–United Nations Educational, Scientific and Cultural Organization (ICRO–UNESCO), Chile; and UNESCO Biotechnology France",institutionString:"Mansoura University",institution:{name:"Mansoura University",country:{name:"Egypt"}}},{id:"329385",title:"Dr.",name:"Rajesh K.",middleName:"Kumar",surname:"Singh",slug:"rajesh-k.-singh",fullName:"Rajesh K. Singh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/329385/images/system/329385.png",biography:"Dr. Singh received a BPharm (2003) and MPharm (2005) from Panjab University, Chandigarh, India, and a Ph.D. (2013) from Punjab Technical University (PTU), Jalandhar, India. He has more than sixteen years of teaching experience and has supervised numerous postgraduate and Ph.D. students. He has to his credit more than seventy papers in SCI- and SCOPUS-indexed journals, fifty-five conference proceedings, four books, six Best Paper Awards, and five projects from different government agencies. He is currently an editorial board member of eight international journals and a reviewer for more than fifty scientific journals. He received Top Reviewer and Excellent Peer Reviewer Awards from Publons in 2016 and 2017, respectively. He is also on the panel of The International Reviewer for reviewing research proposals for grants from the Royal Society. He also serves as a Publons Academy mentor and Bentham brand ambassador.",institutionString:"Punjab Technical University",institution:{name:"Punjab Technical University",country:{name:"India"}}},{id:"142388",title:"Dr.",name:"Thiago",middleName:"Gomes",surname:"Gomes Heck",slug:"thiago-gomes-heck",fullName:"Thiago Gomes Heck",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/142388/images/7259_n.jpg",biography:null,institutionString:null,institution:{name:"Universidade Regional do Noroeste do Estado do Rio Grande do Sul",country:{name:"Brazil"}}},{id:"336273",title:"Assistant Prof.",name:"Janja",middleName:null,surname:"Zupan",slug:"janja-zupan",fullName:"Janja Zupan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/336273/images/14853_n.jpeg",biography:"Janja Zupan graduated in 2005 at the Department of Clinical Biochemistry (superviser prof. dr. Janja Marc) in the field of genetics of osteoporosis. Since November 2009 she is working as a Teaching Assistant at the Faculty of Pharmacy, Department of Clinical Biochemistry. In 2011 she completed part of her research and PhD work at Institute of Genetics and Molecular Medicine, University of Edinburgh. She finished her PhD entitled The influence of the proinflammatory cytokines on the RANK/RANKL/OPG in bone tissue of osteoporotic and osteoarthritic patients in 2012. From 2014-2016 she worked at the Institute of Biomedical Sciences, University of Aberdeen as a postdoctoral research fellow on UK Arthritis research project where she gained knowledge in mesenchymal stem cells and regenerative medicine. She returned back to University of Ljubljana, Faculty of Pharmacy in 2016. She is currently leading project entitled Mesenchymal stem cells-the keepers of tissue endogenous regenerative capacity facing up to aging of the musculoskeletal system funded by Slovenian Research Agency.",institutionString:null,institution:{name:"University of Ljubljana",country:{name:"Slovenia"}}},{id:"357453",title:"Dr.",name:"Radheshyam",middleName:null,surname:"Maurya",slug:"radheshyam-maurya",fullName:"Radheshyam Maurya",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/357453/images/16535_n.jpg",biography:null,institutionString:null,institution:{name:"University of Hyderabad",country:{name:"India"}}},{id:"418340",title:"Dr.",name:"Jyotirmoi",middleName:null,surname:"Aich",slug:"jyotirmoi-aich",fullName:"Jyotirmoi Aich",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000038Ugi5QAC/Profile_Picture_2022-04-15T07:48:28.png",biography:"Biotechnologist with 15 years of research including 6 years of teaching experience. Demonstrated record of scientific achievements through consistent publication record (H index = 13, with 874 citations) in high impact journals such as Nature Communications, Oncotarget, Annals of Oncology, PNAS, and AJRCCM, etc. Strong research professional with a post-doctorate from ACTREC where I gained experimental oncology experience in clinical settings and a doctorate from IGIB where I gained expertise in asthma pathophysiology. A well-trained biotechnologist with diverse experience on the bench across different research themes ranging from asthma to cancer and other infectious diseases. An individual with a strong commitment