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

Abstract

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.