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Carbohydrate-Active Enzymes

Carbohydrate-Active Enzymes
Structure, Function and Applications

by K.-H. Park

  • Publisher : Elsevier
  • Release : 2008-09-23
  • Pages : 312
  • ISBN : 1845695755
  • Language : En, Es, Fr & De
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Recent advances in biochemistry and biotechnology have enabled significant progress in basic research on carbohydrate-active enzymes and advances in their effective application. The mechanism of catalytic reaction of carbohydrate-active enzymes is not fully understood, though, as they often show unusual substrate specificity and modes of action. This comprehensive collection summarises some of the most important research in the field of carbohydrate-active enzymes, focusing on the enzymatic reaction mechanism, structure-function relationship and role in the living organism The book is based on papers presented in the 2008 Agricultural Biotechnology Symposium Carbohydrate-active enzymes: structure, function and applications held on September 26th-27th 2008 in Seoul National University, Korea. This symposium was organized by the Center for Agricultural Biomaterials, Seoul National University, Korea, which has organized symposia on agricultural biotechnology annually since 1990. Many important results on new types of carbohydrate-active enzymes and their applications have been reported at these meetings. Papers in Part one of this collection focus on structure-function relationships of carbohydrate-active enzymes. Papers in Part two discuss functions and applications of carbohydrate-active enzymes, such as enzymes for grain processing and glycosidases and their mutants as useful tools for glycoside synthesis. With its distinguished editor and international team of contributors, Carbohydrate-active enzymes: structure, function and applications is an essential reference for research scientists, post-graduate students and those in the food industry with an interest in enzymes. Summarises some of the most important research in the field of carbohydrate-active enzymes Covers topics ranging from enzyme classification and structural elucidation to applications of enzymes in food processing and other industries

Carbohydrate-Active Enzymes

Carbohydrate-Active Enzymes
Structure, Activity and Reaction Products

by Stefano Benini

  • Publisher : MDPI
  • Release : 2020-06-18
  • Pages : 408
  • ISBN : 3039360906
  • Language : En, Es, Fr & De
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Carbohydrate-active enzymes are responsible for both biosynthesis and the breakdown of carbohydrates and glycoconjugates. They are involved in many metabolic pathways; in the biosynthesis and degradation of various biomolecules, such as bacterial exopolysaccharides, starch, cellulose and lignin; and in the glycosylation of proteins and lipids. Carbohydrate-active enzymes are classified into glycoside hydrolases, glycosyltransferases, polysaccharide lyases, carbohydrate esterases, and enzymes with auxiliary activities (CAZy database, www.cazy.org). Glycosyltransferases synthesize a huge variety of complex carbohydrates with different degrees of polymerization, moieties and branching. On the other hand, complex carbohydrate breakdown is carried out by glycoside hydrolases, polysaccharide lyases and carbohydrate esterases. Their interesting reactions have attracted the attention of researchers across scientific fields, ranging from basic research to biotechnology. Interest in carbohydrate-active enzymes is due not only to their ability to build and degrade biopolymers—which is highly relevant in biotechnology—but also because they are involved in bacterial biofilm formation, and in glycosylation of proteins and lipids, with important health implications. This book gathers new research results and reviews to broaden our understanding of carbohydrate-active enzymes, their mutants and their reaction products at the molecular level.

Carbohydrate-active Enzymes Metabolising Maltose

Carbohydrate-active Enzymes Metabolising Maltose
Kinetic and Structural Features

by Julia Smirnova

  • Publisher : Unknown Publisher
  • Release : 2012
  • Pages : 324
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Structural Studies of Carbohydrate Active Enzymes

Structural Studies of Carbohydrate Active Enzymes
A Book

by Carlos Martinez Fleites

  • Publisher : Unknown Publisher
  • Release : 2006
  • Pages : 329
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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New approaches in starch science and carbohydrate active enzymes

New approaches in starch science and carbohydrate active enzymes
A Book

by Nihon Ōyō Toshitsu Kagakkai

  • Publisher : Unknown Publisher
  • Release : 2003
  • Pages : 329
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Computational Methods in the Study of Carbohydrates and Carbohydrate-active Enzymes

Computational Methods in the Study of Carbohydrates and Carbohydrate-active Enzymes
A Book

by Anthony David Hill

  • Publisher : Unknown Publisher
  • Release : 2006
  • Pages : 329
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Functional Characterization of Carbohydrate-active Enzymes from Marine Bacteria

Functional Characterization of Carbohydrate-active Enzymes from Marine Bacteria
A Book

by Marcus Bäumgen

  • Publisher : Unknown Publisher
  • Release : 2020
  • Pages : 329
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Strategies for the Discovery of Carbohydrate-active Enzymes from Environmental Bacteria

Strategies for the Discovery of Carbohydrate-active Enzymes from Environmental Bacteria
A Book

by Anonim

  • Publisher : Unknown Publisher
  • Release : 2013
  • Pages : 82
  • ISBN : 9789175018348
  • Language : En, Es, Fr & De
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Metagenome Derived Carbohydrate Active Enzymes for Directed Modification of Polyphenols

Metagenome Derived Carbohydrate Active Enzymes for Directed Modification of Polyphenols
Development of a TLC-based Functional Screening Method for Identification of Flavonoid Modifying Enzymes and the Isolation and Characterization of Flavonoid Modifying Glycosyltransferases and Glycoside Hydrolases

by Anonim

  • Publisher : Unknown Publisher
  • Release : 2013
  • Pages : 329
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Heterologous Expression, Characterization and Applications of Carbohydrate Active Enzymes and Binding Modules

Heterologous Expression, Characterization and Applications of Carbohydrate Active Enzymes and Binding Modules
A Book

by Åsa Kallas,Kungliga tekniska högskolan. Institutionen för bioteknologi

  • Publisher : Unknown Publisher
  • Release : 2006
  • Pages : 69
  • ISBN : 9789171783493
  • Language : En, Es, Fr & De
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Characterization of Carbohydrate Active Enzymes Involved in Arabinogalactan Protein Metabolism

Characterization of Carbohydrate Active Enzymes Involved in Arabinogalactan Protein Metabolism
A Book

by Anonim

  • Publisher : Unknown Publisher
  • Release : 2013
  • Pages : 159
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Plant Proteinaceous Inhibitors of Carbohydrate-active Enzymes

Plant Proteinaceous Inhibitors of Carbohydrate-active Enzymes
A Book

by Nathalie Juge

  • Publisher : Unknown Publisher
  • Release : 2004
  • Pages : 148
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Carbohydrate-active Enzymes that Modify the Cell Wall of Aspergillus Niger

Carbohydrate-active Enzymes that Modify the Cell Wall of Aspergillus Niger
Biochemical Properties and Physiological Functions During Autolysis and Differentiation

by Marc Jos Elise Cornelis Maarel,Rijksuniversiteit Groningen

  • Publisher : Unknown Publisher
  • Release : 2014
  • Pages : 329
  • ISBN : 9789036772372
  • Language : En, Es, Fr & De
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Characterization and Engineering of Carbohydrate-active Enzymes for Biotechnological Applications

Characterization and Engineering of Carbohydrate-active Enzymes for Biotechnological Applications
A Book

by Anonim

  • Publisher : Unknown Publisher
  • Release : 2015
  • Pages : 57
  • ISBN : 9789175955117
  • Language : En, Es, Fr & De
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Structural Studies of Industrial Dehydrogenases and Two Additional Carbohydrate Active Enzymes

Structural Studies of Industrial Dehydrogenases and Two Additional Carbohydrate Active Enzymes
PhD Thesis

by Harm Otten

  • Publisher : Unknown Publisher
  • Release : 2011
  • Pages : 329
  • ISBN : 9788799503001
  • Language : En, Es, Fr & De
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Discovery and Characterization of Novel Carbohydrate-active Enzymes from Marine Bacteria

