Particulate alcohol dehydrogenase of acetic acid bacteria was purified to homogeneous state from Acetobacter aceti IFO 3284. The enzyme was purified about 70-fold with an overall yield of 55% from the cell homogenate by solubilization and extraction of the enzyme with Triton X-100 and subsequent fractionations on column chromatography. The purified enzyme was revealed of its properties as flavo-cytochrome complex and was composed of four different subunits having a molecular weight of 63, 000, 44, 000, 29, 000 and 13, 500. A tightly bound cytochrome component was not alcohol dehydrogenase itself and had a function as an electron acceptor in vivo. The first subunit which reacts with ethanol was shown to be a flavoprotein of the particulate alcohol dehydrogenase complex. Catalytic properties of the enzyme were also examined and the data that the enzyme is a representative as the vinegar fermenter were ob-tained.
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Adachi et al. (1978) studied this question.