and innovative mindset. Have the ability to work on diverse projects such as regenerative and molecular medicine with an overall mindset of improving healthcare.",institutionString:"DY Patil Deemed to Be University",institution:null},{id:"349288",title:"Prof.",name:"Soumya",middleName:null,surname:"Basu",slug:"soumya-basu",fullName:"Soumya Basu",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000035QxIDQA0/Profile_Picture_2022-04-15T07:47:01.jpg",biography:"Soumya Basu, Ph.D., is currently working as an Associate Professor at Dr. D. Y. Patil Biotechnology and Bioinformatics Institute, Dr. D. Y. Patil Vidyapeeth, Pune, Maharashtra, India. With 16+ years of trans-disciplinary research experience in Drug Design, development, and pre-clinical validation; 20+ research article publications in journals of repute, 9+ years of teaching experience, trained with cross-disciplinary education, Dr. Basu is a life-long learner and always thrives for new challenges.\r\nHer research area is the design and synthesis of small molecule partial agonists of PPAR-γ in lung cancer. She is also using artificial intelligence and deep learning methods to understand the exosomal miRNA’s role in cancer metastasis. Dr. Basu is the recipient of many awards including the Early Career Research Award from the Department of Science and Technology, Govt. of India. She is a reviewer of many journals like Molecular Biology Reports, Frontiers in Oncology, RSC Advances, PLOS ONE, Journal of Biomolecular Structure & Dynamics, Journal of Molecular Graphics and Modelling, etc. She has edited and authored/co-authored 21 journal papers, 3 book chapters, and 15 abstracts. She is a Board of Studies member at her university. She is a life member of 'The Cytometry Society”-in India and 'All India Cell Biology Society”- in India.",institutionString:"Dr. D.Y. Patil Vidyapeeth, Pune",institution:{name:"Dr. D.Y. Patil Vidyapeeth, Pune",country:{name:"India"}}},{id:"354817",title:"Dr.",name:"Anubhab",middleName:null,surname:"Mukherjee",slug:"anubhab-mukherjee",fullName:"Anubhab Mukherjee",position:null,profilePictureURL:"https://intech-files.s3.amazonaws.com/0033Y0000365PbRQAU/ProfilePicture%202022-04-15%2005%3A11%3A18.480",biography:"A former member of Laboratory of Nanomedicine, Brigham and Women’s Hospital, Harvard University, Boston, USA, Dr. Anubhab Mukherjee is an ardent votary of science who strives to make an impact in the lives of those afflicted with cancer and other chronic/acute ailments. He completed his Ph.D. from CSIR-Indian Institute of Chemical Technology, Hyderabad, India, having been skilled with RNAi, liposomal drug delivery, preclinical cell and animal studies. He pursued post-doctoral research at College of Pharmacy, Health Science Center, Texas A & M University and was involved in another postdoctoral research at Department of Translational Neurosciences and Neurotherapeutics, John Wayne Cancer Institute, Santa Monica, California. In 2015, he worked in Harvard-MIT Health Sciences & Technology as a visiting scientist. He has substantial experience in nanotechnology-based formulation development and successfully served various Indian organizations to develop pharmaceuticals and nutraceutical products. He is an inventor in many US patents and an author in many peer-reviewed articles, book chapters and books published in various media of international repute. Dr. Mukherjee is currently serving as Principal Scientist, R&D at Esperer Onco Nutrition (EON) Pvt. Ltd. and heads the Hyderabad R&D center of the organization.",institutionString:"Esperer Onco Nutrition Pvt Ltd.",institution:null},{id:"319365",title:"Assistant Prof.",name:"Manash K.",middleName:null,surname:"Paul",slug:"manash-k.-paul",fullName:"Manash K. Paul",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/319365/images/system/319365.png",biography:"Manash K. Paul is a Principal Investigator and Scientist at the University of California Los Angeles. He has contributed significantly to the fields of stem cell biology, regenerative medicine, and lung cancer. His research focuses on various signaling processes involved in maintaining stem cell homeostasis during the injury-repair process, deciphering lung stem cell niche, pulmonary disease modeling, immuno-oncology, and drug discovery. He is currently investigating the role of extracellular vesicles in premalignant lung cell migration and detecting the metastatic phenotype of lung cancer via machine-learning-based analyses of exosomal signatures. Dr. Paul has published in more than fifty peer-reviewed international journals and is highly cited. 