Production of chiral alcohols by enantioselective reduction with NADH-dependent phenylacetaldehyde reductase from Corynebacterium strain, ST-10

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 6; no. 1; pp. 41 - 50
• Main Authors: Itoh, Nobuya, Mizuguchi, Naoyuki, Mabuchi, Mariko
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 04.01.1999; Elsevier Science
• Subjects: ( S)-1-Phenylethanol; ( S)-2-Alkanol; Aromatic hydrocarbons; Bacteria; Bioconversions. Hemisynthesis; Biological and medical sciences; Biosynthesis; Biotechnology; Chiral alcohol; Corynebacterium sp; Enzymatic reduction; Enzymes; Fundamental and applied biological sciences. Psychology; Ketones; Methods. Procedures. Technologies; Phenylacetaldehyde reductase (NADH); Reduction; Stereochemistry; Enzymatic reduction; Chiral alcohol; ( S)-1-Phenylethanol; Phenylacetaldehyde reductase (NADH); ( S)-2-Alkanol; Corynebacterium sp; Enantioselectivity; Enzyme; Chiral compound; Ketone; Reduction; Corynebacterium; Biotransformation; Bacteria; Actinomycetes; Corynebacteriaceae; Oxidoreductases; Secondary alcohol; Enzymatic reaction
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/S1381-1177(98)00118-0

Phenylacetaldehyde reductase (PAR) (systematic name, 2-phenylethanol: NAD + oxidoreductase) isolated from styrene-assimilating Corynebacterium strain ST-10 was used to produce chiral alcohols. This enzyme with a broad substrate range reduced various prochiral 2-alkanones and aromatic ketones to yield optically active secondary alcohols with an enantiomeric purity of 87–100% enantiomeric excess (e.e.). The stereochemistry of PAR revealed that the pro-R hydrogen of NADH was transferred to carbonyl moiety of acetophenone derivatives or alkanones through its re face. The combination with a NADH-regenerating system using formate dehydrogenase and formate was able to practically produce optically pure alcohols.