LEADER 06703nam 2201825z- 450 001 9910557134503321 005 20231214132838.0 035 $a(CKB)5400000000040708 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/68651 035 $a(EXLCZ)995400000000040708 100 $a20202105d2020 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aCarbohydrate-Active Enzymes$eStructure, Activity and Reaction Products 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2020 215 $a1 electronic resource (408 p.) 311 $a3-03936-090-6 311 $a3-03936-091-4 330 $aCarbohydrate-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. 517 $aCarbohydrate-Active Enzymes 606 $aResearch & information: general$2bicssc 606 $aBiology, life sciences$2bicssc 610 $aglycoside hydrolase 610 $axylanase 610 $acarbohydrate-binding module 610 $aCBM truncation 610 $ahalo-tolerant 610 $axylan hydrolysis 610 $apectate lyase 610 $aPaenibacillus polymyxa 610 $apectins 610 $adegradation 610 $aLactobacillus 610 $aGH13_18 610 $asucrose phosphorylase 610 $aglycoside phosphorylase 610 $aIlumatobacter coccineus 610 $aThermoanaerobacterium thermosaccharolyticum 610 $acrystallography 610 $agalactosidase 610 $ahydrolysis 610 $areaction mechanism 610 $acomplex structures 610 $acold-adapted 610 $aGH2 610 $aCellulase 610 $arandom mutagenesis 610 $acellulose degradation 610 $astructural analysis 610 $a?-amylase 610 $astarch degradation 610 $abiotechnology 610 $astructure 610 $apyruvylation 610 $apyruvyltransferase 610 $aexopolysaccharides 610 $acapsular polysaccharides 610 $acell wall glycopolymers 610 $aN-glycans 610 $alipopolysaccharides 610 $abiosynthesis 610 $asequence space 610 $apyruvate analytics 610 $aNanopore sequencing 610 $aganoderic acid 610 $aBacillus thuringiensis 610 $abiotransformation 610 $aglycosyltransferase 610 $awhole genome sequencing 610 $aapplied biocatalysis 610 $aenzyme cascades 610 $achemoenzymatic synthesis 610 $asugar chemistry 610 $acarbohydrate 610 $aLeloir 610 $anucleotide 610 $aEnzymatic glycosylation 610 $aalkyl glycosides (AG)s 610 $aDeep eutectic solvents (DES) 610 $aAmy A 610 $aalcoholysis 610 $amethanol 610 $acircular dichroism 610 $aprotein stability 610 $aalpha-amylase 610 $abiomass 610 $ahemicellulose 610 $abioethanol 610 $axylanolytic enzyme 610 $ahemicellulase 610 $alysozyme 610 $apeptidoglycan cleavage 610 $aavian gut GH22 610 $acrystal structure 610 $aglycosylation 610 $aUDP-glucose pyrophosphorylase 610 $aUDP-glucose 610 $anucleotide donors 610 $aRhodococcus, Actinobacteria, gene redundancy 610 $aLeloir glycosyltransferases 610 $aactivated sugar 610 $aUTP 610 $athermophilic fungus 610 $a?-glucosidases 610 $aChaetomium thermophilum 610 $aprotein structure 610 $afungal enzymes 610 $aendo-?-(1?6)-d-mannase 610 $amannoside 610 $aMycobacterium 610 $alipomannan 610 $alipoarabinomannan 610 $aphosphatidylinositol mannosides 610 $aGH68 610 $afructosyltransferase 610 $afructooligosaccharides 610 $aFOS biosynthesis 610 $aprebiotic oligosaccharides 610 $aArxula adeninivorans 610 $a?-glucosidase 610 $amaltose 610 $apanose 610 $aamylopectin 610 $aglycogen 610 $ainhibition by Tris 610 $atransglycosylation 610 $aglycoside hydrolyase 610 $aTrichoderma harzianum 610 $acomplete saccharification 610 $alignocellulose 610 $aN-acetylhexosamine specificity 610 $aGH20 610 $aphylogenetic analysis 610 $aNAG-oxazoline 610 $aacceptor diversity 610 $alacto-N-triose II 610 $ahuman milk oligosaccharides 610 $aNMR 610 $amolecular phylogeny 610 $a?2,8-sialyltransferases 610 $apolySia motifs 610 $aevolution 610 $aST8Sia 610 $afunctional genomics 615 7$aResearch & information: general 615 7$aBiology, life sciences 700 $aBenini$b Stefano$4edt$0564835 702 $aBenini$b Stefano$4oth 906 $aBOOK 912 $a9910557134503321 996 $aCarbohydrate-Active Enzymes$93027624 997 $aUNINA