A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14

Bioscience, Biotechnology, and Biochemistry
E ShinagawaO Adachi

Abstract

Membrane-bound NADP-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.

References

Jan 1, 1979·Annual Review of Microbiology·J ColbyR Whittenbury
Sep 1, 1980·Archives of Biochemistry and Biophysics·R N PatelA Felix
Jan 1, 1994·Advances in Microbial Physiology·K MatsushitaO Adachi
May 10, 2002·Bioscience, Biotechnology, and Biochemistry·Emiko ShinagawaOsao Adachi
Sep 5, 2002·Archives of Microbiology·Julia A Vorholt
Oct 20, 2005·Journal of Bioscience and Bioengineering·Akinori YasuharaKazuo Aisaka

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Citations

Jan 28, 2014·Environmental Science and Pollution Research International·Diansi YuChanghong Guo
Mar 23, 2010·Applied Microbiology and Biotechnology·Toshiharu Yakushi, Kazunobu Matsushita
Apr 10, 2008·Journal of Bioscience and Bioengineering·Emiko ShinagawaOsao Adachi
Apr 3, 2015·Physiological Reviews·Yuri L DorokhovTatiana V Komarova

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