Oxidation of chlorinated olefins by Escherichia coli transformed with dimethyl sulfide monooxygenase genes or cmene dioxygenase genes.

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  • Takami Wako
    New Energy and Industrial Technology Development Organization (NEDO) Asahi Chemical Industry Co., Ltd. Biotechnology Research Center, The University of Tokyo
  • Yoshida Takako
    Biotechnology Research Center, The University of Tokyo
  • Nojiri Hideaki
    Biotechnology Research Center, The University of Tokyo
  • Yamane Hisakazu
    Biotechnology Research Center, The University of Tokyo
  • Omori Toshio
    Biotechnology Research Center, The University of Tokyo

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In the present work, it was shown that the dimethyl sulfide (DMS) monooxygenase and the cumene dioxygenase catalyzed oxidation of various chlorinated ethenes, propenes, and butenes. The specific activities of these oxygenases were determined for C2 to C4 chlorinated olefins, and the oxidation rates ranged from 0.19 to 4.18 nmol·min−1·mg−1 of dry cells by the DMS monooxygenase and from 0.19 to 1.29 nmol·min−1·mg−1 of dry cells by the cumene dioxygenase. The oxidation products were identified by gas chromatography-mass spectrometry. Most chlorinated olefins were monooxygenated by the DMS monooxygenase to yield chlorinated epoxides. In the case of the cumene dioxygenase, the substrates lacking any chlorine atom on double-bond carbon atoms were dioxygenated, and those with chlorine atoms attaching to double-bond carbon atoms were monooxygenated to yield allyl alcohols.

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