LEADER 04547nam 2201045z- 450 001 9910557576703321 005 20210501 035 $a(CKB)5400000000043882 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/69179 035 $a(oapen)doab69179 035 $a(EXLCZ)995400000000043882 100 $a20202105d2020 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aMolecular Biocatalysis 2.0 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2020 215 $a1 online resource (166 p.) 311 08$a3-03943-278-8 311 08$a3-03943-279-6 330 $aBiotransformation has accompanied mankind since the Neolithic community, when people settled down and began to engage in agriculture. Modern biocatalysis started in the mid-1850s with the pioneer works of Pasteur. Today, biotransformations have become an indispensable part of our lives, similar to other hi-tech products. Now, in 2019, biocatalysis "received" the Nobel Prize in Chemistry due to prof. Frances H. Arnold's achievements in the area of the directed evolution of enzymes. This book deals with some major topics of biotransformation, such as the application of enzymatic methods in glycobiology, including the synthesis of hyaluronan, complex glycoconjugates of N-acetylmuramic acid, and the enzymatic deglycosylation of rutin. Enzymatic redox reactions were exemplified by the enzymatic synthesis of indigo from indole, oxidations of ?-ketoesters and the engineering of a horse radish peroxidase. The enzymatic reactions were elegantly employed in biosensors, such as glucose oxidase, in the case of electrochemical glucose sensors. Nitrilases are important enzymes for nitrile metabolism in plants and microorganisms have already found broad application in industry-here, these enzymes were for the first time described in Basidiomyceta. This book nicely describes molecular biocatalysis as a pluripotent methodology-"A jack of all trades..."-which strongly contributes to the high quality and sustainability of our daily lives. 606 $aTechnology: general issues$2bicssc 610 $a"solid-state biocatalysis" 610 $a2-ketoglutarate generation 610 $aabiotic manganese oxides 610 $aAgaricomycotina 610 $aamine-reactive phenazine ethosulfate 610 $aAspergillus niger 610 $aBasidiomycota 610 $abiogenic manganese oxides 610 $acell wall anchor 610 $acyanide hydratase 610 $adirect electron transfer 610 $aE. coli 610 $aenzyme cascade 610 $aFe(II)/2-ketoglutarate-dependent dioxygenase 610 $aflavin 610 $aFMO 610 $aGlide docking 610 $aglucose oxidase 610 $aglucose sensor 610 $aglycemic level monitoring 610 $aglycosylation sites 610 $ahomology modeling 610 $ahyaluronic acid 610 $ahydroxy amino acids 610 $ain vitro synthesis 610 $aindigo 610 $aLactobacillus plantarum 610 $aMISO library 610 $amonooxygenase 610 $amuramic acid 610 $an/a 610 $anitrilase 610 $anitrile 610 $anon-reducing carbohydrate 610 $aone-pot multi-enzyme 610 $aoptimization 610 $aoverproduction 610 $aperiplasm 610 $aphylogenetic distribution 610 $aPseudomonas putida MnB1 610 $aquercetin 610 $arecombinant horseradish peroxidase 610 $aregio- and stereo-selective synthesis 610 $arutin 610 $arutinose 610 $arutinosidase 610 $asequential cascade reaction 610 $asite-directed mutagenesis 610 $asubstrate docking 610 $asubstrate specificity 610 $asurface display 610 $aTalaromyces flavus 610 $atransglycosylation 610 $awhole-cell biocatalysis 610 $awhole-cell biocatalyst 610 $a?-Hydroxy-?-keto esters 610 $a?-N-acetylhexosaminidases 615 7$aTechnology: general issues 700 $aKr?en$b Vladimi?r$4edt$0367039 702 $aBojarova?$b Pavla$4edt 702 $aKr?en$b Vladimi?r$4oth 702 $aBojarova?$b Pavla$4oth 906 $aBOOK 912 $a9910557576703321 996 $aMolecular Biocatalysis 2.0$93021312 997 $aUNINA