A genomic search approach to identify carbonyl reductases in Gluconobacter oxydans for enantioselective reduction of ketones. Issue 8 (3rd August 2014)

• Record Type: Journal Article
• Authors: Chen, Rong; Liu, Xu; Lin, Jinping; Wei, Dongzhi
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 78:Issue 8(2014)
• Page Start: 1350
• Page End: 1356
• Publication Date: 2014-08-03
• Subjects: carbonyl reductase -- enantioselective reduction -- chiral alcohols; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2014.925775
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: The versatile carbonyl reductases from Gluconobacter oxydans in the enantioselective reduction of ketones to the corresponding alcohols were exploited by genome search approach. All purified enzymes showed activities toward the tested ketoesters with different activities. In the reduction of 4-phenyl-2-butanone with in situ NAD(P)H regeneration system, (S)-alcohol was obtained with an e.e. of up to 100% catalyzed by Gox0644. Under the same experimental condition, all enzymes catalyzed ethyl 4-chloroacetoacetate to give chiral products with an excellent e.e. of up to 99%, except Gox0644. Gox2036 had a strict requirement for NADH as the cofactor and showed excellent enantiospecificity in the synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate. For the reduction of ethyl 2-oxo-4-phenylbutyrate, excellent e.e. (>99%) and high conversion (93.1%) were obtained by Gox0525, whereas the other enzymes showed relatively lower e.e. and conversions. Among them, Gox2036 and Gox0525 showed potentials in the synthesis of chiral alcohols as useful biocatalysts. Graphical abstract: : The carbonyl reductases from Gluconobacter oxydans exploited by genome search approach were investigated the enantioselective reduction of three ketones