Purification and Characterization of Two Epoxide Hydrolases from Corynebacterium sp. Strain N-1074

Author:

Nakamura Tetsuji1,Nagasawa Toru2,Yu Fujio1,Watanabe Ichiro1,Yamada Hideaki3

Affiliation:

1. Central Research Laboratory, Nitto Chemical Industry Company Ltd., Tsurumi-ku, Yokohama 230, Japan

2. Department of Applied Biological Sciences, Nagoya University, Chikusa-ku, Nagoya 464, Japan

3. Department of Agricultural Chemistry, Kyoto University, Sakyo-ku, Kyoto 606, Japan

Abstract

Enzymes II a and II b , which catalyze the conversion of epichlorohydrin (ECH) to 3-chloro-1,2-propanediol (MCP), were purified from Corynebacterium sp. strain N-1074, which catalyzes the formation of ( R )-MCP from prochiral 1,3-dichloro-2-propanol via ECH. The specific activity of enzyme II a for the formation of MCP from ECH was about 6.4-fold higher than that of enzyme II b . Both enzymes catalyzed the conversion of 1,2-epoxides to the corresponding diol, although they differed in several enzymatic properties.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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