",isbn:null,printIsbn:"979-953-307-X-X",pdfIsbn:null,doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"8b3c5c4439c736e81433536f7a5447eb",bookSignature:"Prof. Prof Nasser S Awwad and Dr. Ali Abdullah Shati",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/9936.jpg",keywords:"Gadolinium Enhancement, Diagnostic Tool, Alloys, Salts, Magnetic Cooling, E. Coli, Bacillus Subtillis, Gadolinium as Burnable, Selective Separation, F-Block Elements, Adsorption, Kinetics",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"September 16th 2020",dateEndSecondStepPublish:"October 14th 2020",dateEndThirdStepPublish:"December 13th 2020",dateEndFourthStepPublish:"March 3rd 2021",dateEndFifthStepPublish:"May 2nd 2021",remainingDaysToSecondStep:"5 months",secondStepPassed:!0,currentStepOfPublishingProcess:5,editedByType:null,kuFlag:!1,biosketch:"Dr. Awwad edited a book for Lanthanides and published more than 25 papers about the elements at f blook, especially Gadolinium. He is a supervisor for 5 Master thesis in the field of Adsorption, removal, purification, kinetics, and modeling of Gadolinium.",coeditorOneBiosketch:"Dr. Shati has a lot of applications about the utilization of gadolinium enhancement. He has published papers about the inhibition of Gadolinium ion for the giant stretch‐activated channels of E. coli and Bacillus subtillis and in use for Kupffer cell depletion ( inactivation).",coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"145209",title:"Prof.",name:"Nasser",middleName:"S",surname:"Awwad",slug:"nasser-awwad",fullName:"Nasser Awwad",profilePictureURL:"https://mts.intechopen.com/storage/users/145209/images/system/145209.jpg",biography:'Dr. Nasser Awwad received his Ph.D. in inorganic and radiochemistry in 2000 from Ain Shams University and his Ph.D. at Sandia National Labs, New Mexico, USA, 2004. Nasser Awwad was an Associate Professor of Radiochemistry in 2006 and Professor of Inorganic and Radiochemistry in 2011. He has been a Professor at King Khalid University, Abha, KSA, from 2011 until now. He has published two chapters in the following books \\"Natural Gas - Extraction to End Use\\" and “Advances in Petrochemicals”. Pro Awwad has edited four books (Uranium, New trends in Nuclear Sciences, Lanthanides, and Nuclear Power Plants) and he has co-edited two books (“Chemistry and Technology of Natural and Synthetic Dyes and Pigments” and “Chromatography - Separation, Identification, and Purification Analysis”). He has also published 95 papers in ISI journals. He has supervised 4 Ph.D. and 18 MSc students in the field of radioactive and wastewater treatment. He has participated in 26 international conferences in South Korea, the USA, Lebanon, KSA, and Egypt. He has reviewed 2 Ph.D. and 13 MSc theses. He participated in 6 big projects with KACST at KSA and Sandia National Labs in the USA. He is a member of the Arab Society of Forensic Sciences and Forensic Medicine. He is a permanent member of the American Chemical Society, and a rapporteur of the Permanent Committee for Nuclear and Radiological Protection at KKU. He is Head of the Scientific Research and International Cooperation Unit, Faculty of Science, King Khalid University.',institutionString:"King Khalid University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"5",totalChapterViews:"0",totalEditedBooks:"4",institution:{name:"King Khalid University",institutionURL:null,country:{name:"Saudi Arabia"}}}],coeditorOne:{id:"330586",title:"Dr.",name:"Ali",middleName:"Abdullah",surname:"Shati",slug:"ali-shati",fullName:"Ali Shati",profilePictureURL:"https://intech-files.s3.amazonaws.com/a043Y00000cA8q1QAC/Co2_Profile_Picture-1599648357298",biography:"Prof. Dr. Ali Abdullah Shati, a Saudi Biologist, graduated with BSc in Biology from King Saud University, Kingdom of Saudi Arabia in 1998, and MSc in Environmental Sciences from Essex University, the United Kingdom in 2004. He received his Ph.D. in Biology of Vertebrates in 2007 from Aberdeen University, United Kingdom. Since 2000, he has been working at King Khalid University in the Kingdom of Saudi Arabia, where he was promoted to Associate Professor in 2013, Professor in 2017 in the major of Vertebrate Physiology and Toxicology. He has held several positions at King Khalid University, including the head of Research Center at College of Science in 2012, Vice Dean of Scientific Research in 2012, Vice Dean of Academic Affairs in the college of science in 2014, and he is currently the Dean of College of Science. His research interests focus on studying the physiological and molecular changes invertebrates as a result of various environmental impacts, in addition to the cytotoxicity of Nano-materials, the therapeutic and protective effect of different bio-extracts, and antioxidant research, He has published more than eighty-seven online papers in international journals indexed in Clarivate Analytics and Scopus, with high impact factor. He has supervised MSc students specialized in the Physiological and Molecular effects of various components on vertebrate's functions. He participated in fourteen international conferences in the United States, United Kingdom, Canada, Australia, New Zealand, and Brazil. In the last ten years, he has awarded several research grants from the deanship of scientific researches at King Khalid University, as a principal investigator. He is also a member of the American Society of Toxicology, the Association of Arab Biologists, and the Saudi Biological Society.",institutionString:"King Khalid University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"0",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"King Khalid University",institutionURL:null,country:{name:"Saudi Arabia"}}},coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"8",title:"Chemistry",slug:"chemistry"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"259492",firstName:"Sara",lastName:"Gojević-Zrnić",middleName:null,title:"Mrs.",imageUrl:"https://mts.intechopen.com/storage/users/259492/images/7469_n.png",email:"sara.p@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. From chapter submission and review, to approval and revision, copyediting and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. I maintain constant and effective communication with authors, editors and reviewers, which allows for a level of personal support that enables contributors to fully commit and concentrate on the chapters they are writing, editing, or reviewing. I assist authors in the preparation of their full chapter submissions and track important deadlines and ensure they are met. I help to coordinate internal processes such as linguistic review, and monitor the technical aspects of the process. As an ASM I am also involved in the acquisition of editors. Whether that be identifying an exceptional author and proposing an editorship collaboration, or contacting researchers who would like the opportunity to work with IntechOpen, I establish and help manage author and editor acquisition and contact."}},relatedBooks:[{type:"book",id:"6303",title:"Uranium",subtitle:"Safety, Resources, Separation and Thermodynamic Calculation",isOpenForSubmission:!1,hash:"4812c0bc91279bd79f03418aca6d17c5",slug:"uranium-safety-resources-separation-and-thermodynamic-calculation",bookSignature:"Nasser S. 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1. Introduction
Nearly 60 years after the first successful organ transplantation in humans, it has been an exponential increase in our understanding of the immunological processes involved in organ transplantation. This knowledge has resulted in the identification of immunogenic drug targets and improvement on the management of patient’s surveillance. The past 5 decades have also seen an explosive evolution in the fields of molecular biology, chemistry and informatics that have enabled increased data throughput, permitting the study of complete sets of molecules with increasing speed and accuracy using the omics techniques such as, genomics (DNA), transcriptomics (RNA), proteomics (proteins) and metabolomics (metabolites) (Bañón-Maneus et al 2007)
Despite overall improvements in immunosuppression regimens, chronic allograft dysfunction (CAD) continues to have a negative impact on graft and patient survival, even with the use of appropriate doses of immunosuppressive drugs to prevent acute rejection. Successful management requires an early detection along with adequate treatment. (Hariharan et al 2000 and Meier-Kriesche et al 2004)
Available diagnostic methods include clinical presentation, biochemical parameters and biopsies. Currently, the only non-invasive biomarkers for follow up the kidney graft are serum creatinine, glomerular filtration rate (GFR) and proteinuria but neither is particularly sensitive or specific and may not reflect early changes. At present, biopsy allograft is regarded as the gold standard for the diagnosis of CAD allowing its early detection; however, this is a costly procedure which is associated with clinical complications (Ojo et al 2000 and Nankivell et al 2003). The patient’s management would be facilitated if there were appropriate biomarkers enabling the diagnosis or prognosis of different states throughout the post transplant course. At that point the proteomics have emerged as a really useful technology for biomarker discovery.
2. Urine as a source of biomarkers
The Biomarkers Definitions Working Group, defined Biomarker as a molecule that it is a characteristic, objectively measured and evaluated as an indicator of normal biological processes, pathogenic processes or pharmacological responses (Biomarkers Definitions Working Group, 2001). The ideal biological sample for detecting biomarkers is the so-called “proximal fluid”, the bio fluid in closest contact with the site of disease (Decramer et al 2008). Then, in the context of kidney transplantation the closest biological sample, besides the biopsy, is the urine which represent a fairly simple, non-invasive and inexpensive method for obtaining suitable samples for biomarker analyses, and presents a huge advantage as it can be performed regularly and frequently if necessary.
The human kidney (Fig. 1) is composed of 1 million nephrons, which can be divided in two functional parts: the glomerulous, which filters the plasma yielding the “primitive” urine, and the renal tubule, which reabsorbs most of the primitive urine. However, more than 99% of this primitive urine is reabsorbed. The remainder (the urine) exits the kidney via the urethra into the bladder (Fig. 1) (Decramer et al 2008). Therefore urine may contain
Figure 1.
Urinary proteins origin. Human kidney it is constituted by nephrons. The plasma filtration occurs into the glomerulus and the reabsorption into the tubule. The urine generated exits the kidney via urethra into the bladder. (Adapted Decramer et al 2008) (images from www. turbosquid.com and www.ratical.org)
information not only from the kidney and the urinary tract but also from more distant organs via plasma obtained by glomerular filtration. In healthy individuals, 70% of the urinary proteome originates from the kidney and the urinary tract, whereas the remaining 30% represents proteins filtered by the glomerulus (Thongboonkerd and Malasit 2005).
For these reasons urine is defined as "fluid biopsy" of the kidney and urogenital tract, and many of the changes in kidney and urogenital tract can be detected in the urinary proteome. Furthermore, as blood filtering, urine contains protein components that are similar to those found in the blood. Thus, pathological changes occurring in other organs can be detected in blood plasma and, therefore, can be detected in the urinary proteome. NHGRI (National Human Genome Research Institute) has said that the study of proteomics of fluids is one of the most promising tools for the development of noninvasive tools for early detection of human diseases. Human urine is a fluid that contains immediately accessible useful biomarkers, it is easy to obtain, non invasive, could be stored for long time and other advantages described into Table 1. But the urine has some disadvantages too.
Table 1.
Advantages and disadvantages of urine as source of biomarkers (Decramer et al 2008, Fliser et al 2005, Kolch et al 2005, Omenn et al 2005, Schaub et al 2004, Schiffer et al 2006, and Theodorescu et al 2006)
Clinical proteomics is growing significantly in recent years due to the prospect of identifying new targets for treatment and therapeutic intervention and biomarkers for diagnosis, prognosis, and therapeutic efficacy using technologies that allow us to compare proteomic profiles between different conditions pathophysiology. The measurement of protein in the urine has been used for many years for the diagnosis and monitoring of many kidney diseases.
3. Omics strategies and single molecule approaches
The major differences between omics strategies and single molecule approaches lies in throughput (hundreds of thousands versus one or a few), but also in experimental design. Classic single molecule bio medical research is based on hypothesis testing, building new experiments based on prior observations and theory, such that classic scientific research tends towards a reductionist approach in understanding disease and disease processes, owing to the limitations of most technologies and the complex nature of pathological systems. After a first omics hypothesis generating approach, classic single molecule experiments should ensue, in order to delve further into the mechanisms of the newly generated hypotheses. (Naesens and Sarwal, 2010)
The development of genomics and transcriptomics notwithstanding, gene polymorphisms and transcript levels correlate incompletely with the expression level of the functionally active proteins, which more accurately reflect actual cellular events. This poor correlation between genotype, gene expression and the localization or activity of the proteins is caused by the complex regulation of the transcription and the post translational modifications that change the properties of proteins. Proteins therefore provide a better picture of events that occur inside an organism and provide ideal biomarkers for disease conditions. (Abbott 1999, Quintana et al 2010 and Righetti and Boschetti 2007)
4. Proteomics technology
Proteomics methods are also increasingly being used in the field of organ transplantation. Because urine is the ideal non invasive specimen for renal diseases, the number of proteomic studies of urine has surged, and urine proteomics are a promising tool for the non invasive diagnosis of acute rejection and chronic allograft histological damage.
New tools and new applications of chemical technologies have revolutionized proteomics and peptidomics last years. Proteomics tools include gel electrophoresis (like one dimensional gel electrophoresis (1D); two dimensional gel electrophoresis (2D)) and gel free methods using mass spectrometry (like matrix-assisted laser ionization (MALDI); liquid chromatography mass spectrometry (LC-MS); surface-enhanced laser ionizationwith time of flight mass spectrometry (SELDI-TOF-MS)) (Naesens and Sarwal, 2010).
Proteome analysis of urine requires fractionation to reduce complexity of the sample. Fractionation can be obtained by different techniques. These fractions are subsequently analyzed by a mass spectrometer (MS) where the relative abundance of the different proteins and peptides is determined. Bioinformatics treatment of the protein data in combination with the fractionation parameters yields protein profiles representing the partial protein content of samples (Fig. 2)
Figure 2.
Proteome analysis of urine requires fractionation to reduce complexity of the sample. Fractionation can be obtained by different chromatographic techniques or 2DE-PAGE. 2 These fractions are subsequently analyzed by a mass spectrometer (MS) 3 Bioinformatics treatment of the obtained data give us the sample proteome.
4.1. Urine sample: Collection, storage and preparation
Sample collection, storage and preparation it is a crucial issue, and many of the techniques described later requires different preparation methods. (Lee et al 2008)
Collection
The volume, protein concentration and composition of urine show considerable variation among the day. There is no ideal time of day to collect urine specimens for proteomics, but it is preferable to obtain samples at the same time of the day to minimize variations. The first morning void could be contaminated by cells from the lower urinary tract and bacteria harbored in the urinary tract. 24 hour samples have the problem of protein degradation. The second void of the morning could be one of the best samples that could be used, because it is easy to obtain when patients come to hospital and could be quickly processed. (O\'Riordan et al 2006)
Some intra-patient variability in the urine proteome has been previously observed, but other investigations have identified only minor variations in samples collected for up to a year. Individual fluctuations seem to be minimally affected by diet and exercise. The relative influence of exogenous and endogenous factors needs further exploration, but should be considered when planning protocols and in interpretation of data (Akkina et al 2009).
Storage
The addition of protease inhibitors, filtration, centrifugation before and after freezing to reduce contamination by proteins leaking cellular debris and bacteria it is necessary. It is necessary to do some test to confirm the absence of red blood cells and leukocytes to avoid possible contamination of the samples.
