Association of Coenzyme-Independent Alcohol and Aldehyde Dehydrogenases from the Membrane Fraction of Acetobacter aceti and their Localization

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In order to confirm that alcohol dehydrogenase and aldehyde dehydrogenase in the crude enzyme solubilized with Triton X-100 from the membrane fraction of Acetobacter aceti constitute an enzyme complex, an isotope dilution experiment was carried out. No significant decrease in specific activities of ^<14>C-acetic acid which was produced from ^<14>C-ehtanol by the crude enzyme with ferricyanide as electron acceptor was demonstrated even in the presence of unlabeled acetaldehyde in an amount 8 times as much as that of ^<14>C-ethanol. The same experiment was performed using a mixture of almost homogeneously purified alcohol dehydrogenase and partially purified aldehyde dehydrogenase instead of the crude enzyme. When unlabeled acetaldehyde was added to the reaction mixture at a concentration of eight times as much, the specific radio-activity decreased to half of that of the control without unlabeled acetaldehyde. Cells subjected to osmotic shock released small amounts of both dehydrogenases into the shock fluid.
公益社団法人日本生物工学会の論文
1982-04-25