Cloning and overexpression of thermostable D-hydantoinase from thermophile in E. coli and its application to the synthesis of optically active D-amino acids

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Title
Cloning and overexpression of thermostable D-hydantoinase from thermophile in E. coli and its application to the synthesis of optically active D-amino acids
Author(s)
Dong Chul LeeSeung Goo Lee; Seung Pyo Hong; Moon Hee Sung; Hak Sung Kim
Bibliographic Citation
Annals of New York Academy of Sciences, vol. 799, pp. 401-405
Publication Year
1996
Abstract
We cloned the thermostable D-hydantoinase gene from B. stearothermophilus SD-1 into E. coli. The cloned gene was constitutively expressed by its own promoter, and the enzyme was produced in its soluble form. The specific activity of the recombinant E. coli was 30 times higher than that of B. stearathermophilus SD-1. The cultivation conditions were investigated for the overproduction of the enzyme, and the temperature was found to affect the plasmid content and the expression level of the enzyme. Recombinant E. coli was cultivated in 30-L batch fermentation, the cell concentration reached 25 g-DCW/L, and the specific activity was about 20,000 units/g-DCW. D-Hydantoinase produced from the recombinant E. coli could be successfully applied to the synthesis of N-carbarnoyl-D-amino acid from the 5-monosubstituted hydantoin derivative.
ISSN
0077-8923
Publisher
Wiley
DOI
http://dx.doi.org/10.1111/j.1749-6632.1996.tb33232.x
Type
Article
Appears in Collections:
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
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