Reprint
Biocatalytic Process Optimization
Edited by
January 2021
296 pages
- ISBN978-3-03943-915-7 (Hardback)
- ISBN978-3-03943-916-4 (PDF)
This is a Reprint of the Special Issue Biocatalytic Process Optimization that was published in
Chemistry & Materials Science
Engineering
Summary
Biocatalysis is very appealing to the industry because it allows, in principle, the synthesis of products not accessible by chemical synthesis. Enzymes are very effective, as are precise biocatalysts, as they are enantioselective, with mild reaction conditions and green chemistry. Biocatalysis is currently widely used in the pharmaceutical industry, food industry, cosmetic industry, and textile industry. This includes enzyme production, biocatalytic process development, biotransformation, enzyme engineering, immobilization, the synthesis of fine chemicals and the recycling of biocatalysts. One of the most challenging problems in biocatalysis applications is process optimization. This Special Issue shows that an optimized biocatalysis process can provide an environmentally friendly, clean, highly efficient, low cost, and renewable process for the synthesis and production of valuable products. With further development and improvements, more biocatalysis processes may be applied in the future.
Format
- Hardback
License and Copyright
© 2022 by the authors; CC BY-NC-ND license
Keywords
catechin; degalloylation; flavonol; glycoside hydrolase; optimization; tannase; immobilized DERA; statin side chain; continuous flow synthesis; alginate-luffa matrix; design of experiments; optimization; Anguilla marmorata; eel protein hydrolysates; functional properties; herbal eel extracts; agarose; agarase; agarotriose; agaropentaose; expression; calycosin; calycosin-7-O-β-D-glucoside; glucosyltransferase; sucrose synthase; UDP-glucose recycle; UGT–SuSy cascade reaction; Candida antarctica lipase A; surface-display system; shear rate; mass transfer rate; enzymatic kinetic study; enzymatic synthesis; β-amino acid esters; microreactor; aromatic amines; Michael addition; kraft pulp; cellulose; xylan; enzymatic hydrolysis; Penicillium verruculosum; glucose; xylose; lipase; acidolysis; docosahexaenoic acid ethyl ester; eicosapentaenoic acid ethyl ester; ethyl acetate; kinetics; styrene monooxygenase; indole monooxygenase; two-component system; chiral biocatalyst; solvent tolerance; biotransformation; epoxidation; NAD(P)H-mimics; superoxide dismutase (SOD); catalase (CAT); glutathione reductase (GR); aluminum (Al); selenium (Se); mouse; brain; liver; phosphatidylcholine; 3,4-dimethoxycinnamic acid; enzymatic interesterification; lipase; biocatalysis; Pleurotus ostreatus; enenzymatic hydrolysis; peptide; antioxidant; hepatoprotective activity; Yarrowia lipolytica; whole–cell biocatalysis; indolizine; cycloaddition; trehalose; viscosity; enzymes; protein dynamics; Kramers’ theory; protein stabilization; enzyme inhibition; Lipase; transesterification; 2-phenylethyl acetate; packed-bed reactor; solvent-free; ethyl acetate; cyclic voltammetry; electrochemical impedance spectroscopy; carbon nanotubes; redox mediators; CYP102A1; naringin dihydrochalcone; neoeriocitrin dihydrochalcone; regioselective hydroxylation; n/a