Molecular Biocatalysis 2.0

Biotransformation 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 o...

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Year of Publication:2020
Language:English
Physical Description:1 electronic resource (166 p.)
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520 |a Biotransformation 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 β-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. 
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650 7 |a Technology: general issues  |2 bicssc 
653 |a E. coli 
653 |a recombinant horseradish peroxidase 
653 |a site-directed mutagenesis 
653 |a periplasm 
653 |a glycosylation sites 
653 |a Aspergillus niger 
653 |a quercetin 
653 |a rutin 
653 |a rutinose 
653 |a rutinosidase 
653 |a "solid-state biocatalysis" 
653 |a hyaluronic acid 
653 |a in vitro synthesis 
653 |a one-pot multi-enzyme 
653 |a optimization 
653 |a enzyme cascade 
653 |a Basidiomycota 
653 |a Agaricomycotina 
653 |a nitrilase 
653 |a cyanide hydratase 
653 |a nitrile 
653 |a substrate specificity 
653 |a overproduction 
653 |a homology modeling 
653 |a substrate docking 
653 |a phylogenetic distribution 
653 |a indigo 
653 |a MISO library 
653 |a flavin 
653 |a monooxygenase 
653 |a FMO 
653 |a β-N-acetylhexosaminidases 
653 |a transglycosylation 
653 |a Glide docking 
653 |a Talaromyces flavus 
653 |a muramic acid 
653 |a non-reducing carbohydrate 
653 |a glucose oxidase 
653 |a direct electron transfer 
653 |a amine-reactive phenazine ethosulfate 
653 |a glucose sensor 
653 |a glycemic level monitoring 
653 |a Pseudomonas putida MnB1 
653 |a biogenic manganese oxides 
653 |a abiotic manganese oxides 
653 |a α-Hydroxy-β-keto esters 
653 |a whole-cell biocatalysis 
653 |a surface display 
653 |a cell wall anchor 
653 |a Lactobacillus plantarum 
653 |a whole-cell biocatalyst 
653 |a Fe(II)/2-ketoglutarate-dependent dioxygenase 
653 |a 2-ketoglutarate generation 
653 |a regio- and stereo-selective synthesis 
653 |a hydroxy amino acids 
653 |a sequential cascade reaction 
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