Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 76, Issue 6, Pages 1210-1212Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.120048
Keywords
biocatalysis; reductase; ethyl 4-chloro-3-hydroxybutanoate; ethyl 4-chloro-3-oxobutanoate; candida albican
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Funding
- National Basic Research Program of China [2009CB724700]
- Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)
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A novel NADPH-dependent reductase (CaCR) from Candida albicans was cloned for the first time. It catalyzed asymmetric reduction to produce ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE). It contained an open reading frame of 843 bp encoding 281 amino acids. When co-expressed with a glucose dehydrogenase in Escherichia coli, recombinant CaCR exhibited an activity of 5.7 U/mg with ethyl 4-chloro-3-oxobutanoate (COBE) as substrate. In the biocatalysis of COBE to (S)-CHBE, 1320 mm (S)-CHBE was obtained without extra NADP(+)/NADPH in a water/butyl acetate system, and the optical purity of the (S)-isomer was higher than 99% enantiomeric excess.
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