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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.

Research & information: general --- Biology, life sciences --- 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 --- 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

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The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals

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• Reference Manager
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• RefWorks (Direct export to RefWorks)

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.

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

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals