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...
Saved in:
| 格式: | Online |
|---|---|
| 語言: | 英语 |
| 出版: |
MDPI - Multidisciplinary Digital Publishing Institute
2021
|
| 主題: | |
| 在線閱讀: | ONIX_20210501_9783039432783_925 |
| 標簽: |
沒有標簽, 成為第一個標記此記錄!
|
| _version_ | 1869528889933430784 |
|---|---|
| collection | Directory of Open Access Books |
| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-69179 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-691792024-04-09T23:15:44Z Molecular Biocatalysis 2.0 Křen, Vladimír Bojarová, Pavla E. coli recombinant horseradish peroxidase site-directed mutagenesis periplasm glycosylation sites Aspergillus niger quercetin rutin rutinose rutinosidase “solid-state biocatalysis” hyaluronic acid in vitro synthesis one-pot multi-enzyme optimization enzyme cascade Basidiomycota Agaricomycotina nitrilase cyanide hydratase nitrile substrate specificity overproduction homology modeling substrate docking phylogenetic distribution indigo MISO library flavin monooxygenase FMO β-N-acetylhexosaminidases transglycosylation Glide docking Talaromyces flavus muramic acid non-reducing carbohydrate glucose oxidase direct electron transfer amine-reactive phenazine ethosulfate glucose sensor glycemic level monitoring Pseudomonas putida MnB1 biogenic manganese oxides abiotic manganese oxides α-Hydroxy-β-keto esters whole-cell biocatalysis surface display cell wall anchor Lactobacillus plantarum whole-cell biocatalyst n/a Fe(II)/2-ketoglutarate-dependent dioxygenase 2-ketoglutarate generation regio- and stereo-selective synthesis hydroxy amino acids sequential cascade reaction thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TB Technology: general issues 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. 2021-05-01T15:43:08Z 2021-05-01T15:43:08Z 2020 book ONIX_20210501_9783039432783_925 9783039432783 9783039432790 https://directory.doabooks.org/handle/20.500.12854/69179 eng application/octet-stream Attribution 4.0 International https://mdpi.com/books/pdfview/book/2951 https://mdpi.com/books/pdfview/book/2951 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-03943-279-0 10.3390/books978-3-03943-279-0 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783039432783 9783039432790 166 Basel, Switzerland open access |
| spellingShingle | E. coli recombinant horseradish peroxidase site-directed mutagenesis periplasm glycosylation sites Aspergillus niger quercetin rutin rutinose rutinosidase “solid-state biocatalysis” hyaluronic acid in vitro synthesis one-pot multi-enzyme optimization enzyme cascade Basidiomycota Agaricomycotina nitrilase cyanide hydratase nitrile substrate specificity overproduction homology modeling substrate docking phylogenetic distribution indigo MISO library flavin monooxygenase FMO β-N-acetylhexosaminidases transglycosylation Glide docking Talaromyces flavus muramic acid non-reducing carbohydrate glucose oxidase direct electron transfer amine-reactive phenazine ethosulfate glucose sensor glycemic level monitoring Pseudomonas putida MnB1 biogenic manganese oxides abiotic manganese oxides α-Hydroxy-β-keto esters whole-cell biocatalysis surface display cell wall anchor Lactobacillus plantarum whole-cell biocatalyst n/a Fe(II)/2-ketoglutarate-dependent dioxygenase 2-ketoglutarate generation regio- and stereo-selective synthesis hydroxy amino acids sequential cascade reaction thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TB Technology: general issues Molecular Biocatalysis 2.0 |
| title | Molecular Biocatalysis 2.0 |
| title_full | Molecular Biocatalysis 2.0 |
| title_fullStr | Molecular Biocatalysis 2.0 |
| title_full_unstemmed | Molecular Biocatalysis 2.0 |
| title_short | Molecular Biocatalysis 2.0 |
| title_sort | molecular biocatalysis 2 0 |
| topic | E. coli recombinant horseradish peroxidase site-directed mutagenesis periplasm glycosylation sites Aspergillus niger quercetin rutin rutinose rutinosidase “solid-state biocatalysis” hyaluronic acid in vitro synthesis one-pot multi-enzyme optimization enzyme cascade Basidiomycota Agaricomycotina nitrilase cyanide hydratase nitrile substrate specificity overproduction homology modeling substrate docking phylogenetic distribution indigo MISO library flavin monooxygenase FMO β-N-acetylhexosaminidases transglycosylation Glide docking Talaromyces flavus muramic acid non-reducing carbohydrate glucose oxidase direct electron transfer amine-reactive phenazine ethosulfate glucose sensor glycemic level monitoring Pseudomonas putida MnB1 biogenic manganese oxides abiotic manganese oxides α-Hydroxy-β-keto esters whole-cell biocatalysis surface display cell wall anchor Lactobacillus plantarum whole-cell biocatalyst n/a Fe(II)/2-ketoglutarate-dependent dioxygenase 2-ketoglutarate generation regio- and stereo-selective synthesis hydroxy amino acids sequential cascade reaction thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TB Technology: general issues |
| topic_facet | E. coli recombinant horseradish peroxidase site-directed mutagenesis periplasm glycosylation sites Aspergillus niger quercetin rutin rutinose rutinosidase “solid-state biocatalysis” hyaluronic acid in vitro synthesis one-pot multi-enzyme optimization enzyme cascade Basidiomycota Agaricomycotina nitrilase cyanide hydratase nitrile substrate specificity overproduction homology modeling substrate docking phylogenetic distribution indigo MISO library flavin monooxygenase FMO β-N-acetylhexosaminidases transglycosylation Glide docking Talaromyces flavus muramic acid non-reducing carbohydrate glucose oxidase direct electron transfer amine-reactive phenazine ethosulfate glucose sensor glycemic level monitoring Pseudomonas putida MnB1 biogenic manganese oxides abiotic manganese oxides α-Hydroxy-β-keto esters whole-cell biocatalysis surface display cell wall anchor Lactobacillus plantarum whole-cell biocatalyst n/a Fe(II)/2-ketoglutarate-dependent dioxygenase 2-ketoglutarate generation regio- and stereo-selective synthesis hydroxy amino acids sequential cascade reaction thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TB Technology: general issues |
| url | ONIX_20210501_9783039432783_925 |