06703nam 2201825z- 450 991055713450332120231214132838.0(CKB)5400000000040708(oapen)https://directory.doabooks.org/handle/20.500.12854/68651(EXLCZ)99540000000004070820202105d2020 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierCarbohydrate-Active EnzymesStructure, Activity and Reaction ProductsBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20201 electronic resource (408 p.)3-03936-090-6 3-03936-091-4 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 Research & information: generalbicsscBiology, life sciencesbicsscglycoside hydrolasexylanasecarbohydrate-binding moduleCBM truncationhalo-tolerantxylan hydrolysispectate lyasePaenibacillus polymyxapectinsdegradationLactobacillusGH13_18sucrose phosphorylaseglycoside phosphorylaseIlumatobacter coccineusThermoanaerobacterium thermosaccharolyticumcrystallographygalactosidasehydrolysisreaction mechanismcomplex structurescold-adaptedGH2Cellulaserandom mutagenesiscellulose degradationstructural analysisα-amylasestarch degradationbiotechnologystructurepyruvylationpyruvyltransferaseexopolysaccharidescapsular polysaccharidescell wall glycopolymersN-glycanslipopolysaccharidesbiosynthesissequence spacepyruvate analyticsNanopore sequencingganoderic acidBacillus thuringiensisbiotransformationglycosyltransferasewhole genome sequencingapplied biocatalysisenzyme cascadeschemoenzymatic synthesissugar chemistrycarbohydrateLeloirnucleotideEnzymatic glycosylationalkyl glycosides (AG)sDeep eutectic solvents (DES)Amy Aalcoholysismethanolcircular dichroismprotein stabilityalpha-amylasebiomasshemicellulosebioethanolxylanolytic enzymehemicellulaselysozymepeptidoglycan cleavageavian gut GH22crystal structureglycosylationUDP-glucose pyrophosphorylaseUDP-glucosenucleotide donorsRhodococcus, Actinobacteria, gene redundancyLeloir glycosyltransferasesactivated sugarUTPthermophilic fungusβ-glucosidasesChaetomium thermophilumprotein structurefungal enzymesendo-α-(1→6)-d-mannasemannosideMycobacteriumlipomannanlipoarabinomannanphosphatidylinositol mannosidesGH68fructosyltransferasefructooligosaccharidesFOS biosynthesisprebiotic oligosaccharidesArxula adeninivoransα-glucosidasemaltosepanoseamylopectinglycogeninhibition by Tristransglycosylationglycoside hydrolyaseTrichoderma harzianumcomplete saccharificationlignocelluloseN-acetylhexosamine specificityGH20phylogenetic analysisNAG-oxazolineacceptor diversitylacto-N-triose IIhuman milk oligosaccharidesNMRmolecular phylogenyα2,8-sialyltransferasespolySia motifsevolutionST8Siafunctional genomicsResearch & information: generalBiology, life sciencesBenini Stefanoedt564835Benini StefanoothBOOK9910557134503321Carbohydrate-Active Enzymes3027624UNINA