Novel Enzyme and Whole-Cell Biocatalysts
The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for "green" synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and...
| Format: | eBook |
|---|---|
| Language: | English |
| Published: |
Basel, Switzerland
MDPI - Multidisciplinary Digital Publishing Institute
2020
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| Subjects: | |
| Online Access: | Open Access: DOAB: description of the publication Open Access: DOAB, download the publication |
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| 720 | 1 | |a Sunna, Anwar |4 edt | |
| 720 | 1 | |a Daniellou, Richard |4 edt | |
| 720 | 1 | |a Daniellou, Richard |4 oth | |
| 720 | 1 | |a Sunna, Anwar |4 oth | |
| 245 | 0 | 0 | |a Novel Enzyme and Whole-Cell Biocatalysts |
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| 300 | |a 1 online resource (332 p.) | ||
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| 520 | |a The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for "green" synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications. | ||
| 540 | |a Creative Commons |f https://creativecommons.org/licenses/by/4.0/ |2 cc |u https://creativecommons.org/licenses/by/4.0/ | ||
| 546 | |a English | ||
| 650 | 7 | |a Technology: general issues |2 bicssc | |
| 653 | |a 2-keto-3-deoxygluconate | ||
| 653 | |a 2G ethanol | ||
| 653 | |a 5-hydroxymethylfurfural | ||
| 653 | |a 5-hydroxymethylfuroic acid | ||
| 653 | |a aldohexose dehydrogenase | ||
| 653 | |a Antarctica and homology modelling | ||
| 653 | |a archaea | ||
| 653 | |a artificial neural network | ||
| 653 | |a asymmetric synthesis | ||
| 653 | |a Bacillus subtilis lipase A | ||
| 653 | |a bio-based chemicals | ||
| 653 | |a bioactive peptides | ||
| 653 | |a biocatalysis | ||
| 653 | |a biodiesel | ||
| 653 | |a biotransformation | ||
| 653 | |a carbohydrate active enzymes | ||
| 653 | |a carbohydrates | ||
| 653 | |a cell immobilization | ||
| 653 | |a cell surface display | ||
| 653 | |a cell-free biocatalysis | ||
| 653 | |a cell-free systems | ||
| 653 | |a chemo-enzymatic synthesis | ||
| 653 | |a chiral amine | ||
| 653 | |a cofactor biosynthesis | ||
| 653 | |a cofactor F420 | ||
| 653 | |a cyclodextrin glucanotransferases | ||
| 653 | |a deazaflavin | ||
| 653 | |a DNase | ||
| 653 | |a endo-β-1,3-glucanase | ||
| 653 | |a ene reductase | ||
| 653 | |a engineered Escherichia coli | ||
| 653 | |a enzyme immobilization | ||
| 653 | |a enzyme sourcing | ||
| 653 | |a esterase | ||
| 653 | |a extremophile | ||
| 653 | |a Fervidobacterium | ||
| 653 | |a flavonoid glucuronides | ||
| 653 | |a flux optimization | ||
| 653 | |a fuel properties | ||
| 653 | |a functionalized magnetic nanoparticles | ||
| 653 | |a gene duplication | ||
| 653 | |a Glaciozyma antarctica | ||
| 653 | |a glycolysis | ||
| 653 | |a glycosidase | ||
| 653 | |a glycoside hydrolase | ||
| 653 | |a glycoside hydrolases | ||
| 653 | |a glycosyl transferases | ||
| 653 | |a hemicellulose usage | ||
| 653 | |a hormone-sensitive lipase | ||
| 653 | |a hydride transfer | ||
| 653 | |a hydrogenation | ||
| 653 | |a hydrolase | ||
| 653 | |a immobilization | ||
| 653 | |a immobilized lipase | ||
| 653 | |a industrial enzymes | ||
| 653 | |a interfacial activation | ||
| 653 | |a keratin hydrolysis | ||
| 653 | |a keratin waste | ||
| 653 | |a keratinase | ||
| 653 | |a kinetic profile | ||
| 653 | |a kinetic profiles | ||
| 653 | |a Lactobacillus | ||
| 653 | |a laminarinase | ||
| 653 | |a large-ring cyclodextrins | ||
| 653 | |a lipase | ||
| 653 | |a lipase immobilization | ||
| 653 | |a LysM domains | ||
| 653 | |a machine learning | ||
| 653 | |a mannonate dehydratase | ||
| 653 | |a mannono-1,4-lactone | ||
| 653 | |a mannose metabolism | ||
| 653 | |a metabolic pathways optimization | ||
| 653 | |a metalloprotease | ||
| 653 | |a multienzyme whole-cell biocatalyst | ||
| 653 | |a natural and non-natural multi-enzyme pathways | ||
| 653 | |a NDM-24 | ||
| 653 | |a New Delhi metallo-β-lactamase | ||
| 653 | |a old yellow enzyme | ||
| 653 | |a organic solvent | ||
| 653 | |a organic solvents | ||
| 653 | |a oxidoreductase | ||
| 653 | |a peptidase | ||
| 653 | |a platform chemicals | ||
| 653 | |a protein engineering | ||
| 653 | |a psychrophilic yeast | ||
| 653 | |a RNase | ||
| 653 | |a RSM | ||
| 653 | |a S. cerevisiae | ||
| 653 | |a Saccharolobus solfataricus | ||
| 653 | |a secondary structure | ||
| 653 | |a semi rational mutagenesis | ||
| 653 | |a semi-rational mutagenesis | ||
| 653 | |a serine protease | ||
| 653 | |a SHIF | ||
| 653 | |a solvent stability | ||
| 653 | |a substrate specificity | ||
| 653 | |a Sulfolobus solfataricus | ||
| 653 | |a synthetic biology | ||
| 653 | |a Thermoplasma acidophilum | ||
| 653 | |a thermostable | ||
| 653 | |a thermostable enzymes | ||
| 653 | |a thioglycosides | ||
| 653 | |a transesterification | ||
| 653 | |a valorisation | ||
| 653 | |a waste cooking oil | ||
| 653 | |a water activity | ||
| 653 | |a whole cells | ||
| 653 | |a α-methylbenzylamine | ||
| 653 | |a β-galactosidase | ||
| 653 | |a ω-transaminase | ||
| 793 | 0 | |a DOAB Library. | |
| 856 | 4 | 0 | |u https://directory.doabooks.org/handle/20.500.12854/69259 |7 0 |z Open Access: DOAB: description of the publication |
| 856 | 4 | 0 | |u https://mdpi.com/books/pdfview/book/3047 |7 0 |z Open Access: DOAB, download the publication |