期刊
BIORESOURCE TECHNOLOGY
卷 102, 期 14, 页码 7023-7028出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2011.04.046
关键词
Carbonyl reductase; Streptomyces coelicolor; Asymmetric reduction; Ethyl (S)-4-chloro-3-hydroxybutanoate; NADH regeneration
资金
- National Natural Science Foundation of China [20902023, 31071604]
- Ministry of Science and Technology, P.R. China [2009CB724706, 2009BADB1B0301-03, 2009ZX09501-016, 2010CB710800]
- China National Special Fund for State Key Laboratory of Bioreactor Engineering [2060204]
An NADH-dependent reductase (ScCR) from Streptomyces coelicolor was discovered by genome mining for carbonyl reductases. ScCR was overexpressed in Escherichia coli BL21, purified to homogeneity and its catalytic properties were studied. This enzyme catalyzed the asymmetric reduction of a broad range of prochiral ketones including aryl ketones, alpha- and beta-ketoesters, with high activity and excellent enantioselectivity (>99% ee) towards beta-ketoesters. Among them, ethyl 4-chloro-3-oxobutanoate (CUBE) was efficiently converted to ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE), an important pharmaceutical intermediate, in water/toluene biphasic system. As much as 600 g/L (3.6 M) of CUBE was asymmetrically reduced within 22 h using 2-propanol as a co-substrate for NADH regeneration, resulting in a yield of 93%, an enantioselectivity of >99% ee, and a total turnover number (UN) of 12,100. These results indicate the potential of ScCR for the industrial production of valuable chiral alcohols. (C) 2011 Elsevier Ltd. All rights reserved.
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