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Enzyme identification and development of a whole-cell biotransformation for asymmetric reduction of o-chloroacetophenone.
- Source :
- Biotechnology & Bioengineering; Apr2011, Vol. 108 Issue 4, p797-803, 7p
- Publication Year :
- 2011
-
Abstract
- The article discusses a study on possible enzymes that transform o-chloroacetophenone to chiral 1-(o-chlorophenyl)-ethanols, a key intermediate in the synthesis of anti-tumor drugs. A few catalysts have been tested for the production of the chiral alcohol product but none were successful. Using development studies of xylose reductase from the yeast Candida tenuis, whole cell catalysts from Escherichia coli and Saccharomyces cerevisiae were developed and tested. Results showed that E.coli enzymes converted six times more than S. cerevisiae enzymes.
- Subjects :
- ENZYMES
ETHANOL
CANDIDA
CATALYSTS
ESCHERICHIA coli
CARBONYL reductase
Subjects
Details
- Language :
- English
- ISSN :
- 00063592
- Volume :
- 108
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Biotechnology & Bioengineering
- Publication Type :
- Academic Journal
- Accession number :
- 59303689
- Full Text :
- https://doi.org/10.1002/bit.23002