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Purification and characterization of halohydrin hydrogen-halide lyase from a recombinant Escherichia coli containing the gene from a Corynebacterium sp.

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Summary

An enzyme catalyzing the interconversion of 1,3-dichloro-2-propanol (DCP) to epichlorohydrin (ECH) was purified from Escherichia coli JM109/ pST001, which carried the gene from Corynebacterium sp. N-1074. The enzyme was crystallized by the addition of ammonium sulphate. The enzyme had a relative molecular mass (Mr) of about 105 000 and consisted of four subunits identical in Mr (approx. 28 000). The enzyme catalysed both the transformation of various halohydrins into the corresponding epoxides with liberation of halide and its reverse reaction. These facts indicated that the enzyme was halohydrin hydrogen-halidelyase.

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Authors and Affiliations

  1. Department of Agricultural Chemistry, Kyoto University, Kitsashirakawa, Oiwake-cho, 606, Sakyo-ku, Kyoto, Japan

    Toru Nagasawa & Hideaki Yamada

  2. Central Research Laboratory, Nitto Chemical Industry Co., Ltd., 10-1 Daikoku-cho, 230, Tsurumi-ku, Yokohama, Japan

    Tetsuji Nakamura, Fujio Yu & Ichiro Watanabe

Authors
  1. Toru Nagasawa
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  2. Tetsuji Nakamura
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  3. Fujio Yu
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  4. Ichiro Watanabe
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  5. Hideaki Yamada
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Nagasawa, T., Nakamura, T., Yu, F. et al. Purification and characterization of halohydrin hydrogen-halide lyase from a recombinant Escherichia coli containing the gene from a Corynebacterium sp.. Appl Microbiol Biotechnol 36, 478–482 (1992). https://doi.org/10.1007/BF00170187

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  • DOI: https://doi.org/10.1007/BF00170187

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