Carbohydrate-Active Enzymes

Structure, Activity and Reaction Products

Edited by
June 2020
408 pages
  • ISBN978-3-03936-090-1 (Paperback)
  • ISBN978-3-03936-091-8 (PDF)

This book is a reprint of the Special Issue Carbohydrate-Active Enzymes: Structure, Activity and Reaction Products that was published in

Biology & Life Sciences
Chemistry & Materials Science
Medicine & Pharmacology
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, 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.
  • Paperback
License and Copyright
© 2020 by the authors; CC BY-NC-ND license
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; glycosyltransferase; applied biocatalysis; enzyme cascades; chemoenzymatic synthesis; sugar chemistry; carbohydrate; Leloir; nucleotide; Enzymatic glycosylation; alkyl glycosides (AG)s; Deep eutectic solvents (DES); Amy A; alcoholysis; hydrolysis; methanol; circular dichroism; protein stability; alpha-amylase; biomass; hemicellulose; bioethanol; xylanolytic enzyme; hemicellulase; glycoside hydrolase; 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; glycoside hydrolase; cellulose degradation; thermophilic fungus; β-glucosidases; Chaetomium thermophilum; protein structure; fungal enzymes; endo-α-(16)-d-mannase; mannoside; Mycobacterium; lipomannan; lipoarabinomannan; phosphatidylinositol mannosides; glycoside hydrolase; GH68; fructosyltransferase; fructooligosaccharides; FOS biosynthesis; prebiotic oligosaccharides; Arxula adeninivorans; glycoside hydrolase; α-glucosidase; maltose; panose; amylopectin; glycogen; inhibition by Tris; transglycosylation; glycoside hydrolyase; Trichoderma harzianum; complete saccharification; lignocellulose; N-acetylhexosamine specificity; glycoside hydrolase; GH20; phylogenetic analysis; transglycosylation; 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

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