Discovery and Characterization of Novel Carbohydrate-active Enzymes from Marine Bacteria
A Book

by Lukas Reisky

  • Publisher : Unknown Publisher
  • Release : 2019
  • Pages : 329
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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Biochemical and Structural Characterization of Two Thermostable Carbohydrate-active Enzymes with Potential in Biotechnological Applications

Biochemical and Structural Characterization of Two Thermostable Carbohydrate-active Enzymes with Potential in Biotechnological Applications
A Book

by Anonim

  • Publisher : Unknown Publisher
  • Release : 2014
  • Pages : 49
  • ISBN : 9789175950945
  • Language : En, Es, Fr & De
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Carbohydrate Bioengineering

Carbohydrate Bioengineering
Interdisciplinary Approaches

by Tuula T Teeri,B Svensson,H J Gilbert,T Feizi

  • Publisher : Royal Society of Chemistry
  • Release : 2007-10-31
  • Pages : 206
  • ISBN : 1847550320
  • Language : En, Es, Fr & De
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Carbohydrate bioengineering is a rapidly expanding field with many applications in medicine and industry. Presenting state-of-the-art research, Carbohydrate Bioengineering: Interdisciplinary Approaches brings together international experts on many different aspects of this burgeoning topic. Coverage includes: the engineering of glycosidases for constructive purposes; structure-function studies and protein engineering of carbohydrate-active enzymes; chemo-enzymatic carbohydrate synthesis; and trends emerging from comprehensive work on genomes and glycomes. This timely publication will be welcomed by all those needing access to the latest research in the field, including practitioners in the medicinal, chemical, food and pharmaceutical areas.

Modification of Carbohydrate Active Enzymes in Switchgrass (Panicum Virgatum L.) to Improve Saccharification and Biomass Yields for Biofuels

Modification of Carbohydrate Active Enzymes in Switchgrass (Panicum Virgatum L.) to Improve Saccharification and Biomass Yields for Biofuels
A Book

by Jonathan Duran Willis

  • Publisher : Unknown Publisher
  • Release : 2016
  • Pages : 214
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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The natural recalcitrance of plant cell walls is a major commercial hurdle for plant biomass to be converted into a viable energy source as alternative to fossil fuels. To circumvent this hurdle manipulation of carbohydrate enzymes active in the cellulose and hemicellulose portions of the plant cell wall can be utilized to improve feedstocks. Production of cellulolytic enzymes by plants have been evaluated for reducing the cost associated with lignocellulosic biofuels. Plants have successfully served as bioreactors producing bacterial and fungal glycosyl hydrolases, which have altered plant growth to improve saccharification. A bioprospecting opportunity lies with the utilization of insect glycosyl hydrolases for transgenic production in plants. Lessons learned from microbial hydrolase expression can be applied to insect hydrolase expression along with gene stacking to develop autohydrolysis plant lines. A step toward production of insect cellulases in plants was performed by insertion of the endoglucanase TcEG1 gene, from Tribolium castaneum, into switchgrass. Transgenic lines overexpressing TcEG1 produced a functional enzyme with an optimal alkaline pH activity of 12.0. Recalcitrance was assayed by performing saccharification analysis, in which one line was superior over non-transgenic control; this line also had reduced 9% lignin content. Transgenic lines developed narrow stems, although biomass yield was unchanged due to increased tiller number and cell wall thickness. Grasses contain a relatively high amount of glucoarabinoxylan in their cell walls, which cross links with lignin. By down-regulation of a uridine diphosphate arabinomutase (UAM) gene via RNAi, it was hypothesized that attenuated production of this carbohydrate transferase would increase saccharification of switchgrass biomass from a disruption of cross linking. Transgenic events showed a reduction in arabinose content (up to 58%) and altered arabino-side chains, however saccharification was unchanged. UAM transgenic switchgrass showed a red node phenotype, which could be in response to increased lignin biosynthesis. A model of UAMinfluenced cell wall interactions was proposed and will used to build hypotheses for future - omics research. In summary, switchgrass saccharification and biomass yield can be increased by introduction of carbohydrate active enzymes. Combination of presented transgenic lines with low-lignin germplasm could be utilized to further improve saccharification yield.

