Mass production of thermostable D-hydantoinase by batch culture of recombinant Escherichia coli with a constitutive expression system

• Published in: Biotechnology and bioengineering Vol. 56; no. 4; pp. 449 - 455
• Main Authors: Lee, Dong-Cheol, Kim, Geun-Joong, Cha, Yoo-Kyong, Lee, Cheo-Young, Kim, Hak-Sung
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 20.11.1997; Wiley
• Subjects: Batch cell culture; batch cultivation; Biological and medical sciences; Biomass; Biotechnology; Catalyst activity; Coliform bacteria; constitutive expression; Enzyme engineering; Enzyme kinetics; Fermentation; Fundamental and applied biological sciences. Psychology; Genetic engineering; Glycerol; Methods. Procedures. Technologies; Production of selected enzymes; recombinant E. coli; Thermal effects; Thermodynamic stability; thermostable D-hydantoinase; Recombinant microorganism; Mass production; Stability; Enzyme; Escherichia coli; Dihydropyrimidinase; Environmental factor; Bacillaceae; Gene expression; Optimization; Operating conditions; Plasmid; Bacillales; Batchwise; Bacillus stearothermophilus; Microorganism culture; Bacteria; Hydrolases; Enterobacteriaceae
• ISSN: 0006-3592; 1097-0290
• DOI: 10.1002/(SICI)1097-0290(19971120)56:4<449::AID-BIT10>3.0.CO;2-7

D‐Hydantoinase is an industrial enzyme widely used for the synthesis of optically active D‐amino acids. A gene encoding thermostable D‐hydantoinase of Bacillus stearothermophilus SD‐1 has previously been cloned and constitutively expressed by its native promoter in Escherichia coli XL1‐Blue (Lee et...