Repeated freezing and thawing is known to fragment certain proteins, such as IgG and α-1-antitrypsin, and should be avoided. Urine stored at 37 °C can exhibit specific protease activity. An advantage of urinary proteomics is that the analytical reproducibility of the urine proteomic profile is unaffected by long term freezing, remaining stable for several years, even when stored at -20ºC (O\'Riordan et al 2006).
Preparation
The presence of several excessively abundant urinary proteins, among them albumin and uromodulin (uromodulin is most abundant in normal urine, whereas albumin predominates in urine from diseased kidneys), can interfere with analyses. Depletion of these abundant proteins can increase the relative concentration and odds of detecting lower abundance proteins, but with the depletion we can lose some not abundant proteins (Hewitt et al 2004).
Isolating or concentrating urinary proteins may be essential in low concentration specimens, particularly for gel-based studies. Numerous methods have been compared including precipitation with organic solvents, centrifugal filtration, lyophilization and ultrafiltration but with varying results. Precipitation with Trichloroacetic Acid gave good qualitative yield.
Reverse phase extraction has also been shown to be effective in specimen concentration as well as for desalting urinary peptides and segregating lower-molecular weight proteins (Bañón-Maneus et al 2007 and 2011).
Two-dimensional electrophoresis was first described by O’Farrell over 30 years ago. The technology used for separation of proteins is polyacrylamide gel electrophoresis. For many proteomic applications, electrophoresis in one dimension is the method of choice. The proteins are separated according to their mass and how the proteins are solubilized in sodium dodecyl sulfate (SDS) there are generally no problems of solubilization. It is a simple, reproducible and allows the separation of proteins of 10-300 kDa. The 2D-PAGE two-dimensional electrophoresis allows separate thousands of proteins in a single experiment, and is currently the most efficient method for separating very complex protein mixtures. It is based on a separation of proteins according to the isoelectric point, followed by separation of proteins according to their molecular mass (Fig. 3). The first dimension separation is performed by isoelectric focusing, during which proteins are separated in a pH gradient until reaching a position where its net charge is zero, its isoelectric point (Fig. 4A). In a second dimension, proteins are separated by molecular weight in polyacrylamide gels (Fig. 4B). The high resolution of the technique is that the two separations are based on independent parameters. The key innovation for the 2D-PAGE was the development of gels with immobilized pH gradient (IPG). For detection of proteins has traditionally been using the radioactive labeling or staining with Coomassie blue or silver, for greater sensitivity. It also has developed a silver staining method compatible with surface protein digestion and mass spectrometry (Fig. 3) (Bañon-Maneus et al 2010, Oh et al 2004 and Thongboonkerd 2002). A recent development of 2D-PAGE technology is DIGE (Difference in Gel Electrophoresis), explained later.
The 2D-PAGE also has limitations: It is a very demanding technique, is time consuming, and difficult to automate, is limited by the number and type of proteins to solve; the very large or hydrophobic proteins do not enter the gel during the first dimension while proteins very acidic or very basic not well resolved, and in the presence of abundant proteins are difficult to detect low abundance proteins. Some of these problems can be resolved by fractionation,
Figure 3.
PAGE workflow. After the protein extraction of the samples proteins were firs separated by the isoelectric point and after that by molecular weight. After the 2DE-PAGE staining the images were analyzed by finding of differential spots, that after the scission were identified by distinct Mass spectrometry approaches.
the use of certain solubilization conditions and the use of IPGs with different pH ranges. (Table 2) (Yoshida et al 2005)
Liquid chromatography
LC is a physical method of separation based on the distribution of the various components of a mixture into two immiscible phases one stationary and the other mobile. The mobile phase involves a liquid that flows through a column containing the steady phase. Classic LC is carried out in a column which is generally made of glass and filled with the steady phase. The steady phase may be a solid with different chemical properties which give rise to different types of chromatography – ion exchange chromatography, reverse-phase chromatography, and others. The mobile phase may be a pure solvent or mixture of solvents. After placing the sample on the upper part, the mobile phase flows through the column as a result of gravity. To improve the efficiency of separations, the size of steady phase particles was gradually diminished down to microns, and this called for high pressures to ensure mobile phase flow. (Table 2) (Cutillas et al 2003 and Mann et al 2002)
Figure 4.
A) IEF Samples were loaded into a dry polyacrylamide gel strips with an immobilized pH gradient for the separation by isoelectric point B) Second dimension, strips were loaded on the top of polyacrylamide gel and proteins were separated by molecular weight
Table 2.
Advantages and disadvantages of proteomic techniques for use in urinary biomarker discovery
High Performance Liquid Chromatography
High-performance liquid chromatography (HPLC) involves dissolving the protein mixture in buffer and pumping it through a series of columns. The columns are composed of materials with various physical, chemical and immunological properties, which bind different proteins with varying degrees of affinity depending on the complementary protein properties. The proteins can then be eluted from the columns. The properties on which separation can be based are numerous; the elements most frequently applied to urine are size exclusion (based on size), reverse phase (based on hydrophobicity), strong and weak cation binding, and affinity binding (i.e. an immunoglobulin adsorbing to protein of interest). (Bañón-Maneus et al 2007)
Capillary electrophoresis
In a silica capillary, proteins or peptides are separated as a function of charge at a desired pH by an electric field in which the capillary is housed. Like HPLC, this method can be applied to intact proteins, as well as digests. Although a powerful separation technique, capillary electrophoresis (CE) does not yield reliable quantitative information. (Table 2) (Schiffer et al 2006)
Mass spectrometry (MS): Identification and characterization of proteins
Proteins can be identified by various means, among which include the sequencing of the N-terminal specific antibody detection, amino acid composition, co-migration with known proteins and over-expression and depletion of genes. All these methods are generally slow, laborious or expensive and therefore not suitable for use as large-scale strategies. However, the MS, because of its rapidity and high sensitivity, has become the preferred method for identifying large-scale protein and the first step to study the proteome of different organisms. It also allows the characterization of post-translational modifications that have physiological relevance, such as glycosylation and phosphorylation. To analyze proteins by mass spectrometry these must be converted into peptides through proteolysis, usually with trypsin (Mauri et al 2009). This so robust technique involves (Fig. 5):
Conversion of peptides into gas phase ions using soft ionization techniques such as ionization-assisted laser desorption matrix (MALDI) from a sample in solid form, or by electrospray ionization (ESI) of a sample solution.
Separation of ions according to m/z (mass / charge) in a mass analyzer (e.g. type analyzer TOF (Time Of Flight), quadrupole, ion trap, etc.). Optional Fragmentation of selected peptide ions through goal decomposition stable (or PSD technique: post source decay) or by collision-induced dissociation (CID) conducted in a tandem mass spectrometer combining two different analyzers.
Measurement of the masses in a detector obtaining a mass spectrum that reflects the abundance of ions versus their value m / z
For protein identification it has been developed two strategies:
Identification by peptide fingerprint (PMF: peptide mass fingerprinting) or peptide mapping using MALDI-TOF spectrometer type.
Identification of peptides obtained by fragmentation of whole or partial sequence of amino acids (sequence tag) using a tandem mass spectrometer.
Peptide mass fingerprinting
Peptide mapping is a technique used routinely to identify proteins quickly, usually from SDS-PAGE gels or 2D-PAGE and that is normally performed in a mass spectrometer type MALDITOF. In this approach the protein is digested with an enzyme, usually trypsin. The sample is incorporated into a metal plate with a matrix and crystals formed upon evaporation. Subsequently, the sample is irradiated with laser to ionize the molecules. The ions are accelerated by an electric field towards a detector, the value m / z of each ion is determined by the flight time from the source reaching the detector.
Figure 5.
Urine samples were concentrated and separated from organic salts by solid phase. Each sample was applied and dried on an uncoated MALDI target plate using the sandwich technique.
The peptide fingerprint (PMF) of a particular protein is a set of peptides generated by digestion of a specific protease. These experimental peptide masses are compared with theoretical peptide masses of proteins present in databases by developing various algorithms available on the network. For the correct identification of the protein mass requires a large number of peptides matching the theoretical masses of peptides, covering part of the protein sequence database. The limitations of mass spectrometry are that the ionization of peptides is selective and not quantitative. In an equimolar set of peptides derived from digestion of a protein, some peptides may not be detected and the rest of them can be a large variation in signal intensity. If the amount of protein in the gel is small, the number of peptides observed can be small and therefore the protein can not be identified with certainty. The MALDI-TOF MS is of little use to analyze protein mixtures. Very clear protein spots from 2D gels can contain several proteins (Bañón-Maneus et al 2007 and Gazzana and Borlak 2007)
Peptide sequence
It is a strategy to identify proteins not annotated in databases or for the ambiguous identification by MALDI-TOF. The tandem mass spectrometer MS / MS can also determine the amino acid sequence. Ion is selected by a mass spectrometer and fragmented first collision with a gas and the fragments are analyzed in a second spectrometer. Peptide sequence can be done with MALDI ionization source type or ESI. (Gazzana and Borlak 2007)
SELDI–MS incorporates chromatographic and MS principles in a single platform. An activated surface on a ‘chip’ binds proteins on the basis of their chemical and physical properties; unbound proteins are washed off. A subset of the proteome is thus selected and the chip plugs directly into the mass spectrometer for analysis. This is a high-throughput screening technique that facilitates relative abundance profiling of individual proteins from different samples. Although the approach can be extremely useful for screening peptide/protein samples for recognition of biomarker ions, it does not enable the protein origin of these ions to be reliably discerned. Other disadvantages are use of relatively low-resolution MS, the fact that only a subset of the proteome can be studied on any particular surface, and that the performance varies between different machines (as does performance of a single machine over time). (O´Riordan et al 2006)
4.3. Expression level quantitative techniques
The main application of proteomics is the study of protein expression profile. There are two strategies that enhance the study of differential protein expression between different samples, the gel based and the free gel technologies.
Gel based quantitative proteomics: DIGE
Also recently described an approach based on the labeling of proteins with different fluorophores and the separation of samples by 2D-PAGE in the same gel. This methodology, called DIGE (Differential Gel Electrophoresis), minimizes the variability of the gels decreased analysis time and allows quantification of very specific expression profile. Briefly, two samples are differentially labeled with two different fluorescence CyDyes (p.e, Cy3 and Cy5), mixed, and then resolved simultaneously within the same 2DE gel. The introduction of a pooled internal standard labeled with a third dye (p.e. Cy2) improves the accuracy of protein quantification between samples from different gels allowing detection of small changes in protein levels. Differentially expressed proteins could be identified using protein fingerprinting MS methods as modern matrix-assisted laser desorption/ionization-time of-flight MS (MALDI-TOF-MS) instrumentation. (Alban et al 2003, Shaw et al 2003, Unlu et al 1997 and Wu 2006)
Gel Free quantitative proteomics: ICAT, iTRAQ, SILAC
The ICAT (isotope-coded affinity tags), which can determine the relative amount of protein between two samples. The two protein samples are labeled with the ICAT reagent light or heavy (as hydrogen or deuterium leads). This reagent binds to cystein and contains biotin to facilitate purification. Subsequently, the two samples are mixed and digested with trypsin. The peptides marked with ICAT reagent are separated in an affinity column and analyzed by MS. The relative intensity of the peptides identical in each sample (differ in a mass of 8 Da) are abundant protein from which they came. The fragmentation of the peptide by MS / MS led to the identification of the protein (Sobhani 2010).
An improved approach analogous to ICAT has been developed called iTRAQ (Applied Biosystems). The technique is based upon chemically tagging the N-terminus of peptides generated from protein digests that have been isolated from cells, tissues, biological fluids in two different states (Chen et al 2010). The two labeled samples are then combined, fractionated by nanoLC and analyzed by tandem mass spectrometry. Database searching of peptides data fragmentation provides the identification of the labeled peptides and hence the corresponding proteins. Fragmentation of the tag attached to the peptides generates a low molecular mass reporter ion that is unique to the tag used to label each of the digests. Measurement of the intensity of these reporter ions, enables relative quantification of the peptides in each digest and hence the proteins from where they originate. There are four tags available enabling four different conditions to be multiplexed together in one experiment. (Gigy et al 1999)
Stable isotope labeling with amino acids in cell culture (SILAC) is a simple and straightforward approach for in vivo incorporation of a label into proteins for mass spectrometry (MS)-based quantitative proteomics. SILAC relies on metabolic incorporation of a given \'light\' or \'heavy\' form of the amino acid into the proteins. The method relies on the incorporation of amino acids with substituted stable isotopic nuclei (e.g. deuterium, 13C, 15N). Thus in an experiment, two cell populations are grown in culture media that are identical except that one of them contains a \'light\' and the other a \'heavy\' form of a particular amino acid (e.g. 12C and 13C labeled L-lysine, respectively). When the labeled analog of an amino acid is supplied to cells in culture instead of the natural amino acid, it is incorporated into all newly synthesized proteins. After a number of cell divisions, each instance of this particular amino acid will be replaced by its isotope labeled analog. Since there is hardly any chemical difference between the labeled amino acid and the natural amino acid isotopes, the cells behave exactly like the control cell population grown in the presence of normal amino acid. It is efficient and reproducible as the incorporation of the isotope label is 100%. This technology it is not yet available for human urine proteomics but it could be used in experimental models by the administration of pellet food with the isotope enhanced. (Quan et al 2011)
Protein Arrays
Protein arrays are rapidly being developed for the characterization of activities and for detecting protein-protein interactions on a large scale. Like DNA arrays, protein arrays will be essential for basic research and more applied research to drug discovery and development of diagnostic methods. In a pioneering work done by the group of Snyder, we developed a chip with 6,000 yeast proteins to identify new proteins that interact with calmodulin or phospholipids. The proteins were obtained by cloning the corresponding ORFs and each protein was expressed fused to GST (glutathione S-transferase) and a histidine tag. This important work showed that it is possible to prepare microarrays with thousands of proteins and used to study interactions. However, although significant progress has been made for the preparation of the arrays, we still need to face several technological challenges to allow allowing the use of this tool to many researchers. (Zhu et al, 2001)
5. Protein biomarkers for kidney transplantation
Currently follow up of renal transplant recipients is done by the physicians checking serum creatinine and glomerular filtration rate (GFR), but neither is particularly sensitive or specific and may not reflect early alterations (Paul 2009 and Nankivell 2003). At present, biopsy allograft is regarded as the gold standard for the diagnosis of kidney diseases allowing its early detection; however, this is a costly procedure that is associated with clinical complications (Beckingham et al 1994).
5.1. Acute renal allograft rejection
One of the major problems in renal transplantation is acute renal allograft rejection. Acute rejection is one of the key factors that determine long term graft function and survival in renal transplant patients. This fatal complication is inevitable if the diagnosis is delayed.