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He has 60 articles published in scientific journals and 20 poster presentations in scientific congresses. His research interests include physiology, endocrine system, cancer, diabetes, cardiovascular system diseases, and isolated organ bath system studies.",institutionString:"Kafkas University",institution:{name:"Kafkas University",country:{name:"Turkey"}}},{id:"418963",title:"Dr.",name:"Augustine Ododo",middleName:"Augustine",surname:"Osagie",slug:"augustine-ododo-osagie",fullName:"Augustine Ododo Osagie",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/418963/images/16900_n.jpg",biography:"Born into the family of Osagie, a prince of the Benin Kingdom. I am currently an academic in the Department of Medical Biochemistry, University of Benin. 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She is a fellow member of the Royal Society of Chemistry UK and the American Chemical Society of the United States.",institutionString:"King Saud University",institution:{name:"King Saud University",country:{name:"Saudi Arabia"}}},{id:"49848",title:"Dr.",name:"Wen-Long",middleName:null,surname:"Hu",slug:"wen-long-hu",fullName:"Wen-Long Hu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/49848/images/system/49848.jpg",biography:"Wen-Long Hu is Chief of the Division of Acupuncture, Department of Chinese Medicine at Kaohsiung Chang Gung Memorial Hospital, as well as an adjunct associate professor at Fooyin University and Kaohsiung Medical University. Wen-Long is President of Taiwan Traditional Chinese Medicine Medical Association. He has 28 years of experience in clinical practice in laser acupuncture therapy and 34 years in acupuncture. He is an invited speaker for lectures and workshops in laser acupuncture at many symposiums held by medical associations. He owns the patent for herbal preparation and producing, and for the supercritical fluid-treated needle. Dr. Hu has published three books, 12 book chapters, and more than 30 papers in reputed journals, besides serving as an editorial board member of repute.",institutionString:"Kaohsiung Chang Gung Memorial Hospital",institution:{name:"Kaohsiung Chang Gung Memorial Hospital",country:{name:"Taiwan"}}},{id:"298472",title:"Prof.",name:"Andrey V.",middleName:null,surname:"Grechko",slug:"andrey-v.-grechko",fullName:"Andrey V. Grechko",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/298472/images/system/298472.png",biography:"Andrey Vyacheslavovich Grechko, Ph.D., Professor, is a Corresponding Member of the Russian Academy of Sciences. He graduated from the Semashko Moscow Medical Institute (Semashko National Research Institute of Public Health) with a degree in Medicine (1998), the Clinical Department of Dermatovenerology (2000), and received a second higher education in Psychology (2009). Professor A.V. Grechko held the position of Сhief Physician of the Central Clinical Hospital in Moscow. He worked as a professor at the faculty and was engaged in scientific research at the Medical University. Starting in 2013, he has been the initiator of the creation of the Federal Scientific and Clinical Center for Intensive Care and Rehabilitology, Moscow, Russian Federation, where he also serves as Director since 2015. He has many years of experience in research and teaching in various fields of medicine, is an author/co-author of more than 200 scientific publications, 13 patents, 15 medical books/chapters, including Chapter in Book «Metabolomics», IntechOpen, 2020 «Metabolomic Discovery of Microbiota Dysfunction as the Cause of Pathology».",institutionString:"Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology",institution:null},{id:"199461",title:"Prof.",name:"Natalia V.",middleName:null,surname:"Beloborodova",slug:"natalia-v.