Membrane-bound Quinoprotein D-Arabitol Dehydrogenase of Gluconobacter suboxydans IFO 3257 : A Versatile Enzyme for the Oxidative Fermentation of Various Ketoses(Microbiology & Fermentation Technology)

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概要

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• Solubilization of membrane-bound quinoprotein D-arabitol dehydrogenase (ARDH) was done successfully with the membrane fraction of Gluconobacter suboxydans IFO 3257. In enzyme solubilization and subsequent enzyme purification steps, special care was taken to purifiy ARDH as active as it was in the native membrane, after many disappointing trials. Selection of the best detergent, keeping ARDH as the holoenzyme by the addition of PQQ and Ca^<2+>, and of a buffer system involving acetate buffer supplemented with Ca^<2+>, were essential to treat the highly hydrophobic and thus labile enzyme. Purification of the enzyme was done by two steps of column chromatography on DEAE-Toyopearl and CM-Toyopearl in the presence of detergent and Ca^<2+>. ARDH was homogenous and showed a single sedimentation peak in analytical ultracentrifugation. ARDH was dissociated into two different subunits upon SDS-PAGE with molecular masses of 82 kDa (subunit I) and 14 kDa (subunit II), forming a heterodimeric structure. ARDH was proven to be a quinoprotein by detecting a liberated PQQ from SDS-treated ARDH in HPLC chromatography. More preliminarily, an EDTA-treated membrane fraction lost the enzyme activity and ARDH activity was restored to the original level by the addition of PQQ and Ca^<2+>. The most predominant unique character of ARDH, the substrate specificity, was highly versatile and many kinds of substrates were oxidized irreversibly by ARDH, not only pentitols but also other polyhydroxy alcohols including D-sorbitol, D-mannitol, glycerol, meso-erythritol, and 2, 3-butanediol. ARDH may have its primary function in the oxidative fermentation of ketose production by acetic acid bacteria. ARDH contained no heme component, unlike the type II or type III quinoprotein alcohol dehydrogenase (ADH) and did not react with primary alcohols.

• 2001-12-23

著者

• 品川 恵美子

  宇部高専物質工学科

• FUJII Yoshikazu

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• Toyama Hirohide

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Adachi Osao

  Derartment Of Blological Chemistry Faculty Of Agriculture Yamaguchi University

• Adachi Osao

  Department Of Agricultural Chemistry Yamaguchi University

• Fujii Y

  Ritsumeikan Univ. Shiga Jpn

• Shinagawa Emiko

  Department Of Chemical And Biological Engineering Ube National College Of Technology

• Fujii Yoshikazu

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Matsushita Kazunobu

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Matsushita K

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• GHALY Mohamed

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• Ghaly Mohamed

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University:(present Address)depa

• Shinagawa Emiko

  Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

• Matsushita Kazunobu

  Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

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