Mainly for groups reported urinary proteomic approach for acute rejection. Interestingly, each group found a different pattern of protein biomarkers that were associated with allograft rejection. These differences are not surprising, as each study had differences in disease definition, sample collection and handling, protocol for protein and data analysis. (Rush and Nickerson 2011)
Clarke et al reported the comparison between 17 urines from rejecting patients to urines from 15 stable (not biopsied) controls. Proteomic analysis of the urine was done using SELDI15 and ProteinChip Arrays with immobilized metal affinity (IMAC-3) and hydrophobic (H4) surface. The best candidate biomarkers were four proteins of molecular around 7 kd and one of 13.4 kd. A separate analysis using the CART algorithm in the Ciphergen Biomarker Pattern Software using two different proteins of 3.4 kd and 10 kd, respectively, correctly classified 91% of the 34 urine specimens in the training set, producing a sensitivity of 83% and a specificity of 100%. (Clarke et al 2003)
O’Riordan et al reported on the urine proteome in 23 renal transplant patients with biopsy-proven acute rejection, 22 recipients with stable graft function (characterized by serum creatinine) and 20 healthy volunteers (27). The urine was preadsorbed on four different chip surfaces, and was analyzed by SELDI-TOF. Protein masses that were useful in the construction of the classification algorithms were of approximately 2.0, 2.8, 4.8, 5.8 7.0, 19.0 and 25.6 kd. Patients that had experienced acute rejection could be distinguished from stable patients with a sensitivity of 90.5% to 91.3% and a specificity of 77.2% to 83.3%, depending on the classifier used. (O’Riordan et al 2004)
The main drawback with this two studies is that control samples (stable renal transplant recipients) where characterized by a serum creatinine and no biopsies were done at the time of urine collection.
Wittke et al reported the analysis done by CE-MS from 19 patients with subclinical or clinical rejection, 10 patients with urinary tract infection but without rejection, and 29 patients without acute rejection or urinary tract infection (28). These patients were from a centre that performs protocol biopsies, and the urine samples were obtained at the time of protocol biopsy. An additional cohort of 66 healthy controls was studied. The authors were able to discriminate the rejecting patients from those without rejection in 16 of 19 patients using combinations of 16 polypeptides. (Wittke et al 2005)
Finally, Schaub et al sought to determine whether such candidate proteins can be detected in urine using mass spectrometry. Four patient groups were defined on the basis of allograft function, clinical course, and biopsy result. Four groups where analyzed: acute clinical rejection, stable transplant, acute tubular necrosis, and recurrent (or de novo) glomerulopathy. Urines were collected the day of the allograft biopsy. As a normal control group, urines from healthy individuals were analyzed, as well as 5 urines from non-transplanted patients with lower urinary tract infection. Three prominent peak clusters were found in 94% of the patients with acute rejection episodes, but only in 18% of patients without clinical and histologic evidence for rejection and in any of normal controls. In addition, the presence or absence of these peak clusters correlated with the clinicopathologic course in most patients. Acute tubular necrosis, glomerulopathies, lower urinary tract infection, and cytomegalovirus viremia were not confounding variables. (Schaub et al 2004)
In conclusion, proteomic technology together with stringent definition of patient groups can detect urine proteins associated with acute renal allograft rejection. Identification of these proteins may prove useful as non-invasive diagnostic markers for rejection and the development of novel therapeutic agents.
5.2. BKV renal allograft nephropathy
BKV renal allograft nephropathy (BKVAN have an important role in development of renal allograft dysfunction (Fishman 2002). About 6-10% of these patients develop BKVAN, and the reported graft loss rate in this group has been as high as 50% (6,7). BKVAN can resemble acute allograft rejection (AR) and differentiation between them can be challenging both at histological and molecular levels (Fishman 2002). The discrimination is important because the treatment is diametrically opposite for the two conditions. In general, immunosuppression needs to be reduced in patients with BKVAN, whereas it is increased in AR. Currently, these two clinical conditions cannot be differentiated in a reliable way on the basis of clinical and laboratory findings and a definitive diagnosis of BKVAN requires allograft biopsy. Even the histological differentiation of BKVAN from AR can be difficult unless viral inclusions are seen on allograft biopsy (Fishman 2002).
Jahnukainen et al used Surface-enhanced laser desorption/ionization (SELDI) time of flight mass spectrometry to compare the urinary of patients with BKVAN, AR and stable graft function. They were able to detect several peaks that were differentially expressed in the BKVAN group compared with both the AR and stable function groups. Peaks that corresponded to m/z values of 5.872, 11.311, 11.929, 12.727, and 13.349 kD were significantly higher in patients with BKVAN. As Mannon et al showed significant similarity of transcriptional expression of molecules associated with inflammation and fibrosis between BKVAN and AR (Mannon et al 2005). This probably is due to the similarity of the inflammatory response and leakage of inflammation related small molecular weight proteins into urine in both conditions. The limitations of this study are that all of their analyses were based on a limited sample size, and their results on the sensitivity and the specificity of the various algorithms should be interpreted with caution. A true assessment of sensitivity and specificity of the SELDI technique and the various models tested in this report cannot be determined until an independent validation set that is derived from another set of patients is assessed. Proteomic marker(s) profiles, together with plasma and urine BKV PCR and clinical information, may help in making differentiation of BKVAN from AR in a non-invasive manner. Histological verification of BKVAN probably will continue to be required for the foreseeable future, but it is likely that proteomic biomarkers could be used in deciding when a biopsy is necessary. Further studies on a larger number of patients are needed to validate these findings and to detect the identity of the significantly different peaks to develop robust, non-invasive methods for BKVAN diagnostics. (Fishman 2002).
5.3. Chronic allograft rejection
The survival half-life for kidneys from deceased donors is approximately 11 yr, and the pathogenesis of chronic allograft rejection (CAD) is multifactorial (Mauiyyedi et al, 2001). Analyses of graft histology reflected in the revised Banff criteria indicate CAD can be subcategorized, in part, on the basis of evidence of local inflammation and the presence or absence of interstitial fibrosis and tubular atrophy (IF/TA) (Solez et al, 2008). Although specific inciting factors are difficult to define in each situation, distinct histopathologic entities often correlate with likely causes. For example, calcineurin inhibitor toxicity frequently manifests as IF/TA without inflammation; ongoing cellular alloimmunity presents histologically with tubulitis with or without IF/TA; C4d staining suggests transplant glomerulopathy with or without IF/TA; and detectable, donor-specific serum antibodies underlie antibody-mediated allograft injury (Solez et al, 2008).
Because only a subset of patients develop CAD and at present physicians do not have the ability to reverse chronic fibrotic kidney damage, it is essential that the transplant community develop reliable and noninvasive approaches to predict which patients are most likely to develop graft failure so that appropriate interventions can be instituted before graft failure becomes clinically apparent (Mauiyyedi et al, 2001).
Urine proteomic profiling of CAD has been investigated in a few studies to date. Using SELDI as screening methodology and liquid chromatography coupled to mass spectrometry (LCMS) to obtain protein ID information, O’Riordan et al studied the urinary proteome of 75 renal transplant recipients and 20 healthy volunteers. Patients could be classified into subgroups with normal histology and Banff CAN grades 2-3 with 86% sensitivity and 92% specificity. Several urinary proteins associated with advanced CAN were identified including a1-microglobulin, b2-microglobulin, prealbumin, and endorepellin, the antiangiogenic C-terminal fragment of perlecan. Increased urinary endorepellin was confirmed by ELISA and increased tissue expression of the endorepellin/perlecan ratio by immunofluoresence analysis of renal biopsies (O’Riordan 2008).
Our group is also investigating the utility of proteomic analysis of urinary samples as a non-invasive method to detect and evaluate CAD. We did the two main proteomic approaches, gel based and gel free approach. Proteomics based on two-dimensional electrophoresis (2-DE) has been optimized with the development of Difference Gel Electrophoresis (DIGE). A proteome map of stable renal patients as a reference protein database, to validate the utility of 2D-DIGE technology in finding new candidates as CAD urinary biomarkers were established. Morning spot urine of kidney transplant patients with a biopsy two years after transplantation with CI/CT score 0-I-II/III (n=8/group) was collected. 2D silver stained and mass spectrometry (MS) analyses were used to establish the proteome map and 2D-DIGE and MS were used to identify proteins exhibiting differential abundance. In this work not only the urinary proteome of renal stable patients was established but we were able to identify 11 proteins with elevated levels on advanced CAD: β-2 microglobulin, MASP-2, α-1-β-glycoprotein, leucine-rich α-2-glycoprotein 1, α-1-antitrypsin, Gelsolin precursor, AIF-like mitchondrion-associated inducer of death, heparan sulfate proteoglycan, anti-TNF-α antibody light-chain, immunoglobulin lambda light chain and dimethylarginine- dimethylaminohydrolase 2 and wnt-1. Eight of these proteins, α-1-antitrypsin, angiotensinogen, β-2-microglobulin, dimethyl-arginine dimethylaminohydrolase-2, immunoglobulin lambda light chain, transferrin, trypsin precursor, and Zn-β-2-glycoprotein, have been described in other renal injuries thus reducing their validity as biomarkers of, but we identified wnt-1, a protein from wnt/β-catenin pathway that has been described as a pathway really involved in fibrosis in other organs such as lung (Bañón-Maneus et al 2010).
Proteomic analysis using solid phase extraction as protein purification method and Protein profiling by MALDI-TOF was also performed. This is a relatively simple proteomic approach that allows rapid differential diagnosis of patients and information transfer between the laboratory and the clinical context. Fifty individuals: 32 patients with chronic allograft dysfunction (14 with pure interstitial fibrosis and tubular atrophy, and 18 with chronic active antibody-mediated rejection) and 18 controls (8 stable recipients and 10 healthy controls) were studied. Unsupervised hierarchical clustering showed good segregation of samples in groups corresponding mainly to the four biomedical conditions. Moreover, the composition of the proteome of the pure interstitial fibrosis and tubular atrophy group differed from that of the chronic active antibody-mediated rejection group, and an independent validation set confirmed the results from the training set (Quintana et al 2009). With the gel free approach we detected (by LC-M/MS) and quantified (by LCMS) 6000 polypeptide ions in undigested urine specimens across 39 CAD patients and 32 control individuals. Although unsupervised hierarchical clustering differentiated between the groups when including all the identified peptides, specific peptides derived from uromodulin and kininogen were found to be significantly more abundant in control than in CAD patients and correctly identified the two groups. These peptides are therefore potential biomarkers that might be used for the diagnosis of CAD. In addition, ions at m/z 645.59 and m/z 642.61 were able to differentiate between patients with different forms of CAD with specificities and sensitivities of 90% in a training set and, significantly, of 70% in an independent validation set of samples. Interestingly low expression of uromodulin at m/z 638.03 coupled with high expression of m/z 642.61 diagnosed CAD in virtually all cases (Quintana et al 2009).
This suggests that urinary proteome analysis can be used for the non-invasive monitoring of renal transplant patients, although it awaits validation in larger cohorts.
6. Conclusion
In summary, the application of proteomics in the field of renal and organ transplantation opens important options diagnostic and prognostic purposes. At present, urinary proteomics allows us a more early and accurate diagnosis of acute rejection by the experimental determination of peptides in the urine. The differential detection of peptides at diverse stages of the NCT in acute rejection allows us a better way to understand rejection and tolerance. The combined information derived from genomics and proteomics will lead us to consistently reduce the risk factors for graft failure (acute rejection, ischemia-reperfusion, immunosuppression, NCT), with increased life of the organs and improved patient’s quality of life, because proteomics is one of the fields that can help to establish a connection between genomic sequences and biological behavior, constituting an important tool in functional analysis of genes of unknown function. The main advantage of a urine proteomic study as a source of markers for the detection of renal disease in the transplant is that urine is a fluid readily available and non-invasive. There are multiple proteomic techniques although it is noteworthy that, even though the results that each technique offers are very consistent, none is sufficient by itself to obtain and complete proteome and is advisable to combine several of the techniques described. Therefore, the primary application of proteomics is the search for markers that could be the basis for the realization of a microarray of proteins with diagnostic potential.