-beloborodova",fullName:"Natalia V. Beloborodova",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/199461/images/system/199461.jpg",biography:'Natalia Vladimirovna Beloborodova was educated at the Pirogov Russian National Research Medical University, with a degree in pediatrics in 1980, a Ph.D. in 1987, and a specialization in Clinical Microbiology from First Moscow State Medical University in 2004. She has been a Professor since 1996. Currently, she is the Head of the Laboratory of Metabolism, a division of the Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow, Russian Federation. N.V. Beloborodova has many years of clinical experience in the field of intensive care and surgery. She studies infectious complications and sepsis. She initiated a series of interdisciplinary clinical and experimental studies based on the concept of integrating human metabolism and its microbiota. Her scientific achievements are widely known: she is the recipient of the Marie E. Coates Award \\"Best lecturer-scientist\\" Gustafsson Fund, Karolinska Institutes, Stockholm, Sweden, and the International Sepsis Forum Award, Pasteur Institute, Paris, France (2014), etc. Professor N.V. Beloborodova wrote 210 papers, five books, 10 chapters and has edited four books.',institutionString:"Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology",institution:null},{id:"354260",title:"Ph.D.",name:"Tércio Elyan",middleName:"Azevedo",surname:"Azevedo Martins",slug:"tercio-elyan-azevedo-martins",fullName:"Tércio Elyan Azevedo Martins",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/354260/images/16241_n.jpg",biography:"Graduated in Pharmacy from the Federal University of Ceará with the modality in Industrial Pharmacy, Specialist in Production and Control of Medicines from the University of São Paulo (USP), Master in Pharmaceuticals and Medicines from the University of São Paulo (USP) and Doctor of Science in the program of Pharmaceuticals and Medicines by the University of São Paulo. Professor at Universidade Paulista (UNIP) in the areas of chemistry, cosmetology and trichology. Assistant Coordinator of the Higher Course in Aesthetic and Cosmetic Technology at Universidade Paulista Campus Chácara Santo Antônio. Experience in the Pharmacy area, with emphasis on Pharmacotechnics, Pharmaceutical Technology, Research and Development of Cosmetics, acting mainly on topics such as cosmetology, antioxidant activity, aesthetics, photoprotection, cyclodextrin and thermal analysis.",institutionString:null,institution:{name:"University of Sao Paulo",country:{name:"Brazil"}}},{id:"334285",title:"Ph.D. Student",name:"Sameer",middleName:"Kumar",surname:"Jagirdar",slug:"sameer-jagirdar",fullName:"Sameer Jagirdar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/334285/images/14691_n.jpg",biography:"I\\'m a graduate student at the center for biosystems science and engineering at the Indian Institute of Science, Bangalore, India. 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He has experience teaching DPharm, Pharm.D, BPharm, and MPharm students. He has more than five publications in reputed journals to his credit. Dr. Faheem’s research area is the development and characterization of nanoformulation for the delivery of drugs to various organs.",institutionString:"Integral University",institution:{name:"Integral University",country:{name:"India"}}},{id:"329795",title:"Dr.",name:"Mohd Aftab",middleName:"Aftab",surname:"Siddiqui",slug:"mohd-aftab-siddiqui",fullName:"Mohd Aftab Siddiqui",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/329795/images/system/329795.png",biography:"Dr. Mohd Aftab Siddiqui is an assistant professor in the Faculty of Pharmacy, Integral University, Lucknow, India, where he obtained a Ph.D. in Pharmacology in 2020. He also obtained a BPharm and MPharm from the same university in 2013 and 2015, respectively. His area of research is the pharmacological screening of herbal drugs/natural products in liver cancer and cardiac diseases. He is a member of many professional bodies and has guided many MPharm and PharmD research projects. Dr. Siddiqui has many national and international publications and one German patent to his credit.",institutionString:"Integral University",institution:null},{id:"255360",title:"Dr.",name:"Usama",middleName:null,surname:"Ahmad",slug:"usama-ahmad",fullName:"Usama Ahmad",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/255360/images/system/255360.png",biography:"Dr. Usama Ahmad holds a specialization in Pharmaceutics from Amity University, Lucknow, India. He received his Ph.D. from Integral University, Lucknow, India, with his work titled ‘Development and evaluation of silymarin nanoformulation for hepatic carcinoma’. Currently, he is an Assistant Professor of Pharmaceutics, at the Faculty of Pharmacy, Integral University. He has been teaching PharmD, BPharm, and MPharm students and conducting research in the novel drug delivery domain. From 2013 to 2014 he worked on a research project funded by SERB-DST, Government of India. He has a rich publication record with more than twenty-four original journal articles, two edited books, four book chapters, and several scientific articles to his credit. He