Purification and Properties of Coenzyme-independent Aldehyde Dehydrogenase from the Membrane Fraction of Acetobacter aceti

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Coenzyme-independent aldehyde dehydrogenase was solubilized from the membrane fraction of Acetobacter aceti subsp. aceti with NaI. Since the enzyme was not bound to a cytochrome c-like component in this preparation, but formed an aggregate with other membrane-derived fragments, its gel electrophoretic profile was diffuse. When this preparation was purified by differential solubility fractionation, SP-Sephadex chromatography, acetone precipitation and Tween 81 treatment, it was found to contain three different enzymes. One of these enzymes was purified by CM-cellulose column chromatography to an electrophoretically homogeneous state.Properties of the enzyme preparation solubilized with Triton X-100 and apparently complexed with alcohol dehydrogenase were compared with those of the purified enzyme. The two preparations differed in pH optimum, pH stability, sensitivities toward various inhibitors, substrate specificities and K_m value for acetaldehyde.The purified enzyme was most active at pH 8 and relatively stable at pH 4 to 6. It showed a broad substrate specificity, and its molecular weight was estimated to be approximately 125,000 by gradient polyacrylamide gel and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
公益社団法人日本生物工学会の論文
1981-08-25