\n',keywords:null,chapterPDFUrl:"https://cdn.intechopen.com/pdfs/18113.pdf",chapterXML:"https://mts.intechopen.com/source/xml/18113.xml",downloadPdfUrl:"/chapter/pdf-download/18113",previewPdfUrl:"/chapter/pdf-preview/18113",totalDownloads:1899,totalViews:193,totalCrossrefCites:0,totalDimensionsCites:1,hasAltmetrics:0,dateSubmitted:"November 29th 2010",dateReviewed:"May 17th 2011",datePrePublished:null,datePublished:"August 23rd 2011",dateFinished:null,readingETA:"0",abstract:null,reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/18113",risUrl:"/chapter/ris/18113",book:{slug:"kidney-transplantation-new-perspectives"},signatures:"Elisenda Banon-Maneus, Luis F Quintana and Josep M Campistol",authors:[{id:"53337",title:"Dr.",name:"Josep",middleName:null,surname:"Campistol",fullName:"Josep Campistol",slug:"josep-campistol",email:"jmcampis@clinic.ub.es",position:null,institution:null},{id:"53360",title:"Dr.",name:"Elisenda",middleName:null,surname:"Banon-Maneus",fullName:"Elisenda Banon-Maneus",slug:"elisenda-banon-maneus",email:"ebanon@clinic.ub.es",position:null,institution:null},{id:"53361",title:"Dr.",name:"Luis F",middleName:null,surname:"Quintana",fullName:"Luis F Quintana",slug:"luis-f-quintana",email:"lfquinta@clinic.ub.es",position:null,institution:null}],sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_2",title:"2. Urine as a source of biomarkers",level:"1"},{id:"sec_3",title:"3. Omics strategies and single molecule approaches",level:"1"},{id:"sec_4",title:"4. Proteomics technology ",level:"1"},{id:"sec_4_2",title:"4.1. Urine sample: Collection, storage and preparation",level:"2"},{id:"sec_5_2",title:"4.2. Separation of proteins",level:"2"},{id:"sec_6_2",title:"4.3. Expression level quantitative techniques ",level:"2"},{id:"sec_8",title:"5. Protein biomarkers for kidney transplantation",level:"1"},{id:"sec_8_2",title:"5.1. Acute renal allograft rejection",level:"2"},{id:"sec_9_2",title:"5.2. BKV renal allograft nephropathy",level:"2"},{id:"sec_10_2",title:"5.3. Chronic allograft rejection",level:"2"},{id:"sec_12",title:"6. Conclusion",level:"1"}],chapterReferences:[{id:"B1",body:'AbbottA.1999A post-genomic challenge: learning to read patterns of protein synthesis. Nature. Dec 16;402676371520\n\t\t\t'},{id:"B2",body:'AkkinaS. K.ZhangY.NelsestuenG. 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G.BoschettiE.2007Sherlock Holmes and the proteome-a detective story. FEBS J. Feb;2744897905\n\t\t\t'},{id:"B40",body:'RushD.NickersonP.2011Urine proteomics in acute renal transplant rejection, In Biblioteca de Trasplantes Siglo XXI 8GENOMICS AND PROTEOMICS IN SOLID ORGAN TRANSPLANT, 73Drug Farma S.L., 978-8-49672-469-3Madrid'},{id:"B41",body:'SchaubS.WilkinsJ.WeilerT.SangsterK.RushD.NickersonP.2004Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry. Kidney Int.\n\t\t\t\t\t65323332\n\t\t\t'},{id:"B42",body:'SchaubS.RushD.WilkinsJ.GibsonI. W.WeilerT.SangsterK.NicolleL.KarpinskiM.JefferyJ.NickersonP.2004Proteomic-based detection of urine proteins associated with acute renal allograft rejection J Am Soc Nephrol. Jan;15121927\n\t\t\t'},{id:"B43",body:'ShawJ.RowlinsonR.NicksonJ.StoneT.SweetA.WilliamsK.TongeR.2003Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. 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F.2006Discovery and validation of new protein biomarkers for urothelial cancer: a prospective analysis. Lancet Oncol. 7230240\n\t\t\t'},{id:"B48",body:'ThongboonkerdV.Mc LeishK. R.ArthurJ. M.KleinJ. B.2002Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation. Kidney Int; 62: 1461.'},{id:"B49",body:'ThongboonkerdV.MalasitP.2005Renal and urinary proteomics: current applications and challenges. Proteomics\n\t\t\t\t\t510331042\n\t\t\t'},{id:"B50",body:'UnlüM.MorganM.E. MindenJ.S. \n\t\t\t\t\t(1997) Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis; 18: 2071'},{id:"B51",body:'WittkeS. HaubitzM. WaldenM.RohdeF.SchwarzA.MengelMMischakH. HallerH.GwinnerW. (2005) Detection of acute tubulointerstitial rejection by proteomic analysis of urinary samples in renal transplant recipients. Am J Transplant; 5: 5247988'},{id:"B52",body:'WuT. L.2006Two-dimensional difference gel electrophoresis. Methods Mol Biol; 328: 71.'},{id:"B53",body:'YoshidaY.MiyazakiK.KamiieJ.SatoM.OkuizumiS.KenmochiA.KamijoK.NabetaniT.TsugitaA.XuB.ZhangY.YaoitaE.OsawaT.YamamotoT.2005Two-dimensional electrophoretic profiling of normal human kidney glomerulus proteome and construction of an extensible markup language (XML)-based database. Proteomics; 5: 1083.'},{id:"B54",body:' ZhuH.BilginM.BanghamRHallD.CasamayorA. BertoneP.LanN.JansenR.BidlingmaierS.HoufekT. MitchellT. MillerP.DeanR.A. GersteinM.SnyderM. (2001). Global analysis of protein activities using proteome arrays. Science 29321012105\n\t\t\t'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"Elisenda Banon-Maneus",address:"",affiliation:'
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Soel Encalada and Beatriz González Yebra",authors:[{id:"64137",title:"Dr.",name:"Marco Antonio",middleName:null,surname:"Ayala-Garcia",fullName:"Marco Antonio Ayala-Garcia",slug:"marco-antonio-ayala-garcia"},{id:"67078",title:"Dr.",name:"Beatriz",middleName:null,surname:"Gonzalez Yebra",fullName:"Beatriz Gonzalez Yebra",slug:"beatriz-gonzalez-yebra"},{id:"69374",title:"BSc.",name:"Joel Maximo",middleName:null,surname:"Soel Encalada",fullName:"Joel Maximo Soel Encalada",slug:"joel-maximo-soel-encalada"},{id:"117861",title:"MSc.",name:"Miguel",middleName:"Angel",surname:"Pantoja-Hernández",fullName:"Miguel Pantoja-Hernández",slug:"miguel-pantoja-hernandez"},{id:"118126",title:"Dr.",name:"Éctor Jaime",middleName:null,surname:"Ramírez Barba",fullName:"Éctor Jaime Ramírez Barba",slug:"ector-jaime-ramirez-barba"}]},{id:"29960",title:"Renal Transplantation from Expanded Criteria Donors",slug:"renal-transplantation-from-expanded-criteria-donors",signatures:"Pooja Binnani, Madan Mohan Bahadur and Bhupendra Gandhi",authors:[{id:"63754",title:"Dr.",name:"Pooja",middleName:null,surname:"Binnani",fullName:"Pooja Binnani",slug:"pooja-binnani"},{id:"73007",title:"Dr.",name:"Madan Mohan",middleName:null,surname:"Bahadur",fullName:"Madan Mohan Bahadur",slug:"madan-mohan-bahadur"},{id:"73008",title:"Dr.",name:"Bhupendra",middleName:null,surname:"Gandhi",fullName:"Bhupendra Gandhi",slug:"bhupendra-gandhi"}]},{id:"29961",title:"Donor Nephrectomy",slug:"donor-nephrectomy",signatures:"Gholamreza Mokhtari, Ahmad Enshaei, Hamidreza Baghani Aval and Samaneh Esmaeili",authors:[{id:"72575",title:"Dr.",name:"Ahmad",middleName:null,surname:"Enshaei",fullName:"Ahmad Enshaei",slug:"ahmad-enshaei"},{id:"72580",title:"Prof.",name:"Gholamreza",middleName:null,surname:"Mokhtari",fullName:"Gholamreza Mokhtari",slug:"gholamreza-mokhtari"},{id:"72720",title:"BSc.",name:"Samaneh",middleName:null,surname:"Esmaeili",fullName:"Samaneh Esmaeili",slug:"samaneh-esmaeili"},{id:"119000",title:"Dr.",name:"Hamidreza",middleName:null,surname:"Baghani Aval",fullName:"Hamidreza Baghani Aval",slug:"hamidreza-baghani-aval"}]},{id:"29962",title:"Renal Transplantation and Urinary Proteomics",slug:"renal-transplant-and-urinary-proteomics",signatures:"Ying Wang, Li Ma, Gaoxing Luo, Yong Huang and Jun Wu",authors:[{id:"63880",title:"Dr.",name:"Jun",middleName:null,surname:"Wu",fullName:"Jun Wu",slug:"jun-wu"},{id:"119241",title:"Ms.",name:"Ying",middleName:null,surname:"Wang",fullName:"Ying Wang",slug:"ying-wang"},{id:"125954",title:"Prof.",name:"Li",middleName:null,surname:"Ma",fullName:"Li Ma",slug:"li-ma"},{id:"125955",title:"Dr.",name:"Gaoxing",middleName:null,surname:"Luo",fullName:"Gaoxing Luo",slug:"gaoxing-luo"},{id:"125956",title:"Mr.",name:"Yong",middleName:null,surname:"Huang",fullName:"Yong Huang",slug:"yong-huang"}]},{id:"29963",title:"Renal Explantation Techniques",slug:"renal-explantation-techniques",signatures:"Marco Antonio Ayala- García, Éctor Jaime Ramírez-Barba, Joel Máximo Soel Encalada, Beatriz González Yebra",authors:[{id:"64137",title:"Dr.",name:"Marco Antonio",middleName:null,surname:"Ayala-Garcia",fullName:"Marco Antonio Ayala-Garcia",slug:"marco-antonio-ayala-garcia"},{id:"67078",title:"Dr.",name:"Beatriz",middleName:null,surname:"Gonzalez Yebra",fullName:"Beatriz Gonzalez Yebra",slug:"beatriz-gonzalez-yebra"},{id:"69374",title:"BSc.",name:"Joel Maximo",middleName:null,surname:"Soel Encalada",fullName:"Joel Maximo Soel Encalada",slug:"joel-maximo-soel-encalada"},{id:"118126",title:"Dr.",name:"Éctor Jaime",middleName:null,surname:"Ramírez Barba",fullName:"Éctor Jaime Ramírez Barba",slug:"ector-jaime-ramirez-barba"}]},{id:"29964",title:"Renal Transplantation in Patient with Fabry’s Disease Maintained by Enzyme Replacement Therapy",slug:"renal-transplantation-in-patient-with-fabry-s-disease-maintained-by-enzyme-replacement-therapy",signatures:"Taigo Kato",authors:[{id:"66178",title:"Dr.",name:"Taigo",middleName:null,surname:"Kato",fullName:"Taigo Kato",slug:"taigo-kato"}]},{id:"29965",title:"Polymorphism of RAS in Patients with AT1-AA Mediated Steroid Refractory Acute Rejection",slug:"polymorphism-of-ras-in-patients-with-at1-aa-mediated-steroid-refractory-acute-rejection",signatures:"Geng Zhang and Jianlin Yuan",authors:[{id:"68413",title:"Dr.",name:"Geng",middleName:null,surname:"Zhang",fullName:"Geng Zhang",slug:"geng-zhang"},{id:"130514",title:"Prof.",name:"Jianlin",middleName:null,surname:"Yuan",fullName:"Jianlin Yuan",slug:"jianlin-yuan"}]},{id:"29966",title:"Soluble CD30 and Acute Renal Allograft Rejection",slug:"soluble-cd30-and-acute-renal-allograft-rejection",signatures:"Koosha Kamali, Mohammad Amin Abbasi, Ata Abbasi and Alireza R. Rezaie",authors:[{id:"65741",title:"Dr.",name:"Mohammad Amin",middleName:null,surname:"Abbasi",fullName:"Mohammad Amin Abbasi",slug:"mohammad-amin-abbasi"},{id:"72621",title:"Prof.",name:"Alireza R.",middleName:null,surname:"Rezaie",fullName:"Alireza R. Rezaie",slug:"alireza-r.-rezaie"},{id:"72625",title:"Dr.",name:"Ata",middleName:null,surname:"Abbasi",fullName:"Ata Abbasi",slug:"ata-abbasi"},{id:"119210",title:"Prof.",name:"Koosha",middleName:null,surname:"Kamali",fullName:"Koosha Kamali",slug:"koosha-kamali"}]},{id:"29967",title:"Role of Cytomegalovirus Reinfection in Acute Rejection and CMV Disease After Renal Transplantation",slug:"role-of-cytomegalovirus-reinfection-in-acute-rejection-and-cmv-disease-after-renal-transplantation",signatures:"Kei Ishibashi and Tatsuo Suzutani",authors:[{id:"66124",title:"Dr.",name:"Kei",middleName:null,surname:"Ishibashi",fullName:"Kei Ishibashi",slug:"kei-ishibashi"},{id:"128693",title:"Prof.",name:"Tatsuo",middleName:null,surname:"Suzutani",fullName:"Tatsuo Suzutani",slug:"tatsuo-suzutani"}]},{id:"29968",title:"Pharmacogenetics of Immunosuppressive Drugs in Renal Transplantation",slug:"pharmacogenetics-of-immunosuppressive-drugs-in-renal-transplantation",signatures:"María Galiana, María José Herrero, Virginia Bosó, Sergio Bea, Elia Ros, Jaime Sánchez-Plumed, Jose Luis Poveda and Salvador F. Aliño",authors:[{id:"66240",title:"Dr.",name:"Maria Jose",middleName:null,surname:"Herrero",fullName:"Maria Jose Herrero",slug:"maria-jose-herrero"},{id:"119325",title:"Ms.",name:"Maria",middleName:null,surname:"Galiana",fullName:"Maria Galiana",slug:"maria-galiana"},{id:"119326",title:"Ms.",name:"Virginia",middleName:null,surname:"Bosó",fullName:"Virginia Bosó",slug:"virginia-boso"},{id:"119327",title:"Mr.",name:"Sergio",middleName:null,surname:"Bea",fullName:"Sergio Bea",slug:"sergio-bea"},{id:"119328",title:"Ms.",name:"Elia",middleName:null,surname:"Ros",fullName:"Elia Ros",slug:"elia-ros"},{id:"119329",title:"Dr.",name:"Jose Luis",middleName:null,surname:"Poveda",fullName:"Jose Luis Poveda",slug:"jose-luis-poveda"},{id:"119330",title:"Dr.",name:"Jaime",middleName:null,surname:"Sánchez-Plumed",fullName:"Jaime Sánchez-Plumed",slug:"jaime-sanchez-plumed"},{id:"119332",title:"Prof.",name:"Salvador F.",middleName:null,surname:"Aliño",fullName:"Salvador F. Aliño",slug:"salvador-f.-alino"}]},{id:"29969",title:"Pharmacokinetics and Pharmacodynamics of Mycophenolate in Patients After Renal Transplantation",slug:"pharmacokinetics-and-pharmacodynamics-of-mycophenolate-in-patients-after-renal-transplantation",signatures:"Thomas Rath and Manfred Küpper",authors:[{id:"67436",title:"Dr.",name:"Thomas",middleName:null,surname:"Rath",fullName:"Thomas Rath",slug:"thomas-rath"},{id:"74462",title:"Dr",name:"Manfred",middleName:null,surname:"Küpper",fullName:"Manfred Küpper",slug:"manfred-kupper"}]},{id:"29970",title:"Malignant Neoplasms in Kidney Transplantation",slug:"malignant-neoplasms-in-kidney-transplantation-",signatures:"S. S. Sheikh, J. A. Amir and A. A. Amir",authors:[{id:"72571",title:"Dr.",name:"Salwa",middleName:"Shabbir",surname:"Sheikh",fullName:"Salwa Sheikh",slug:"salwa-sheikh"},{id:"72577",title:"Dr.",name:"Abdul Razack",middleName:null,surname:"Amir",fullName:"Abdul Razack Amir",slug:"abdul-razack-amir"},{id:"125326",title:"Ms.",name:"Jumana",middleName:null,surname:"Amir",fullName:"Jumana Amir",slug:"jumana-amir"}]},{id:"29971",title:"Osteonecrosis of Femoral Head (ONFH) After Renal Transplantation",slug:"-osteonecrosis-of-femoral-head-onfh-after-renal-transplantation",signatures:"Yan Jie Guo and Chang Qing Zhang",authors:[{id:"73379",title:"Dr.",name:"Chang Qing",middleName:null,surname:"Zhang",fullName:"Chang Qing Zhang",slug:"chang-qing-zhang"},{id:"124047",title:"Dr.",name:"Yan Jie",middleName:null,surname:"Guo",fullName:"Yan Jie Guo",slug:"yan-jie-guo"}]},{id:"29972",title:"Pediatric Kidney Transplant in Uropaties",slug:"-pediatric-transplant-renal-in-uropaties-",signatures:"Cristian Sager, Juan Carlos López, Víctor Durán, Carol Burek, Juan Pablo Corbetta and Santiago Weller",authors:[{id:"65438",title:"Dr.",name:"Cristian",middleName:null,surname:"Sager",fullName:"Cristian Sager",slug:"cristian-sager"},{id:"119806",title:"Dr.",name:"Juan Carlos",middleName:null,surname:"Lopez",fullName:"Juan Carlos Lopez",slug:"juan-carlos-lopez"},{id:"126321",title:"Dr.",name:"Victor",middleName:null,surname:"Duran",fullName:"Victor Duran",slug:"victor-duran"},{id:"126322",title:"Dr.",name:"Carol",middleName:null,surname:"Burek",fullName:"Carol Burek",slug:"carol-burek"},{id:"126634",title:"Dr.",name:"Juan Pablo",middleName:null,surname:"Corbetta",fullName:"Juan Pablo Corbetta",slug:"juan-pablo-corbetta"},{id:"126635",title:"Dr.",name:"Santiago",middleName:null,surname:"Weller",fullName:"Santiago Weller",slug:"santiago-weller"}]}]}]},onlineFirst:{chapter:{type:"chapter",id:"66340",title:"Biological Degradation of Polymers in the Environment",doi:"10.5772/intechopen.85124",slug:"biological-degradation-of-polymers-in-the-environment",body:'\n
\n
1. Introduction
\n
In 1869, the first synthetic polymer was invented in response to a commercial $10,000 prize to provide a suitable replacement to ivory. A continuous string of discoveries and inventions contributed new polymers to meet the various requirements of society. Polymers are constructed of long chains of atoms, organized in repeating components or units often exceeding those found in nature. Plastic can refer to matter that is pliable and easily shaped. Recent usage finds it to be a name for materials called polymers. High molecular weight organic polymers derived from various hydrocarbon and petroleum materials are now referred to as plastics [1].
