Carbohydrate-Active Enzymes
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...
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MDPI - Multidisciplinary Digital Publishing Institute
2021
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| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-68651 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-686512024-03-28T03:33:52Z Carbohydrate-Active Enzymes Benini, Stefano glycoside hydrolase xylanase carbohydrate-binding module CBM truncation halo-tolerant xylan hydrolysis pectate lyase Paenibacillus polymyxa pectins degradation Lactobacillus GH13_18 sucrose phosphorylase glycoside phosphorylase Ilumatobacter coccineus Thermoanaerobacterium thermosaccharolyticum crystallography galactosidase hydrolysis reaction mechanism complex structures cold-adapted GH2 Cellulase random mutagenesis cellulose degradation structural analysis α-amylase starch degradation biotechnology structure pyruvylation pyruvyltransferase exopolysaccharides capsular polysaccharides cell wall glycopolymers N-glycans lipopolysaccharides biosynthesis sequence space pyruvate analytics Nanopore sequencing ganoderic acid Bacillus thuringiensis biotransformation glycosyltransferase whole genome sequencing applied biocatalysis enzyme cascades chemoenzymatic synthesis sugar chemistry carbohydrate Leloir nucleotide Enzymatic glycosylation alkyl glycosides (AG)s Deep eutectic solvents (DES) Amy A alcoholysis methanol circular dichroism protein stability alpha-amylase biomass hemicellulose bioethanol xylanolytic enzyme hemicellulase lysozyme peptidoglycan cleavage avian gut GH22 crystal structure glycosylation UDP-glucose pyrophosphorylase UDP-glucose nucleotide donors Rhodococcus, Actinobacteria, gene redundancy Leloir glycosyltransferases activated sugar UTP thermophilic fungus β-glucosidases Chaetomium thermophilum protein structure fungal enzymes endo-α-(1→6)-d-mannase mannoside Mycobacterium lipomannan lipoarabinomannan phosphatidylinositol mannosides GH68 fructosyltransferase fructooligosaccharides FOS biosynthesis prebiotic oligosaccharides Arxula adeninivorans α-glucosidase maltose panose amylopectin glycogen inhibition by Tris transglycosylation glycoside hydrolyase Trichoderma harzianum complete saccharification lignocellulose N-acetylhexosamine specificity GH20 phylogenetic analysis NAG-oxazoline acceptor diversity lacto-N-triose II human milk oligosaccharides NMR molecular phylogeny α2,8-sialyltransferases polySia motifs evolution ST8Sia functional genomics n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences 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. 2021-05-01T15:16:42Z 2021-05-01T15:16:42Z 2020 book ONIX_20210501_9783039360901_397 9783039360901 9783039360918 https://directory.doabooks.org/handle/20.500.12854/68651 eng application/octet-stream Attribution 4.0 International https://mdpi.com/books/pdfview/book/2413 https://mdpi.com/books/pdfview/book/2413 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-03936-091-8 10.3390/books978-3-03936-091-8 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783039360901 9783039360918 408 Basel, Switzerland open access |
| spellingShingle | glycoside hydrolase xylanase carbohydrate-binding module CBM truncation halo-tolerant xylan hydrolysis pectate lyase Paenibacillus polymyxa pectins degradation Lactobacillus GH13_18 sucrose phosphorylase glycoside phosphorylase Ilumatobacter coccineus Thermoanaerobacterium thermosaccharolyticum crystallography galactosidase hydrolysis reaction mechanism complex structures cold-adapted GH2 Cellulase random mutagenesis cellulose degradation structural analysis α-amylase starch degradation biotechnology structure pyruvylation pyruvyltransferase exopolysaccharides capsular polysaccharides cell wall glycopolymers N-glycans lipopolysaccharides biosynthesis sequence space pyruvate analytics Nanopore sequencing ganoderic acid Bacillus thuringiensis biotransformation glycosyltransferase whole genome sequencing applied biocatalysis enzyme cascades chemoenzymatic synthesis sugar chemistry carbohydrate Leloir nucleotide Enzymatic glycosylation alkyl glycosides (AG)s Deep eutectic solvents (DES) Amy A alcoholysis methanol circular dichroism protein stability alpha-amylase biomass hemicellulose bioethanol xylanolytic enzyme hemicellulase lysozyme peptidoglycan cleavage avian gut GH22 crystal structure glycosylation UDP-glucose pyrophosphorylase UDP-glucose nucleotide donors Rhodococcus, Actinobacteria, gene redundancy Leloir glycosyltransferases activated sugar UTP thermophilic fungus β-glucosidases Chaetomium thermophilum protein structure fungal enzymes endo-α-(1→6)-d-mannase mannoside Mycobacterium lipomannan lipoarabinomannan phosphatidylinositol mannosides GH68 fructosyltransferase fructooligosaccharides FOS biosynthesis prebiotic oligosaccharides Arxula adeninivorans α-glucosidase maltose panose amylopectin glycogen inhibition by Tris transglycosylation glycoside hydrolyase Trichoderma harzianum complete saccharification lignocellulose N-acetylhexosamine specificity GH20 phylogenetic analysis NAG-oxazoline acceptor diversity lacto-N-triose II human milk oligosaccharides NMR molecular phylogeny α2,8-sialyltransferases polySia motifs evolution ST8Sia functional genomics n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences Carbohydrate-Active Enzymes |
