Autore: |
Sunna Anwar
|
Titolo: |
Novel Enzyme and Whole-Cell Biocatalysts
|
Pubblicazione: |
Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020 |
Descrizione fisica: |
1 electronic resource (332 p.) |
Soggetto topico: |
Technology: general issues |
Soggetto non controllato: |
2G ethanol |
|
hemicellulose usage |
|
S. cerevisiae |
|
enzyme immobilization |
|
cell immobilization |
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SHIF |
|
mannonate dehydratase |
|
mannose metabolism |
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Thermoplasma acidophilum |
|
mannono-1,4-lactone |
|
2-keto-3-deoxygluconate |
|
aldohexose dehydrogenase |
|
cyclodextrin glucanotransferases |
|
large-ring cyclodextrins |
|
semi rational mutagenesis |
|
carbohydrate active enzymes |
|
archaea |
|
glycosidase |
|
Sulfolobus solfataricus |
|
Saccharolobus solfataricus |
|
Lactobacillus |
|
β-galactosidase |
|
immobilization |
|
cell surface display |
|
LysM domains |
|
biocatalysis |
|
extremophile |
|
5-hydroxymethylfurfural |
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5-hydroxymethylfuroic acid |
|
platform chemicals |
|
whole cells |
|
New Delhi metallo-β-lactamase |
|
NDM-24 |
|
kinetic profile |
|
secondary structure |
|
glycoside hydrolase |
|
thioglycosides |
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Fervidobacterium |
|
endo-β-1,3-glucanase |
|
laminarinase |
|
thermostable |
|
gene duplication |
|
cofactor F420 |
|
deazaflavin |
|
oxidoreductase |
|
hydride transfer |
|
hydrogenation |
|
asymmetric synthesis |
|
cofactor biosynthesis |
|
ω-transaminase |
|
α-methylbenzylamine |
|
chiral amine |
|
biotransformation |
|
biodiesel |
|
waste cooking oil |
|
lipase immobilization |
|
interfacial activation |
|
functionalized magnetic nanoparticles |
|
DNase |
|
kinetic profiles |
|
RNase |
|
semi-rational mutagenesis |
|
substrate specificity |
|
engineered Escherichia coli |
|
flavonoid glucuronides |
|
multienzyme whole-cell biocatalyst |
|
organic solvents |
|
psychrophilic yeast |
|
hormone-sensitive lipase |
|
Glaciozyma antarctica |
|
Antarctica and homology modelling |
|
keratinase |
|
serine protease |
|
metalloprotease |
|
peptidase |
|
keratin hydrolysis |
|
keratin waste |
|
valorisation |
|
bioactive peptides |
|
ene reductase |
|
enzyme sourcing |
|
old yellow enzyme |
|
solvent stability |
|
machine learning |
|
flux optimization |
|
artificial neural network |
|
synthetic biology |
|
glycolysis |
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metabolic pathways optimization |
|
cell-free systems |
|
hydrolase |
|
lipase |
|
esterase |
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Bacillus subtilis lipase A |
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transesterification |
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organic solvent |
|
water activity |
|
immobilized lipase |
|
RSM |
|
fuel properties |
|
chemo-enzymatic synthesis |
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glycosyl transferases |
|
protein engineering |
|
carbohydrates |
|
industrial enzymes |
|
thermostable enzymes |
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glycoside hydrolases |
|
cell-free biocatalysis |
|
natural and non-natural multi-enzyme pathways |
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bio-based chemicals |
Persona (resp. second.): |
DaniellouRichard |
|
SunnaAnwar |
Sommario/riassunto: |
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. |
Titolo autorizzato: |
Novel Enzyme and Whole-Cell Biocatalysts |
Formato: |
Materiale a stampa |
Livello bibliografico |
Monografia |
Lingua di pubblicazione: |
Inglese |
Record Nr.: | 9910557108903321 |
Lo trovi qui: | Univ. Federico II |
Opac: |
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