Reprint
Novel Enzyme and Whole-Cell Biocatalysts
Edited by
November 2020
332 pages
- ISBN978-3-03943-464-0 (Hardback)
- ISBN978-3-03943-465-7 (PDF)
This book is a reprint of the Special Issue Novel Enzyme and Whole-Cell Biocatalysts that was published in
Chemistry & Materials Science
Engineering
Summary
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.
Format
- Hardback
License
© 2020 by the authors; CC BY-NC-ND license
Keywords
2G ethanol; hemicellulose usage; S. cerevisiae; enzyme immobilization; cell immobilization; SHIF; mannonate dehydratase; mannose metabolism; 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; 5-hydroxymethylfuroic acid; platform chemicals; whole cells; New Delhi metallo-β-lactamase; NDM-24; kinetic profile; secondary structure; glycoside hydrolase; thioglycosides; biocatalysis; Fervidobacterium; endo-β-1,3-glucanase; laminarinase; glycoside hydrolase; thermostable; gene duplication; cofactor F420; deazaflavin; oxidoreductase; hydride transfer; hydrogenation; asymmetric synthesis; cofactor biosynthesis; ω-transaminase; α-methylbenzylamine; biocatalysis; 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; biocatalysis; ene reductase; enzyme sourcing; old yellow enzyme; solvent stability; machine learning; flux optimization; artificial neural network; synthetic biology; glycolysis; metabolic pathways optimization; cell-free systems; hydrolase; lipase; esterase; Bacillus subtilis lipase A; transesterification; organic solvent; water activity; biodiesel; transesterification; immobilized lipase; RSM; fuel properties; chemo-enzymatic synthesis; glycosyl transferases; protein engineering; carbohydrates; biocatalysis; synthetic biology; industrial enzymes; thermostable enzymes; glycoside hydrolases; cell-free biocatalysis; natural and non-natural multi-enzyme pathways; bio-based chemicals