Bioscience, Biotechnology, and Biochemistry 2012-01-01

A novel reductase from Candida albicans for the production of ethyl (S)-4-chloro-3-hydroxybutanoate.

Mingdong An, Ping Cai, Ming Yan, Ning Hao, Shanshan Wang, Huan Liu, Yan Li, Lin Xu

Index: Biosci. Biotechnol. Biochem. 76(6) , 1210-2, (2012)

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Abstract

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.