A Novel Type of Formaldehyde-Oxidizing Enzyme from the Membrane of<i>Acetobacter</i>sp. SKU 14

  • SHINAGAWA Emiko
    Department of Chemical and Biological Engineering, Ube National College of Technology
  • TOYAMA Hirohide
    Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
  • MATSUSHITA Kazunobu
    Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
  • TUITEMWONG Pravate
    Department of Food Science and Technology, Faculty of Science, King Mongkut’s University of Technology Thonburi
  • THEERAGOOL Gunjana
    Department of Microbiology, Faculty of Science, Kasetsart University
  • ADACHI Osao
    Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

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タイトル別名
  • A Novel Type of Formaldehyde-Oxidizing Enzyme from the Membrane of Acetobacter sp. SKU 14
  • Novel Type of Formaldehyde Oxidizing Enzyme from the Membrane of Acetobacter sp SKU 14

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Membrane-bound NAD(P)-independent formaldehyde-oxidizing enzyme was purified to homogeneity from the membrane of Acetobacter sp. SKU 14 isolated in Thailand. The enzyme was solubilized from the membrane fraction of glycerol-grown cells with 1% Tween 20 at pH 2.85, and purified to homogeneity through the steps of column chromatographies on DEAE-Sephadex A-50 and Q-Sepharose in the presence of 0.1% Tween 20 and 0.1% Triton X-100. The enzyme purified together with a cytochrome c showed a single protein band on native-PAGE, and was dissociated into three different subunits upon SDS–PAGE with molecular masses of 78 kDa, 55 kDa, and 18 kDa. The purified enzyme was finally characterized as a quinoprotein alcohol dehydrogenase (QADH), and this is the first indication that QADH highly oxidizes formaldehyde. The substrate specificity of the enzyme was found to be broad toward aldehydes and alcohols, and alcohols, especially n-butanol, n-propanol, and ethanol, were oxidized more rapidly than formaldehyde.

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