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

Bioscience, biotechnology, and biochemistry (2012-07-14)
Mingdong An, Ping Cai, Ming Yan, Ning Hao, Shanshan Wang, Huan Liu, Yan Li, Lin Xu
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Butyl acetate, anhydrous, ≥99%
Sigma-Aldrich
Butyl acetate, ACS reagent, ≥99.5%
Sigma-Aldrich
Ethyl 4-chloroacetoacetate, 95%
Sigma-Aldrich
Butyl acetate, suitable for HPLC, 99.7%
Supelco
Butyl acetate, analytical standard
Sigma-Aldrich
Butyl acetate, natural, ≥98%, FG
Sigma-Aldrich
Butyl acetate, ≥99%, FCC, FG
Sigma-Aldrich
Butyl acetate, ReagentPlus®, 99.5%
Supelco
Butyl acetate, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
Butyl acetate, puriss. p.a., ACS reagent
Sigma-Aldrich
Ethyl 4-chloroacetoacetate, Lonza quality, ≥97.0% (GC)