Purification and characterization of a yeast carbonyl reductase for synthesis of optically active (R)-styrene oxide derivatives.

Noriyuki Kizaki, Ikuo Sawa, Miho Yano, Yoshihiko Yasohara, Junzo Hasegawa

Index: Biosci. Biotechnol. Biochem. 69(1) , 79-86, (2005)

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Abstract

Optically active styrene oxide derivatives are versatile chiral building blocks. Stereoselective reduction of phenacyl halide to chiral 2-halo-1-phenylethanol is the key reaction of the most economical synthetic route. Rhodotorula glutinis var. dairenensis IFO415 was discovered on screening as a potent microorganism reducing a phenacyl halide to the (R)-form of the corresponding alcohol. An NADPH-dependent carbonyl reductase was purified to homogeneity through four steps from this strain. The relative molecular mass of the enzyme was estimated to be 40,000 on gel filtration and 30,000 on SDS-polyacrylamide gel electrophoresis. This enzyme reduced a broad range of carbonyl compounds in addition to phenacyl halides. Some properties of the enzyme and preparation of a chiral styrene oxide using the crude enzyme are reported herein.