is a member of the American Association for Cancer Research, the International Association for the Study of Lung Cancer, and the British Society for Nanomedicine. Dr. Ahmad’s research focus is on the development of nanoformulations to facilitate the delivery of drugs.",institutionString:"Integral University",institution:{name:"Integral University",country:{name:"India"}}},{id:"333824",title:"Dr.",name:"Ahmad Farouk",middleName:null,surname:"Musa",slug:"ahmad-farouk-musa",fullName:"Ahmad Farouk Musa",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/333824/images/22684_n.jpg",biography:"Dato’ Dr Ahmad Farouk Musa\nMD, MMED (Surgery) (Mal), Fellowship in Cardiothoracic Surgery (Monash Health, Aust), Graduate Certificate in Higher Education (Aust), Academy of Medicine (Mal)\n\n\n\nDato’ Dr Ahmad Farouk Musa obtained his Doctor of Medicine from USM in 1992. He then obtained his Master of Medicine in Surgery from the same university in the year 2000 before subspecialising in Cardiothoracic Surgery at Institut Jantung Negara (IJN), Kuala Lumpur from 2002 until 2005. He then completed his Fellowship in Cardiothoracic Surgery at Monash Health, Melbourne, Australia in 2008. He has served in the Malaysian army as a Medical Officer with the rank of Captain upon completing his Internship before joining USM as a trainee lecturer. He is now serving as an academic and researcher at Monash University Malaysia. He is a life-member of the Malaysian Association of Thoracic & Cardiovascular Surgery (MATCVS) and a committee member of the MATCVS Database. He is also a life-member of the College of Surgeons, Academy of Medicine of Malaysia; a life-member of Malaysian Medical Association (MMA), and a life-member of Islamic Medical Association of Malaysia (IMAM). Recently he was appointed as an Interim Chairperson of Examination & Assessment Subcommittee of the UiTM-IJN Cardiothoracic Surgery Postgraduate Program. As an academic, he has published numerous research papers and book chapters. He has also been appointed to review many scientific manuscripts by established journals such as the British Medical Journal (BMJ). He has presented his research works at numerous local and international conferences such as the European Association for Cardiothoracic Surgery (EACTS) and the European Society of Cardiovascular Surgery (ESCVS), to name a few. He has also won many awards for his research presentations at meetings and conferences like the prestigious International Invention, Innovation & Technology Exhibition (ITEX); Design, Research and Innovation Exhibition, the National Conference on Medical Sciences and the Annual Scientific Meetings of the Malaysian Association for Thoracic and Cardiovascular Surgery. He was awarded the Darjah Setia Pangkuan Negeri (DSPN) by the Governor of Penang in July, 2015.",institutionString:null,institution:{name:"Monash University Malaysia",country:{name:"Malaysia"}}},{id:"30568",title:"Prof.",name:"Madhu",middleName:null,surname:"Khullar",slug:"madhu-khullar",fullName:"Madhu Khullar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/30568/images/system/30568.jpg",biography:"Dr. Madhu Khullar is a Professor of Experimental Medicine and Biotechnology at the Post Graduate Institute of Medical Education and Research, Chandigarh, India. She completed her Post Doctorate in hypertension research at the Henry Ford Hospital, Detroit, USA in 1985. She is an editor and reviewer of several international journals, and a fellow and member of several cardiovascular research societies. 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Currently, he is a full professor at Central South University and Shandong First Medical University, and an advisor to MS/PhD students and postdoctoral fellows. He is also a fellow of the Royal Society of Medicine and European Association for Predictive Preventive Personalized Medicine (EPMA), a national representative of EPMA, and a member of the American Society of Clinical Oncology (ASCO) and the American Association for the Advancement of Sciences (AAAS). He is also the editor in chief of International Journal of Chronic Diseases & Therapy, an associate editor of EPMA Journal, Frontiers in Endocrinology, and BMC Medical Genomics, and a guest editor of Mass Spectrometry Reviews, Frontiers in Endocrinology, EPMA Journal, and Oxidative Medicine and Cellular Longevity. 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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. 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