Genome-wide Analysis of Carbohydrate Active Enzyme Diversity and Expression in Eucalyptus Grandis

Genome-wide Analysis of Carbohydrate Active Enzyme Diversity and Expression in Eucalyptus Grandis
A Book

by Desré Pinard

  • Publisher : Unknown Publisher
  • Release : 2013
  • Pages : 218
  • ISBN : 9876543210XXX
  • Language : En, Es, Fr & De
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The woody biomass derived from tree species forms a vital part of the world’s economy, and a thorough understanding of the processes of carbon sequestration and carbohydrate metabolism in trees is paramount in ensuring efficient and sustainable use of this biomass. To date, there is still much to be learnt about wood formation and polysaccharide deposition in plant cell walls. The enzymes responsible for the synthesis, degradation, and modification of polysaccharides and glycosidic bonds are known as Carbohydrate Active enZymes (CAZymes) are organized into functional classes and families based on amino acid sequence. CAZymes in plant genomes can be analyzed using the functional protein domains that form the proteins in order to better understand the functional potential of the carbohydrate metabolism strategy employed by plants. The glycosyltransferase (GT) class of CAZyme domains is responsible for the synthesis of glycosidic bonds, and the glycosylhydrolases (GH), polysaccharide lyase (PL), and carbohydrate esterase (CE) CAZyme domain classes degrade and modify these bonds. The final class of CAZyme domains is the non-enzymatic carbohydrate binding modules (CBMs), which act to increase the activity of the enzymatic CAZyme domain classes via specific binding to polysaccharides, disruption of the cell wall polysaccharide matrix, and proximity effects when appended to enzymatic CAZyme domains in complex CAZyme domain containing proteins. In this project, we used comparative genomics and transcriptomics of CAZyme domains to analyze the functional building blocks of plant carbohydrate metabolism to gain insight into the process of wood formation, with a specific focus on the biomass feedstock crop, Eucalyptus grandis. The aim of this project was to compare the CAZyme domain frequency, diversity and complexity across plant genomes representative of the major land plant lineages and green algae species to identify any delineating factors that contribute to wood formation in tree species. In addition, we analyzed the expression levels of CAZyme domains in the transcriptomes of source and sink tissues in E. grandis and Populus trichocarpa to better understand the expression investment in carbohydrate metabolism in different tissues of divergent tree species. The results show conservation of a fundamental functional strategy for carbohydrate metabolism across land plant evolution. The ratio of CAZyme domain frequency is maintained in land plants, with GTs contributing ?40% of the genomic CAZyme domain content, highlighting the importance of polysaccharide synthesis in plants. The diversity of CAZyme domain families within each class cannot be used to differentiate the genomes of major land plant lineages (lycophytes and bryophytes, monocots, and dicots) from one another, however, species-specific differences in CAZyme domain family diversity are observed. The complexity of CAZyme domain containing proteins shows that CAZyme domains are not very promiscuous, repeated CAZyme domains within a protein are more common than unique combinations of CAZyme domains within a protein, which are also conserved for the most part. The analysis of CAZyme domain expression in six tissues in E. grandis showed that in the wood forming tissue, immature xylem, GT domain families responsible for cellulose and hemicellulose biosynthesis formed the majority of the transcript abundance, a pattern not seen in the other tissues analyzed. This pattern was conserved in P. trichocarpa, highlighting the conserved mechanism for wood formation between divergent tree species. The results of this study reveal the conservation of the fundamental functional machinery responsible for carbohydrate metabolism in land plants, and highlight the importance of differential regulation of this machinery to wood formation. The long-term goal of improving the production of lignocellulosic biomass from trees will be achieved by fully understanding the regulatory mechanisms controlling the concerted expression of these CAZyme domain-containing genes.