\n
Synthetic polymers are constructed of long chains of smaller molecules connected by strong chemical bonds and arranged in repeating units which provide desirable properties. The chain length of the polymers and patterns of polymeric assembly provide properties such as strength, flexibility, and a lightweight feature that identify them as plastics. The properties have demonstrated the general utility of polymers and their manipulation for construction of a multitude of widely useful items leading to a world saturation and recognition of their unattractive properties too. A major trend of ever increasing consumption of plastics has been seen in the areas of industrial and domestic applications. Much of this polymer production is composed of plastic materials that are generally non-biodegradable. This widespread use of plastics raises a significant threat to the environment due to the lack of proper waste management and a until recently cavalier community behavior to maintain proper control of this waste stream. Response to these conditions has elicited an effort to devise innovative strategies for plastic waste management, invention of biodegradable polymers, and education to promote proper disposal. Technologies available for current polymer degradation strategies are chemical, thermal, photo, and biological techniques [2, 3, 4, 5, 6]. The physical properties displayed in Table 1 show little differences in density but remarkable differences in crystallinity and lifespan. Crystallinity has been shown to play a very directing role in certain biodegradation processes on select polymers.
\n
\n
\n
\n
\n
\n
\n\n
\n
Polymer
\n
Abbreviation
\n
Density (23/4°C)
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Crystallinity (%)
\n
Lifespan (year)
\n
\n\n\n
\n
Polyethylene
\n
PE
\n
0.91–0.925
\n
50
\n
10–600
\n
\n
\n
Polypropylene
\n
PP
\n
0.94–0.97
\n
50
\n
10–600
\n
\n
\n
Polystyrene
\n
PS
\n
0.902–0.909
\n
0
\n
50–80
\n
\n
\n
Polyethylene glycol terephthalate
\n
PET
\n
1.03–1.09
\n
0–50
\n
450
\n
\n
\n
Polyvinyl chloride
\n
PVC
\n
1.35–1.45
\n
0
\n
50–100+
\n
\n\n
Table 1.
Selected features of major commercial thermoplastic polymers [7].
\n
Polymers are generally carbon-based commercialized polymeric materials that have been found to have desirable physical and chemical properties in a wide range of applications. A recent assessment attests to the broad range of commercial materials that entered to global economy since 1950 as plastics. The mass production of virgin polymers has been assessed to be 8300 million metric tons for the period of 1950 through 2015 [8]. Globally consumed at a pace of some 311 million tons per year with 90% having a petroleum origin, plastic materials have become a major worldwide solid waste problem. Plastic composition of solid waste has increased for less than 1% in 1960 to greater than 10% in 2005 which was attributed largely to packaging. Packaging plastics are recycled in remarkably low quantities. Should current production and waste management trends continue, landfill plastic waste and that in the natural environment could exceed 12,000 Mt of plastic waste by 2050 [9].
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\n
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2. Polymer structures and features
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A polymer is easily recognized as a valuable chemical made of many repeating units [10]. The basic repeating unit of a polymer is referred to as the “-mer” with “poly-mer” denoting a chemical composed of many repeating units. Polymers can be chemically synthesized in a variety of ways depending on the chemical characteristics of the monomers thus forming a desired product. Nature affords many examples of polymers which can be used directly or transformed to form materials required by society serving specific needs. The polymers of concern are generally composed of carbon and hydrogen with extension to oxygen, nitrogen and chlorine functionalities (see Figure 1 for examples). Chemical resistance, thermal and electrical insulation, strong and light-weight, and myriad applications where no alternative exists are polymer characteristics that continue to make polymers attractive. Significant polymer application can be found in the automotive, building and construction, and packaging industries [12].
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Figure 1.
Structures of major commercial thermoplastic polymers [11].
\n
The environmental behavior of polymers can be only discerned through an understanding of the interaction between polymers and environment under ambient conditions. This interaction can be observed from surface properties changes that lead to new chemical functionality formation in the polymer matrix. New functional groups contribute to continued deterioration of the polymeric structure in conditions such as weathering. Discoloration and mechanical stiffness of the polymeric mass are often hallmarks of the degradative cycle in which heat, mechanical energy, radiation, and ozone are contributing factors [13].
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Polyolefins (PO) are the front-runners of the global industrial polymer market where a broad range of commercial products contribute to our daily lives in the form o packaging, bottles, automobile parts and piping. The PO class family is comprised of saturated hydrocarbon polymers such as high-density polyethylene (HDPE), low-density polyethylene (LDPE) and linear low-density polyethylene (LLDPE), propylene and higher terminal olefins or monomer combinations as copolymers. The sources of these polymers are low-cost petrochemicals and natural gas with monomers production dependent on cracking or refining of petroleum. This class of polymers has a unique advantage derived from their basic composition of carbon and hydrogen in contrast to other available polymers such as polyurethanes, poly(vinyl chloride) and polyamides [14].
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The copolymers of ethylene and propylene are produced in quantities that exceed 40% of plastics produced per annum with no production leveling in sight. This continuous increase suggests that as material use broadens yearly, the amount of waste will also increase and present waste disposal problems. Polyolefin biological and chemical inertness continues to be recognized as an advantage. However, this remarkable stability found at many environmental conditions and the degradation resistance leads to environmental accumulation and an obvious increase to visible pollution and ancillary contributing problems. Desired environmental properties impact the polyolefin market on the production side as well as product recyclability [15].
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\n
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3. Biological degradation
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Biodegradation utilizes the functions of microbial species to convert organic substrates (polymers) to small molecular weight fragments that can be further degraded to carbon dioxide and water [16, 17, 18, 19, 20, 21]. The physical and chemical properties of a polymer are important to biodegradation. Biodegradation efficiency achieved by the microorganisms is directly related to the key properties such as molecular weight and crystallinity of the polymers. Enzymes engaged in polymer degradation initially are outside the cell and are referred to as exo-enzymes having a wide reactivity ranging from oxidative to hydrolytic functionality. Their action on the polymer can be generally described as depolymerization. The exo-enzymes generally degrade complex polymer structure to smaller, simple units that can take in the microbial cell to complete the process of degradation.
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\n
3.1 Requirements to assay polymer biodegradation
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Polymer degradation proceeds to form new products during the degradation path leading to mineralization which results in the formation of process end-products such as, e.g., CO2, H2O or CH4 [22]. Oxygen is the required terminal electron acceptor for the aerobic degradation process. Aerobic conditions lead to the formation of CO2 and H2O in addition to the cellular biomass of microorganisms during the degradation of the plastic forms. Where sulfidogenic conditions are found, polymer biodegradation leads to the formation of CO2 and H2O. Polymer degradation accomplished under anaerobic conditions produces organic acids, H2O, CO2, and CH4. Contrasting aerobic degradation with anaerobic conditions, the aerobic process is found to be more efficient. When considering energy production the anaerobic process produces less energy due to the absence of O2, serving the electron acceptor which is more efficient in comparison to CO2 and SO4−2 [23].
\n
As solid materials, plastics encounter the effects of biodegradation at the exposed surface. In the unweathered polymeric structure, the surface is affected by biodegradation whereas the inner part is generally unavailable to the effects of biodegradation. Weathering may mechanically affect the structural integrity of the plastic to permit intrusion of bacteria or fungal hyphae to initiate biodegradation at inner loci of the plastic. The rate of biodegradation is functionally dependent on the surface area of the plastic. As the microbial-colonized surface area increases, a faster biodegradation rate will be observed assuming all other environmental conditions to be equal [24].
\n
Microorganisms can break organic chemicals into simpler chemical forms through biochemical transformation. Polymer biodegradation is a process in which any change in the polymer structure occurs as a result of polymer properties alteration resulting from the transformative action of microbial enzymes, molecular weight reduction, and changes to mechanical strength and surface properties attributable to microbial action. The biodegradation reaction for a carbon-based polymer under aerobic conditions can be formulated as follows:
\n
\n
\n\n\n\n\nE1
\n
Assimilation of the carbon comprising the polymer (Cpolymer) by microorganisms results in conversion to CO2 and H2O with production of more microbial biomass (Cbiomass). In turn, Cbiomass is mineralized across time by the microbial community or held in reserve as storage polymers [25].
\n
The following set of equations is a more complete description of the aerobic plastic biodegradation process:
\n
\n
\n\n\n\n\nE2
\n
where Cpolymer and newly formed oligomers are converted into Cbiomass but Cbiomass converts to CO2 under a different kinetics scheme. The conversion to CO2 is referred to as microbial mineralization. Each oligomeric fragment is expected to proceed through of sequential steps in which the chemical and physical properties are altered leading to the desired benign result. A technology for monitoring aerobic biodegradation has been developed and optimized for small organic pollutants using oxygen respirometry where the pollutant degrades at a sufficiently rapid rate for respirometry to provide expected rates of biodegradation. When polymers are considered, a variety of analytical approaches relating to physical and chemical changes are employed such as differential scanning calorimetry, scanning electron microscopy, thermal gravimetric analysis, Fourier transform infrared spectrometry, gas chromatograph-mass spectrometry, and atomic force microscopy [26].
\n
Since most polymer disposal occurs in our oxygen atmosphere, it is important to recognize that aerobic biodegradation will be our focus but environmental anaerobic conditions do exist that may be useful to polymer degradation. The distinction between aerobic and anaerobic degradation is quite important since it has been observed that anaerobic conditions support slower biodegradation kinetics. Anaerobic biodegradation can occur in the environment in a variety of situations. Burial of polymeric materials initiates a complex series of chemical and biological reactions. Oxygen entrained in the buried materials is initially depleted by aerobic bacteria. The following oxygen depleted conditions provide conditions for the initiation of anaerobic biodegradation. The buried strata are generally covered by 3-m-thick layers which prevent oxygen replenishment. The alternate electron acceptors such as nitrate, sulfate, or methanogenic conditions enable the initiation of anaerobic biodegradation. Any introduction of oxygen will halt an established anaerobic degradation process.
\n
\n
\n
3.2 Formulation of newer biodegradation schema
\n
This formulation for the aerobic biodegradation of polymers can be improved due to the complexity of the processes involved in polymer biodegradation [27]. Biodegradation, defined as a decomposition of substances by the action of microorganisms, leading to mineralization and the formation of new biomass is not conveniently summarized. A new analysis is necessary to assist the formulation of comparative protocols to estimate biodegradability. In this context, polymer biodegradation is defined as a complex process composed of the stages of biodeterioration, biofragmentation, and assimilation [28].
\n
The biological activity inferred in the term biodegradation is predominantly composed of, biological effects but within nature biotic and abiotic features act synergistically in the organic matter degradation process. Degradation modifying mechanical, physical and chemical properties of a material is generally referred to as deterioration. Abiotic and biotic effects combine to exert changes to these properties. This biological action occurs from the growth of microorganisms on the polymer surface or inside polymer material. Mechanical, chemical, and enzymatic means are exerted by microorganisms, thereby modifying the gross polymer material properties. Environmental conditions such as atmospheric pollutants, humidity, and weather strongly contribute to the overall process. The adsorbed pollutants can assist the material colonization by microbial species. A diverse collection of bacteria, protozoa, algae, and fungi are expected participants involved in biodeterioration. The development of different biota can increase biodeterioration by facilitating the production of simple molecules.
\n
Fragmentation is a material breaking phenomenon required to meet the constraints for the subsequent event called assimilation. Polymeric material has a high molecular weight which is restricted by its size in its transit across the cell wall or cytoplasmic membrane. Reduction of polymeric molecule size is indispensable to this process. Changes to molecular size can occur through the involvement of abiotic and biotic processes which are expected to reduce molecular weight and size. The utility of enzymes derived from the microbial biomass could provide the required molecular weight reductions. Mixtures of oligomers and/or monomers are the expected products of the biological fragmentation.
\n
Assimilation describes the integration of atoms from fragments of polymeric materials inside microbial cells. The microorganisms benefit from the input of energy, electrons and elements (i.e., carbon, nitrogen, oxygen, phosphorus, sulfur and so forth) required for the cell growth. Assimilated substrates are expected to be derived from biodeterioration and biofragmentation effects. Non-assimilated materials, impermeable to cellular membranes, are subject to biotransformation reactions yielding products that may be assimilated. Molecules transported across the cell membrane can be oxidized through catabolic pathways for energy storage and structural cell elements. Assimilation supports microbial growth and reproduction as nutrient substrates (e.g., polymeric materials) are consumed from the environment.
\n
\n
\n
3.3 Factors affecting biodegradability
\n
The polymer substrate properties are highly important to any colonization of the surface by either bacteria or fungi [29]. The topology of the surface may also be important to the colonization process. The polymer properties of molecular weight, shape, size and additives are each unique features which can limit biodegradability. The molecular weight of a polymer can be very limiting since the microbial colonization depends on surface features that enable the microorganisms to establish a locus from which to expand growth. Polymer crystallinity can play a strong role since it has been observed that microbial attachment to the polymer surface occurs and utilizes polymer material in amorphous sections of the polymer surface. Polymer additives are generally low molecular weight organic chemicals that can provide a starting point for microbial colonization due to their ease of biodegradation (Figure 2).
