TY - GEN AU - Benini,Stefano AU - Benini,Stefano TI - Carbohydrate-Active Enzymes : Structure, Activity and Reaction Products SN - books978-3-03936-091-8 PY - 2020/// CY - Basel, Switzerland PB - MDPI - Multidisciplinary Digital Publishing Institute KW - Research & information: general KW - bicssc KW - Biology, life sciences KW - glycoside hydrolase KW - xylanase KW - carbohydrate-binding module KW - CBM truncation KW - halo-tolerant KW - xylan hydrolysis KW - pectate lyase KW - Paenibacillus polymyxa KW - pectins KW - degradation KW - Lactobacillus KW - GH13_18 KW - sucrose phosphorylase KW - glycoside phosphorylase KW - Ilumatobacter coccineus KW - Thermoanaerobacterium thermosaccharolyticum KW - crystallography KW - galactosidase KW - hydrolysis KW - reaction mechanism KW - complex structures KW - cold-adapted KW - GH2 KW - Cellulase KW - random mutagenesis KW - cellulose degradation KW - structural analysis KW - α-amylase KW - starch degradation KW - biotechnology KW - structure KW - pyruvylation KW - pyruvyltransferase KW - exopolysaccharides KW - capsular polysaccharides KW - cell wall glycopolymers KW - N-glycans KW - lipopolysaccharides KW - biosynthesis KW - sequence space KW - pyruvate analytics KW - Nanopore sequencing KW - ganoderic acid KW - Bacillus thuringiensis KW - biotransformation KW - glycosyltransferase KW - whole genome sequencing KW - applied biocatalysis KW - enzyme cascades KW - chemoenzymatic synthesis KW - sugar chemistry KW - carbohydrate KW - Leloir KW - nucleotide KW - Enzymatic glycosylation KW - alkyl glycosides (AG)s KW - Deep eutectic solvents (DES) KW - Amy A KW - alcoholysis KW - methanol KW - circular dichroism KW - protein stability KW - alpha-amylase KW - biomass KW - hemicellulose KW - bioethanol KW - xylanolytic enzyme KW - hemicellulase KW - lysozyme KW - peptidoglycan cleavage KW - avian gut GH22 KW - crystal structure KW - glycosylation KW - UDP-glucose pyrophosphorylase KW - UDP-glucose KW - nucleotide donors KW - Rhodococcus, Actinobacteria, gene redundancy KW - Leloir glycosyltransferases KW - activated sugar KW - UTP KW - thermophilic fungus KW - β-glucosidases KW - Chaetomium thermophilum KW - protein structure KW - fungal enzymes KW - endo-α-(1→6)-d-mannase KW - mannoside KW - Mycobacterium KW - lipomannan KW - lipoarabinomannan KW - phosphatidylinositol mannosides KW - GH68 KW - fructosyltransferase KW - fructooligosaccharides KW - FOS biosynthesis KW - prebiotic oligosaccharides KW - Arxula adeninivorans KW - α-glucosidase KW - maltose KW - panose KW - amylopectin KW - glycogen KW - inhibition by Tris KW - transglycosylation KW - glycoside hydrolyase KW - Trichoderma harzianum KW - complete saccharification KW - lignocellulose KW - N-acetylhexosamine specificity KW - GH20 KW - phylogenetic analysis KW - NAG-oxazoline KW - acceptor diversity KW - lacto-N-triose II KW - human milk oligosaccharides KW - NMR KW - molecular phylogeny KW - α2,8-sialyltransferases KW - polySia motifs KW - evolution KW - ST8Sia KW - functional genomics KW - n/a N1 - Open Access N2 - 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 UR - https://mdpi.com/books/pdfview/book/2413 UR - https://directory.doabooks.org/handle/20.500.12854/68651 ER -