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Applied Microbiology and Biotechnology

, Volume 36, Issue 4, pp 478–482 | Cite as

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

  • Toru Nagasawa
  • Tetsuji Nakamura
  • Fujio Yu
  • Ichiro Watanabe
  • Hideaki Yamada
Applied Genetics and Regulation

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.

Keywords

Enzyme Sulphate Ammonium Escherichia Coli Purification 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • Toru Nagasawa
    • 1
  • Tetsuji Nakamura
    • 2
  • Fujio Yu
    • 2
  • Ichiro Watanabe
    • 2
  • Hideaki Yamada
    • 1
  1. 1.Department of Agricultural ChemistryKyoto UniversitySakyo-ku, KyotoJapan
  2. 2.Central Research LaboratoryNitto Chemical Industry Co., Ltd.Tsurumi-ku, YokohamaJapan

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