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