\n
Figure 2.
Factors controlling polymer biodegradation [30].
\n
Weather is responsible for the deterioration of most exposed materials. Abiotic contributors to these conditions are moisture in its variety of forms, non-ionizing radiation, and atmospheric temperature. When combined with wind effects, pollution, and atmospheric gases, the overall process of deterioration can be quite formable. The ultraviolet (UV) component of the solar spectrum contributes ionizing radiation which plays a significant role in initiating weathering effects. Visible and near-infrared radiation can also contribute to the weathering process. Other factors couple with solar radiation synergistically to significantly influence the weathering processes. The quality and quantity of solar radiation, geographic location changes, time of day and year, and climatological conditions contribute to the overall effects. Effects of ozone and atmospheric pollutants are also important since each can interact with atmospheric radiation to result in mechanical stress such as stiffening and cracking. Moisture when combined with temperature effects can assist microbial colonization. The biotic contributors can strongly assist the colonization by providing the necessary nutrients for microbial growth. Hydrophilic surfaces may provide a more suitable place for colonization to ensue. Readily available exoenzymes from the colonized area can initiate the degradation process.
\n
\n
\n
3.4 Biofilms
\n
Communities of microorganisms attached to a surface are referred to as biofilms [31]. The microorganisms forming a biofilm undergo remarkable changes during the transition from planktonic (free-swimming) biota to components of a complex, surface-attached community (Figure 3). The process is quite simple with planktonic microorganism encountering a surface where some adsorb followed by surface release to final attachment by the secretion of exopolysaccharides which act as an adhesive for the growing biofilm [33]. New phenotypic characteristics are exhibited by the bacteria of a biofilm in response to environmental signals. Initial cell-polymer surface interactions, biofilm maturation, and the return to planktonic mode of growth have regulatory circuits and genetic elements controlling these diverse functions. Studies have been conducted to explore the genetic basis of biofilm development with the development of new insights. Compositionally, these films have been found to be a single microbial species or multiple microbial species with attachment to a range of biotic and abiotic surfaces [34, 35]. Mixed-species biofilms are generally encountered in most environments. Under the proper nutrient and carbon substrate supply, biofilms can grow to massive sizes. With growth, the biofilm can achieve large film structures that may be sensitive to physical forces such as agitation. Under such energy regimes, the biofilm can detach. An example of biofilm attachment and utility can be found in the waste water treatment sector where large polypropylene disks are rotated through industrial or agriculture waste water and then exposed to the atmosphere to treat pollutants through the intermediacy of cultured biofilms attached to the rotating polypropylene disk.
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Figure 3.
Microbial attachment processes to a polymer surface [32].
\n
Biofilm formation and activity to polymer biodegradation are complex and dynamic [36]. The physical attachment offers a unique scenario for the attached microorganism and its participation in the biodegradation. After attachment as a biofilm component, individual microorganisms can excrete exoenzymes which can provide a range of functions. Due to the mixed-species composition found in most environments, a broad spectrum of enzymatic activity is generally possible with wide functionalities. Biofilm formation can be assisted by the presence of pollutant chemical available at the polymer surface. The converse is also possible where surfaces contaminated with certain chemicals can prohibit biofilm formation. Biofilms continue to grow with the input of fresh nutrients, but when nutrients are deprived, the films will detach from the surface and return to a planktonic mode of growth. Overall hydrophobicity of the polymer surface and the surface charge of a bacterium may provide a reasonable prediction of surfaces to which a microorganism might colonize [37]. These initial cell-surface and cell-cell interactions are very useful to biofilm formation but incomplete (Figure 4). Microbial surfaces are heterogeneous, and can change widely in response to environmental changes. Five stages of biofilm development: have been identified as (1) initial attachment, (2) irreversible attachment, (3) maturation I, (4) maturation II, and (5) dispersion. Further research is required to provide the understanding of microbial components involved in biofilm development and regulation of their production to assemble to various facets of this complex microbial phenomenon [38].
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Figure 4.
Biofilm formation and processes [34].
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The activities envisioned in this scenario (depicted in Figure 4) are the reversible adsorption of bacteria occurring at the later time scale, irreversible attachment of bacteria occurring at the second-minute time scale, growth and division of bacteria in hours-days, exopolymer production and biofilm formation in hours-days, and attachment and other organisms to biofilm in days-months.
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3.5 Standardized testing methods
\n
The evaluation of the extent of polymer biodegradation is made difficult by the dependence on polymer surface and the departure of degradation kinetics from the techniques available for small pollutant molecule techniques [39]. For applications for polymer biodegradation a variety of techniques have been applied. Visual observations, weight loss measurements, molar mass and mechanical properties, carbon dioxide evolution and/or oxygen consumption, radiolabeling, clear-zone formation, enzymatic degradation, and compost test under controlled conditions have been cited for their utility [27]. The testing regime must be explicitly described within a protocol of steps that can be collected for various polymers and compared on an equal basis. National and international efforts have developed such protocols to enable the desired comparisons using rigorous data collecting techniques and interpretation [40].
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4. Environmental biodegradation of polymers
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The conventional polymers such as (PE), (PP), (PS), (PUR), and (PET) are recognized for their persistence in the environment [41]. Each of these polymers is subject to very slow fragmentation to form small particles in a process expected to require centuries of exposure to photo-, physical, and biological degradation processes. Until recently, the commercial polymers were not expected to biodegrade. The current perspective supports polymer biodegradation with hopeful expectation that these newly encountered biodegradation processes can be transformed into technologies capable of providing major assistance to the ongoing task of waste polymer management.
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4.1 Polyolefins
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The polyolefins such as polyethylene (PE) have been recognized as a polymer remarkably resistant to degradation [42]. Products made with PE are very diverse and a testament to its chemical and biological inertness. The biodegradation of the polyolefins is complex and incompletely understood. Pure strains elicited from the environment have been used to investigate metabolic pathways or to gain a better understanding of the effect that environmental conditions have on polyolefin degradation. This strategy ignores the importance of different microbial species that could participate in a cooperative process. Treatment of the complex environments associated with polymeric solid waste could be difficult with information based on pure strain analysis. Mixed and complex microbial communities have been used and encountered in different bioremediation environments [43].
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A variety of common PE types, low-density PE (LDPE), high-density PE (HDPE), linear low-density PE (LLDPE) and cross-linked PE (XLPE), differ in their density, degree of branching and availability of functional groups at the surface. The type of polymer used as the substrate can strongly influence the microbial community structure colonizing PE surface. A significant number of microbial strains have been identified for the deterioration caused by their interaction with the polymer surface [44]. Microorganisms have been categorized for their involvement in PE colonization and biodegradation or the combination. Some research studies did not conduct all the tests required to verify PE biodegradation. A more inclusive approach to assessing community composition, including the non-culturable fraction of microorganisms invisible by traditional microbiology methods is required in future assessments. The diversity of microorganisms capable of degrading PE extends beyond 17 genera of bacteria and nine genera of fungi [45]. These numbers are expected to increase with the use of more sensitive isolation and characterization techniques using rDNA sequencing. Polymer additives can affect the kinds of microorganisms colonizing the surfaces of these polymers. The ability of microorganisms to colonize the PE surfaces exhibits a variety of effects on polymer properties. Seven different characteristics have been identified and are used to monitor the extent of polymer surface change resulting from biodegradation of the polymer. The characteristics are hydrophobicity/hydrophilicity, crystallinity, surface topography, functional groups on the surface, mechanical properties, and molecular weight distribution. The use of surfactants has become important to PE biodegradation. Complete solubilization of PE in water by a Pseudomonas fluorescens treated for a month followed by biosurfactant treatment for a subsequent month in the second month and finally a 10% sodium dodecyl sulfate treatment at 60°C for a third month led to complete polymer degradation. A combination of P. fluorescens, surfactant and biosurfactant treatments as a single treatment significantly exhibited polymer oxidation and biodegradation [46]. The metabolically diverse genus Pseudomonas has been investigated for its capabilities to degrade and metabolize synthetic plastics. Pseudomonas species found in environmental matrices have been identified to degrade a variety of polymers including PE, and PP [47]. The unique capabilities of Pseudomonas species related to degradation and metabolism of synthetic polymers requires a focus on: the interactions controlling cell surface attachment of biofilms to polymer surfaces, extracellular polymer oxidation and/or hydrolytic enzyme activity, metabolic pathways mediating polymer uptake and degradation of polymer fragments within the microbial cell through catabolism, and the importance of development of the implementation of enhancing factors such as pretreatments, microbial consortia and nutrient availability while minimizing the effects of constraining factors such as alternative carbon sources and inhibitory by-products. In an ancillary study, thermophilic consortia of Brevibacillus sps. and Aneurinibacillus sp. from waste management landfills and sewage treatment plants exhibited enhanced PE and PP degradation [48].
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The larval stage of two waxworm species, Galleria mellonella and Plodia interpunctella, has been observed to degrade LDPE without pretreatment [49, 50]. The worms could macerate PE as thin film shopping bags and metabolize the film to ethylene glycol which in turn biodegrades rapidly. The remarkable ability to digest a polymer considered non-edible may parallel the worm’s ability utilize beeswax as a food source. From the guts of Plodia interpunctella waxworms two strains of bacteria, Enterobacter asburiae YP1 and Bacillus sp. YP1, were isolated and found to degrade PE in laboratory conditions. The two strains of bacteria were shown to reduce the polymer film hydrophobicity during a 28-day incubation. Changes to the film surface as cavities and pits were observed using scanning electron microscopy and atomic-force microscopy. Simple contact of ~100 Galleria mellonella worms with a commercial PE shopping bag for 12 hours resulted in a mass loss of 92 mg. The waxworm research has been scrutinized and found to be lacking the necessary information to support the claims of the original Galleria mellonella report [51].
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Polypropylene (PP) is very similar to PE, in solution behavior and electrical properties. Mechanical properties and thermal resistance are improved with the addition of the methyl group but chemical resistance decreases. There are three forms of propylene selectively formed from the monomer isotactic, syndiotactic, and atactic due to the different geometric relationships achievable through polymerization technology. PP properties are strongly directed by tacticity or the methyl group orientation as related the methyl groups in neighboring monomer units. Isotactic PP has a greater degree of crystallinity than atactic and syndiotactic PP and therefore more difficult to biodegrade. The high molar mass of PP prohibits permeation through the microbial cell membrane which thwarts metabolism by living organisms. It is generally recognized that abiotic degradation provides a foothold for microorganisms to form a biofilm. With partial destruction of the polymer surface by abiotic effects the microbes can then start breaking the damaged polymer chains [52].
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4.2 Polystyrene
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PS is a sturdy thermoplastic commonly used in short-lifetime items that contribute broadly to the mass of poorly controlled polymers [53]. Various forms of PS such as general purpose (GPPS)/oriented polystyrene (OPS), polystyrene foam, and expanded polystyrene (EPS) foam are available for different commercial leading to a broad solid waste composition. PS has been thought to be non-biodegradable. The rate of biodegradation encountered in the environment is very slow leading to prolonged persistence as solid waste. In the past, PS was recycled through mechanical, chemical, and thermal technologies yielding gaseous and liquid daughter products [54]. A rather large collection of studies has shown that PS is subject to biodegradation but at a very slow rate in the environment. A sheet of PS buried for 32 years. in soil showed no indication of biotic or abiotic degradation [55]. The hydrophobicity of the polymer surface, a function of molecular structure and composition, detracts from the effectiveness of microbial attachment [56, 57]. The general lack of water solubility of PS prohibits the transport into microbial cells for metabolism.
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A narrow range of microorganisms have been elicited for the environment and found to degrade PS [53]. Bacillus and Pseudomonas strains isolated from soil samples have been shown to degrade brominated high impact PS. The activity was seen in weight loss and surface changes to the PS film. Soil invertebrates such as the larvae of the mealworm (Tenebrio molitor Linnaeus) have been shown to chew and eat Styrofoam [57]. Samples of the larvae were fed Styrofoam as the sole diet for 30 days and compared with worms fed a conventional diet. The worms feeding Styrofoam survived for 1 month after which they stopped eating as they entered the pupae stage and emerged as adults after a subsequent 2 weeks. It appears that Styrofoam feeding did not lead to any lethality for the mealworms. The ingested PS mass was efficiently depolymerized within the larval gut during the retention time of 24 hours and converted to CO2 [51]. This remarkable behavior by the mealworm can be considered the action of an efficient bioreactor. The mealworm can provide all the necessary components for PS treatment starting with chewing, ingesting, mixing, reacting with gut contents, and microbial degradation by gut microbial consortia. A PS-degrading bacterial strain Exiguobacterium sp. strain YT2 was isolated from the gut of mealworms and found to degrade PS films outside the mealworm gut. Superworms (Zophobas morio) were found to exhibit similar activity toward Styrofoam. Brominated high impact polystyrene (blend of polystyrene and polybutadiene) has been found to be degraded by Pseudomonas and Bacillus strains [58]. In a complementary study, four non-pathogenic cultures (Enterobacter sp., Citrobacter sedlakii, Alcaligenes sp. and Brevundimonas diminuta) were isolated from partially degraded polymer samples from a rural market setting and each were found to degrade high impact polystyrene [59].
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4.3 Polyvinyl chloride
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PVC is manufactured in two forms rigid and flexible. The rigid form can be found in the construction industry as pipe or in structural applications. The soft and flexible form can be made through the incorporation of plasticizers such as phthalates. Credit cards, bottles, and non-food packaging are notable products with a PVC composition. PVC has been known from its inception as a polymer with remarkable resistance to degradation [60]. Thermal and photodegradation processes are widely recognized for their role in the weathering processes found with PVC [61, 62]. The recalcitrant feature of polyvinyl chloride resistance to biodegradation becomes a matter of environmental concern across the all processes extending from manufacturing to waste disposal. Few reports are available relating the extent of PVC biodegradation. Early studies investigated the biodegradation of low-molecular weight PVC by white rot fungi [63]. Plasticized PVC was found to be degraded by fungi such as As. fumigatus, Phanerochaete chrysosporium, Lentinus tigrinus, As. niger, and Aspergillus sydowii [64].
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Modifying the PVC film composition with adjuvants such as cellulose and starch provided a substrate that fungi could also degrade [65]. Several investigations of soil bacteria for the ability to degrade PVC from enrichment cultures were conducted on different locations [66]. Mixed cultures containing bacteria and fungi were isolated and found to grow on plasticized PVC [67]. Significant differences were observed for the colonization by the various components of the mixed isolates during very long exposure times [68]. Significant drift in isolate activity was averted through the use of talc. Consortia composed of a combination of different bacterial strains of Pseudomonas otitidis, Bacillus cereus, and Acanthopleurobacter pedis have the ability to degrade PVC in the environment [64]. These results offer the opportunity to optimization conditions for consortia growth in PVC and use as a treatment technology to degrade large collections of PVC. PVC film blends were shown to degrade by partnering biodegradable polymers with PVC [69].