| title | Carbohydrate-Active Enzymes |
| title_full | Carbohydrate-Active Enzymes |
| title_fullStr | Carbohydrate-Active Enzymes |
| title_full_unstemmed | Carbohydrate-Active Enzymes |
| title_short | Carbohydrate-Active Enzymes |
| title_sort | carbohydrate active enzymes |
| topic | glycoside hydrolase xylanase carbohydrate-binding module CBM truncation halo-tolerant xylan hydrolysis pectate lyase Paenibacillus polymyxa pectins degradation Lactobacillus GH13_18 sucrose phosphorylase glycoside phosphorylase Ilumatobacter coccineus Thermoanaerobacterium thermosaccharolyticum crystallography galactosidase hydrolysis reaction mechanism complex structures cold-adapted GH2 Cellulase random mutagenesis cellulose degradation structural analysis α-amylase starch degradation biotechnology structure pyruvylation pyruvyltransferase exopolysaccharides capsular polysaccharides cell wall glycopolymers N-glycans lipopolysaccharides biosynthesis sequence space pyruvate analytics Nanopore sequencing ganoderic acid Bacillus thuringiensis biotransformation glycosyltransferase whole genome sequencing applied biocatalysis enzyme cascades chemoenzymatic synthesis sugar chemistry carbohydrate Leloir nucleotide Enzymatic glycosylation alkyl glycosides (AG)s Deep eutectic solvents (DES) Amy A alcoholysis methanol circular dichroism protein stability alpha-amylase biomass hemicellulose bioethanol xylanolytic enzyme hemicellulase lysozyme peptidoglycan cleavage avian gut GH22 crystal structure glycosylation UDP-glucose pyrophosphorylase UDP-glucose nucleotide donors Rhodococcus, Actinobacteria, gene redundancy Leloir glycosyltransferases activated sugar UTP thermophilic fungus β-glucosidases Chaetomium thermophilum protein structure fungal enzymes endo-α-(1→6)-d-mannase mannoside Mycobacterium lipomannan lipoarabinomannan phosphatidylinositol mannosides GH68 fructosyltransferase fructooligosaccharides FOS biosynthesis prebiotic oligosaccharides Arxula adeninivorans α-glucosidase maltose panose amylopectin glycogen inhibition by Tris transglycosylation glycoside hydrolyase Trichoderma harzianum complete saccharification lignocellulose N-acetylhexosamine specificity GH20 phylogenetic analysis NAG-oxazoline acceptor diversity lacto-N-triose II human milk oligosaccharides NMR molecular phylogeny α2,8-sialyltransferases polySia motifs evolution ST8Sia functional genomics n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| topic_facet | glycoside hydrolase xylanase carbohydrate-binding module CBM truncation halo-tolerant xylan hydrolysis pectate lyase Paenibacillus polymyxa pectins degradation Lactobacillus GH13_18 sucrose phosphorylase glycoside phosphorylase Ilumatobacter coccineus Thermoanaerobacterium thermosaccharolyticum crystallography galactosidase hydrolysis reaction mechanism complex structures cold-adapted GH2 Cellulase random mutagenesis cellulose degradation structural analysis α-amylase starch degradation biotechnology structure pyruvylation pyruvyltransferase exopolysaccharides capsular polysaccharides cell wall glycopolymers N-glycans lipopolysaccharides biosynthesis sequence space pyruvate analytics Nanopore sequencing ganoderic acid Bacillus thuringiensis biotransformation glycosyltransferase whole genome sequencing applied biocatalysis enzyme cascades chemoenzymatic synthesis sugar chemistry carbohydrate Leloir nucleotide Enzymatic glycosylation alkyl glycosides (AG)s Deep eutectic solvents (DES) Amy A alcoholysis methanol circular dichroism protein stability alpha-amylase biomass hemicellulose bioethanol xylanolytic enzyme hemicellulase lysozyme peptidoglycan cleavage avian gut GH22 crystal structure glycosylation UDP-glucose pyrophosphorylase UDP-glucose nucleotide donors Rhodococcus, Actinobacteria, gene redundancy Leloir glycosyltransferases activated sugar UTP thermophilic fungus β-glucosidases Chaetomium thermophilum protein structure fungal enzymes endo-α-(1→6)-d-mannase mannoside Mycobacterium lipomannan lipoarabinomannan phosphatidylinositol mannosides GH68 fructosyltransferase fructooligosaccharides FOS biosynthesis prebiotic oligosaccharides Arxula adeninivorans α-glucosidase maltose panose amylopectin glycogen inhibition by Tris transglycosylation glycoside hydrolyase Trichoderma harzianum complete saccharification lignocellulose N-acetylhexosamine specificity GH20 phylogenetic analysis NAG-oxazoline acceptor diversity lacto-N-triose II human milk oligosaccharides NMR molecular phylogeny α2,8-sialyltransferases polySia motifs evolution ST8Sia functional genomics n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| url | ONIX_20210501_9783039360901_397 |