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4.4 Polyurethane
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PUR encompass a broad field of polymer synthesis where a di- or polyisocyanate is chemically linked through carbamate (urethane) formation. These thermosetting and thermoplastic polymers have been utilized to form microcellular foams, high performance adhesives, synthetic fibers, surface coatings, and automobile parts along with a myriad of other applications. The carbamate linkage can be severed by chemical and biological processes [70].
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Aromatic esters and the extent of the crystalline fraction of the polymer have been identified as important factors affecting the biodegradation of PUR [71, 72]. Acid and base hydrolysis strategies can sever the carbamate bond of the polymer. Microbial ureases, esterases and proteases can enable the hydrolysis the carbamate and ester bonds of a PUR polymer [71, 73, 74]. Bacteria have been found to be good sources for enzymes capable of degrading PUR polymers [75, 76, 77, 78, 79, 80, 81, 82]. Fungi are also quite capable of degrading PUR polymers [83, 84, 85]. Each of the enzyme systems has their preferential targets: ureases attack the urea linkages [86, 87, 88] with esterases and proteases hydrolyzing the ester bonds of the polyester PUR as a major mechanism for its enzymatic depolymerization [89, 90, 91, 92]. PUR polymers appear to be more amenable to enzymatic depolymerization or degradation but further searches and inquiry into hitherto unrecognized microbial PUR degrading activities is expected to offer significant PUR degrading activities.
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4.5 Polyethylene terephthalate
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PET is a polyester commonly marketed as a thermoplastic polymer resin finding use as synthetic fibers in clothing and carpeting, food and liquid containers, manufactured objects made through thermoforming, and engineering resins with glass fiber. Composed of terephthalic acid and ethylene glycol through the formation of ester bonds, PET has found a substantial role in packaging materials, beverage bottles and the textile industry. Characterized as a recalcitrant polymer of remarkable durability, the polymer’s properties are reflective of its aromatic units in its backbone and a limited polymer chain mobility [91]. In many of its commercial forms, PET is semicrystalline having crystalline and amorphous phases which has a major effect on PET biodegradability. The environmental accumulation of PET is a testament of its versatility and the apparent lack of chemical/physical mechanisms capable of attacking its structural integrity show it to be a major environmental pollution problem.
\n
The durability and the resulting low biodegradability of PET are due to the presence of repeating aromatic terephthalate units in its backbone and the corresponding limited mobility of the polymer chains [92]. The semicrystalline PET polymer also contains both amorphous and crystalline fractions with a strong effect on its biodegradability. Crystallinity exceeding 30% in PET beverage bottles and fibers having even higher crystalline compositions presents major hurdles to enzyme-induced degradation [93, 94]. At higher temperatures, the amorphous fraction of PET becomes more flexible and available to enzymatic degradation [95, 96]. The hydrolysis of PET by enzymes has been identified as a surface erosion process [97, 98, 99, 100]. The hydrophobic surface significantly limits biodegradation due to the limited ability for microbial attachment. The hydrophobic nature of PET poses a significant barrier to microbial colonization of the polymer surface thus attenuating effective adsorption and access by hydrolytic enzymes to accomplish the polymer degradation [101].
\n
A wide array of hydrolytic enzymes including hydrolases, lipases, esterases, and cutinases has been shown to have the ability to hydrolyze amorphous PET polymers and modify PET film surfaces. Microbes from a vast collection of waste sites and dumping situations have been studied for their ability to degrade PET. A subunit of PET, diethylene glycol phthalate has been found to be a source of carbon and energy necessary to the sustenance of microbial life. Enzyme modification may be effectively employed to improve the efficiency and specificity of the polyester degrading enzymes acknowledged to be active degraders of PET [102]. Significant efforts have been extended to developing an understanding of the enzymatic activity of high-performing candidate enzymes through selection processes, mechanistic probes, and enzyme engineering. In addition to hydrolytic enzymes already identified, enzymes found in thermophilic anaerobic sludge were found to degrade PET copolymers formed into beverage bottles [103].
\n
Recently, the discovery of microbial activity capable of complete degradation of widely used beverage bottle plastic expands the range of technology options available for PET treatment. A microorganism isolated from the area adjacent to a plastic bottle-recycling facility was shown to aerobically degrade PET to small molecular daughter products and eventually to CO2 and H2O. This new research shows that a newly isolated microbial species, Ideonella sakaiensis 201-F6, degrades PET through hydrolytic transformations by the action of two enzymes, which are extracellular and intracellular hydrolases. A primary hydrolysis reaction intermediate, mono (hydroxy-2-ethyl) terephthalate is formed and can be subsequently degraded to ethylene glycol and terephthalic acid which can be utilized by the microorganism for growth [104, 105, 106, 107, 108, 109].
\n
This discovery could be a candidate as a single vessel system that could competently accomplish PET hydrolysis as an enzyme reactor. This may be the beginning of viable technology development applicable to the solution of the global plastic problem recognized for its terrestrial component as well as the water contamination problem found in the sea. These remarkable discoveries offer a new perspective on the recalcitrant nature of PET and how future environmental management of PET waste may be conducted using the power of enzymes. The recognition of current limiting steps in the biological depolymerization of PET are expected to enable the design of a enzymes-based process to reutilized the natural assets contained in scrap PET [110] (Figure 5).
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Figure 5.
Microbial depolymerization of poly(ethylene terephthalate).
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5. Conclusions
\n
The major commercial polymers have been shown to be biodegradable in a variety of circumstances despite a strong predisposition suggesting that many of these polymers were recalcitrant to the effects of biodegradation. The question of whether bioremediation can play a significant role in the necessary management of polymer waste remains to be determined. Treatment technology for massive waste polymer treatment must be sufficiently robust to be reliable at large scale use and adaptable to conditions throughout the environment where this treatment is required. The status of information relating to the application of biodegradation treatment to existing and future polymer solid waste is at early stages of development for several waste polymers. The discovery of that invertebrate species (insect larvae) can reduce the size of the waste polymer by ingesting and degradation in the gut via enzymes which aid or complete degradation is rather amazing and requires additional scrutiny. There is an outside change that a polymer recycling technology based on these findings is a future possibility.
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Disclaimer
\n
The views expressed in this book chapter are those of the author and do not necessarily represent the views or policies of the U.S. Environmental Protection Agency.
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Conflict of interest
No “conflict of interest” is known or expected.
\n',keywords:"polymers, plastics, degradation, microbial degradation, biofilms, extent of degradation",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/66340.pdf",chapterXML:"https://mts.intechopen.com/source/xml/66340.xml",downloadPdfUrl:"/chapter/pdf-download/66340",previewPdfUrl:"/chapter/pdf-preview/66340",totalDownloads:2179,totalViews:496,totalCrossrefCites:4,dateSubmitted:"April 11th 2018",dateReviewed:"February 11th 2019",datePrePublished:"May 13th 2019",datePublished:null,dateFinished:null,readingETA:"0",abstract:"Polymers present to modern society remarkable performance characteristics desired by a wide range of consumers but the fate of polymers in the environment has become a massive management problem. Polymer applications offer molecular structures attractive to product engineers desirous of prolonged lifetime properties. These characteristics also figure prominently in the environmental lifetimes of polymers or plastics. Recently, reports of microbial degradation of polymeric materials offer new emerging technological opportunities to modify the enormous pollution threat incurred through use of polymers/plastics. A significant literature exists from which developmental directions for possible biological technologies can be discerned. Each report of microbial mediated degradation of polymers must be characterized in detail to provide the database from which a new technology developed. Part of the development must address the kinetics of the degradation process and find new approaches to enhance the rate of degradation. The understanding of the interaction of biotic and abiotic degradation is implicit to the technology development effort.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/66340",risUrl:"/chapter/ris/66340",signatures:"John A. Glaser",book:{id:"7479",title:"Plastics in the Environment",subtitle:null,fullTitle:"Plastics in the Environment",slug:"plastics-in-the-environment",publishedDate:"May 15th 2019",bookSignature:"Alessio Gomiero",coverURL:"https://cdn.intechopen.com/books/images_new/7479.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",editors:[{id:"217030",title:"Ph.D.",name:"Alessio",middleName:null,surname:"Gomiero",slug:"alessio-gomiero",fullName:"Alessio Gomiero"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}},authors:null,sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_2",title:"2. Polymer structures and features",level:"1"},{id:"sec_3",title:"3. Biological degradation",level:"1"},{id:"sec_3_2",title:"3.1 Requirements to assay polymer biodegradation",level:"2"},{id:"sec_4_2",title:"3.2 Formulation of newer biodegradation schema",level:"2"},{id:"sec_5_2",title:"3.3 Factors affecting biodegradability",level:"2"},{id:"sec_6_2",title:"3.4 Biofilms",level:"2"},{id:"sec_7_2",title:"3.5 Standardized testing methods",level:"2"},{id:"sec_9",title:"4. Environmental biodegradation of polymers",level:"1"},{id:"sec_9_2",title:"4.1 Polyolefins",level:"2"},{id:"sec_10_2",title:"4.2 Polystyrene",level:"2"},{id:"sec_11_2",title:"4.3 Polyvinyl chloride",level:"2"},{id:"sec_12_2",title:"4.4 Polyurethane",level:"2"},{id:"sec_13_2",title:"4.5 Polyethylene terephthalate",level:"2"},{id:"sec_15",title:"5. Conclusions",level:"1"},{id:"sec_16",title:"Disclaimer",level:"1"},{id:"sec_20",title:"Conflict of interest",level:"1"}],chapterReferences:[{id:"B1",body:'Massy J. A Little Book about BIG Chemistry: The Story of Man-Made Polymers. 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Structural insight into molecular mechanism of poly (ethylene terephthalate) degradation. Nature Communications. 2018;9(1):382\n'},{id:"B108",body:'Doppalapudi S, Jain A, Khan W, Domb AJ. Biodegradable polymers—An overview. Polymers for Advanced Technologies. 2014;25(5):427-435. DOI: 10.1002/pat.3305\n'},{id:"B109",body:'Avérous L, Pollet E. Biodegradable polymers. In: Environmental Silicate Nano-Biocomposites. Springer; 2012. pp. 13-39. DOI: 10.1007/978-1-4471-4108-2_2\n'},{id:"B110",body:'Vroman I, Tighzert L. Biodegradable polymers. Materials. 2009;2(2):307-344. DOI: 10.3390/ma2020307\n'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"John A. Glaser",address:"glaser.john@epa.gov",affiliation:'
U.S. Environmental Protection Agency, Office of Research and Development, National Risk Management Research Laboratory, Cincinnati, Ohio, USA
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He is presently with Alcorn State University (Mississippi, USA) as an associate professor. Dr. Zheng serves as a program director of the Computer Network and Information Technology major, as well as the director of Pattern Recognition and Image Analysis Lab. He is the principle investigator on three federal research grants in night vision enhancement, thermal face recognition, and multispectral face recognition. He was the Co-PI on a breast cancer detection research grant. Dr. Zheng holds two patents on glaucoma classification and face recognition, and has published one book, six book chapters, and more than 70 peer-reviewed papers. His research interests include biomedical imaging, pattern recognition, biometrics, information fusion, colorization, bio-inspired image analysis, and computer-aided diagnosis. Dr. Zheng is a Cisco Certified Network Professional (CCNP), a senior member of SPIE, a member of IEEE & Computer Society, as well as a technical reviewer.",institutionString:null,institution:null},{id:"24824",title:"Prof.",name:"Gang",surname:"Hu",slug:"gang-hu",fullName:"Gang Hu",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Xi'an University of Technology",institutionURL:null,country:{name:"China"}}},{id:"24865",title:"Dr.",name:"Nemir",surname:"Al-Azzawi",slug:"nemir-al-azzawi",fullName:"Nemir Al-Azzawi",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"28288",title:"Dr.",name:"Guangxin",surname:"Li",slug:"guangxin-li",fullName:"Guangxin Li",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"29462",title:"Dr.",name:"Ioana",surname:"Gheta",slug:"ioana-gheta",fullName:"Ioana Gheta",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"29732",title:"Prof.",name:"Wan Ahmed K.",surname:"Wan Abdullah",slug:"wan-ahmed-k.-wan-abdullah",fullName:"Wan Ahmed K. Wan Abdullah",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"66912",title:"Dr.",name:"Rui",surname:"Zhao",slug:"rui-zhao",fullName:"Rui Zhao",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"66913",title:"Dr.",name:"Xin-Qiang",surname:"Qin",slug:"xin-qiang-qin",fullName:"Xin-Qiang Qin",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"67336",title:"Prof.",name:"Jürgen",surname:"Beyerer",slug:"jurgen-beyerer",fullName:"Jürgen Beyerer",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Fraunhofer Institute of Optronics, System Technologies and Image Exploitation",institutionURL:null,country:{name:"Germany"}}}]},generic:{page:{slug:"our-story",title:"Our story",intro:"
The company was founded in Vienna in 2004 by Alex Lazinica and Vedran Kordic, two PhD students researching robotics. While completing our PhDs, we found it difficult to access the research we needed. So, we decided to create a new Open Access publisher. A better one, where researchers like us could find the information they needed easily. The result is IntechOpen, an Open Access publisher that puts the academic needs of the researchers before the business interests of publishers.
",metaTitle:"Our story",metaDescription:"The company was founded in Vienna in 2004 by Alex Lazinica and Vedran Kordic, two PhD students researching robotics. While completing our PhDs, we found it difficult to access the research we needed. So, we decided to create a new Open Access publisher. A better one, where researchers like us could find the information they needed easily. The result is IntechOpen, an Open Access publisher that puts the academic needs of the researchers before the business interests of publishers.",metaKeywords:null,canonicalURL:"/page/our-story",contentRaw:'[{"type":"htmlEditorComponent","content":"
We started by publishing journals and books from the fields of science we were most familiar with - AI, robotics, manufacturing and operations research. Through our growing network of institutions and authors, we soon expanded into related fields like environmental engineering, nanotechnology, computer science, renewable energy and electrical engineering, Today, we are the world’s largest Open Access publisher of scientific research, with over 4,200 books and 54,000 scientific works including peer-reviewed content from more than 116,000 scientists spanning 161 countries. Our authors range from globally-renowned Nobel Prize winners to up-and-coming researchers at the cutting edge of scientific discovery.
\\n\\n
In the same year that IntechOpen was founded, we launched what was at the time the first ever Open Access, peer-reviewed journal in its field: the International Journal of Advanced Robotic Systems (IJARS).
\\n\\n
The IntechOpen timeline
\\n\\n
2004
\\n\\n
\\n\\t
Intech Open is founded in Vienna, Austria, by Alex Lazinica and Vedran Kordic, two PhD students, and their first Open Access journals and books are published.
\\n\\t
Alex and Vedran launch the first Open Access, peer-reviewed robotics journal and IntechOpen’s flagship publication, the International Journal of Advanced Robotic Systems (IJARS).
\\n
\\n\\n
2005
\\n\\n
\\n\\t
IntechOpen publishes its first Open Access book: Cutting Edge Robotics.
\\n
\\n\\n
2006
\\n\\n
\\n\\t
IntechOpen publishes a special issue of IJARS, featuring contributions from NASA scientists regarding the Mars Exploration Rover missions.
\\n
\\n\\n
2008
\\n\\n
\\n\\t
Downloads milestone: 200,000 downloads reached
\\n
\\n\\n
2009
\\n\\n
\\n\\t
Publishing milestone: the first 100 Open Access STM books are published
\\n
\\n\\n
2010
\\n\\n
\\n\\t
Downloads milestone: one million downloads reached
\\n\\t
IntechOpen expands its book publishing into a new field: medicine.
\\n
\\n\\n
2011
\\n\\n
\\n\\t
Publishing milestone: More than five million downloads reached
\\n\\t
IntechOpen publishes 1996 Nobel Prize in Chemistry winner Harold W. Kroto’s “Strategies to Successfully Cross-Link Carbon Nanotubes”. Find it here.
\\n\\t
IntechOpen and TBI collaborate on a project to explore the changing needs of researchers and the evolving ways that they discover, publish and exchange information. The result is the survey “Author Attitudes Towards Open Access Publishing: A Market Research Program”.
\\n\\t
IntechOpen hosts SHOW - Share Open Access Worldwide; a series of lectures, debates, round-tables and events to bring people together in discussion of open source principles, intellectual property, content licensing innovations, remixed and shared culture and free knowledge.
\\n
\\n\\n
2012
\\n\\n
\\n\\t
Publishing milestone: 10 million downloads reached
\\n\\t
IntechOpen holds Interact2012, a free series of workshops held by figureheads of the scientific community including Professor Hiroshi Ishiguro, director of the Intelligent Robotics Laboratory, who took the audience through some of the most impressive human-robot interactions observed in his lab.
\\n
\\n\\n
2013
\\n\\n
\\n\\t
IntechOpen joins the Committee on Publication Ethics (COPE) as part of a commitment to guaranteeing the highest standards of publishing.
\\n
\\n\\n
2014
\\n\\n
\\n\\t
IntechOpen turns 10, with more than 30 million downloads to date.
\\n\\t
IntechOpen appoints its first Regional Representatives - members of the team situated around the world dedicated to increasing the visibility of our authors’ published work within their local scientific communities.
\\n
\\n\\n
2015
\\n\\n
\\n\\t
Downloads milestone: More than 70 million downloads reached, more than doubling since the previous year.
\\n\\t
Publishing milestone: IntechOpen publishes its 2,500th book and 40,000th Open Access chapter, reaching 20,000 citations in Thomson Reuters ISI Web of Science.
\\n\\t
40 IntechOpen authors are included in the top one per cent of the world’s most-cited researchers.
\\n\\t
Thomson Reuters’ ISI Web of Science Book Citation Index begins indexing IntechOpen’s books in its database.
\\n
\\n\\n
2016
\\n\\n
\\n\\t
IntechOpen is identified as a world leader in Simba Information’s Open Access Book Publishing 2016-2020 report and forecast. IntechOpen came in as the world’s largest Open Access book publisher by title count.
\\n
\\n\\n
2017
\\n\\n
\\n\\t
Downloads milestone: IntechOpen reaches more than 100 million downloads
\\n\\t
Publishing milestone: IntechOpen publishes its 3,000th Open Access book, making it the largest Open Access book collection in the world
We started by publishing journals and books from the fields of science we were most familiar with - AI, robotics, manufacturing and operations research. Through our growing network of institutions and authors, we soon expanded into related fields like environmental engineering, nanotechnology, computer science, renewable energy and electrical engineering, Today, we are the world’s largest Open Access publisher of scientific research, with over 4,200 books and 54,000 scientific works including peer-reviewed content from more than 116,000 scientists spanning 161 countries. Our authors range from globally-renowned Nobel Prize winners to up-and-coming researchers at the cutting edge of scientific discovery.
\n\n
In the same year that IntechOpen was founded, we launched what was at the time the first ever Open Access, peer-reviewed journal in its field: the International Journal of Advanced Robotic Systems (IJARS).
\n\n
The IntechOpen timeline
\n\n
2004
\n\n
\n\t
Intech Open is founded in Vienna, Austria, by Alex Lazinica and Vedran Kordic, two PhD students, and their first Open Access journals and books are published.
\n\t
Alex and Vedran launch the first Open Access, peer-reviewed robotics journal and IntechOpen’s flagship publication, the International Journal of Advanced Robotic Systems (IJARS).
\n
\n\n
2005
\n\n
\n\t
IntechOpen publishes its first Open Access book: Cutting Edge Robotics.
\n
\n\n
2006
\n\n
\n\t
IntechOpen publishes a special issue of IJARS, featuring contributions from NASA scientists regarding the Mars Exploration Rover missions.
\n
\n\n
2008
\n\n
\n\t
Downloads milestone: 200,000 downloads reached
\n
\n\n
2009
\n\n
\n\t
Publishing milestone: the first 100 Open Access STM books are published
\n
\n\n
2010
\n\n
\n\t
Downloads milestone: one million downloads reached
\n\t
IntechOpen expands its book publishing into a new field: medicine.
\n
\n\n
2011
\n\n
\n\t
Publishing milestone: More than five million downloads reached
\n\t
IntechOpen publishes 1996 Nobel Prize in Chemistry winner Harold W. Kroto’s “Strategies to Successfully Cross-Link Carbon Nanotubes”. Find it here.
\n\t
IntechOpen and TBI collaborate on a project to explore the changing needs of researchers and the evolving ways that they discover, publish and exchange information. The result is the survey “Author Attitudes Towards Open Access Publishing: A Market Research Program”.
\n\t
IntechOpen hosts SHOW - Share Open Access Worldwide; a series of lectures, debates, round-tables and events to bring people together in discussion of open source principles, intellectual property, content licensing innovations, remixed and shared culture and free knowledge.
\n
\n\n
2012
\n\n
\n\t
Publishing milestone: 10 million downloads reached
\n\t
IntechOpen holds Interact2012, a free series of workshops held by figureheads of the scientific community including Professor Hiroshi Ishiguro, director of the Intelligent Robotics Laboratory, who took the audience through some of the most impressive human-robot interactions observed in his lab.
\n
\n\n
2013
\n\n
\n\t
IntechOpen joins the Committee on Publication Ethics (COPE) as part of a commitment to guaranteeing the highest standards of publishing.
\n
\n\n
2014
\n\n
\n\t
IntechOpen turns 10, with more than 30 million downloads to date.
\n\t
IntechOpen appoints its first Regional Representatives - members of the team situated around the world dedicated to increasing the visibility of our authors’ published work within their local scientific communities.
\n
\n\n
2015
\n\n
\n\t
Downloads milestone: More than 70 million downloads reached, more than doubling since the previous year.
\n\t
Publishing milestone: IntechOpen publishes its 2,500th book and 40,000th Open Access chapter, reaching 20,000 citations in Thomson Reuters ISI Web of Science.
\n\t
40 IntechOpen authors are included in the top one per cent of the world’s most-cited researchers.
\n\t
Thomson Reuters’ ISI Web of Science Book Citation Index begins indexing IntechOpen’s books in its database.
\n
\n\n
2016
\n\n
\n\t
IntechOpen is identified as a world leader in Simba Information’s Open Access Book Publishing 2016-2020 report and forecast. IntechOpen came in as the world’s largest Open Access book publisher by title count.
\n
\n\n
2017
\n\n
\n\t
Downloads milestone: IntechOpen reaches more than 100 million downloads
\n\t
Publishing milestone: IntechOpen publishes its 3,000th Open Access book, making it the largest Open Access book collection in the world
\n
\n"}]},successStories:{items:[]},authorsAndEditors:{filterParams:{sort:"featured,name"},profiles:[{id:"6700",title:"Dr.",name:"Abbass A.",middleName:null,surname:"Hashim",slug:"abbass-a.-hashim",fullName:"Abbass A. Hashim",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/6700/images/1864_n.jpg",biography:"Currently I am carrying out research in several areas of interest, mainly covering work on chemical and bio-sensors, semiconductor thin film device fabrication and characterisation.\nAt the moment I have very strong interest in radiation environmental pollution and bacteriology treatment. The teams of researchers are working very hard to bring novel results in this field. I am also a member of the team in charge for the supervision of Ph.D. students in the fields of development of silicon based planar waveguide sensor devices, study of inelastic electron tunnelling in planar tunnelling nanostructures for sensing applications and development of organotellurium(IV) compounds for semiconductor applications. I am a specialist in data analysis techniques and nanosurface structure. I have served as the editor for many books, been a member of the editorial board in science journals, have published many papers and hold many patents.",institutionString:null,institution:{name:"Sheffield Hallam University",country:{name:"United Kingdom"}}},{id:"54525",title:"Prof.",name:"Abdul Latif",middleName:null,surname:"Ahmad",slug:"abdul-latif-ahmad",fullName:"Abdul Latif Ahmad",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"20567",title:"Prof.",name:"Ado",middleName:null,surname:"Jorio",slug:"ado-jorio",fullName:"Ado Jorio",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Universidade Federal de Minas Gerais",country:{name:"Brazil"}}},{id:"47940",title:"Dr.",name:"Alberto",middleName:null,surname:"Mantovani",slug:"alberto-mantovani",fullName:"Alberto Mantovani",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"12392",title:"Mr.",name:"Alex",middleName:null,surname:"Lazinica",slug:"alex-lazinica",fullName:"Alex Lazinica",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/12392/images/7282_n.png",biography:"Alex Lazinica is the founder and CEO of IntechOpen. After obtaining a Master's degree in Mechanical Engineering, he continued his PhD studies in Robotics at the Vienna University of Technology. Here he worked as a robotic researcher with the university's Intelligent Manufacturing Systems Group as well as a guest researcher at various European universities, including the Swiss Federal Institute of Technology Lausanne (EPFL). During this time he published more than 20 scientific papers, gave presentations, served as a reviewer for major robotic journals and conferences and most importantly he co-founded and built the International Journal of Advanced Robotic Systems- world's first Open Access journal in the field of robotics. Starting this journal was a pivotal point in his career, since it was a pathway to founding IntechOpen - Open Access publisher focused on addressing academic researchers needs. Alex is a personification of IntechOpen key values being trusted, open and entrepreneurial. Today his focus is on defining the growth and development strategy for the company.",institutionString:null,institution:{name:"TU Wien",country:{name:"Austria"}}},{id:"19816",title:"Prof.",name:"Alexander",middleName:null,surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/19816/images/1607_n.jpg",biography:"Alexander I. Kokorin: born: 1947, Moscow; DSc., PhD; Principal Research Fellow (Research Professor) of Department of Kinetics and Catalysis, N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow.\r\nArea of research interests: physical chemistry of complex-organized molecular and nanosized systems, including polymer-metal complexes; the surface of doped oxide semiconductors. He is an expert in structural, absorptive, catalytic and photocatalytic properties, in structural organization and dynamic features of ionic liquids, in magnetic interactions between paramagnetic centers. The author or co-author of 3 books, over 200 articles and reviews in scientific journals and books. He is an actual member of the International EPR/ESR Society, European Society on Quantum Solar Energy Conversion, Moscow House of Scientists, of the Board of Moscow Physical Society.",institutionString:null,institution:{name:"Semenov Institute of Chemical Physics",country:{name:"Russia"}}},{id:"62389",title:"PhD.",name:"Ali Demir",middleName:null,surname:"Sezer",slug:"ali-demir-sezer",fullName:"Ali Demir Sezer",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/62389/images/3413_n.jpg",biography:"Dr. Ali Demir Sezer has a Ph.D. from Pharmaceutical Biotechnology at the Faculty of Pharmacy, University of Marmara (Turkey). He is the member of many Pharmaceutical Associations and acts as a reviewer of scientific journals and European projects under different research areas such as: drug delivery systems, nanotechnology and pharmaceutical biotechnology. Dr. Sezer is the author of many scientific publications in peer-reviewed journals and poster communications. Focus of his research activity is drug delivery, physico-chemical characterization and biological evaluation of biopolymers micro and nanoparticles as modified drug delivery system, and colloidal drug carriers (liposomes, nanoparticles etc.).",institutionString:null,institution:{name:"Marmara University",country:{name:"Turkey"}}},{id:"61051",title:"Prof.",name:"Andrea",middleName:null,surname:"Natale",slug:"andrea-natale",fullName:"Andrea Natale",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"100762",title:"Prof.",name:"Andrea",middleName:null,surname:"Natale",slug:"andrea-natale",fullName:"Andrea Natale",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"St David's Medical Center",country:{name:"United States of America"}}},{id:"107416",title:"Dr.",name:"Andrea",middleName:null,surname:"Natale",slug:"andrea-natale",fullName:"Andrea Natale",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Texas Cardiac Arrhythmia",country:{name:"United States of America"}}},{id:"64434",title:"Dr.",name:"Angkoon",middleName:null,surname:"Phinyomark",slug:"angkoon-phinyomark",fullName:"Angkoon Phinyomark",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/64434/images/2619_n.jpg",biography:"My name is Angkoon Phinyomark. I received a B.Eng. degree in Computer Engineering with First Class Honors in 2008 from Prince of Songkla University, Songkhla, Thailand, where I received a Ph.D. degree in Electrical Engineering. My research interests are primarily in the area of biomedical signal processing and classification notably EMG (electromyography signal), EOG (electrooculography signal), and EEG (electroencephalography signal), image analysis notably breast cancer analysis and optical coherence tomography, and rehabilitation engineering. I became a student member of IEEE in 2008. During October 2011-March 2012, I had worked at School of Computer Science and Electronic Engineering, University of Essex, Colchester, Essex, United Kingdom. In addition, during a B.Eng. I had been a visiting research student at Faculty of Computer Science, University of Murcia, Murcia, Spain for three months.\n\nI have published over 40 papers during 5 years in refereed journals, books, and conference proceedings in the areas of electro-physiological signals processing and classification, notably EMG and EOG signals, fractal analysis, wavelet analysis, texture analysis, feature extraction and machine learning algorithms, and assistive and rehabilitative devices. I have several computer programming language certificates, i.e. Sun Certified Programmer for the Java 2 Platform 1.4 (SCJP), Microsoft Certified Professional Developer, Web Developer (MCPD), Microsoft Certified Technology Specialist, .NET Framework 2.0 Web (MCTS). 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