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Alcohol dehydrogenase of Rhizopus javanicus was purified, and its physical and chemical characteristics were determined. The intact enzyme was shown to have a molecular weight of approximately 60,000. Since the smallest apparent subunit was 14,000, the enzyme was presumed to be composed of four subunits. The crude mycelial extract contained multiple forms of the enzyme, which were separated by ion-exchange chromatography. Published data on alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) indicate that its molecular weight, subunit composition, and substrate specificity are different depending on the organism that produces the enzyme. In this paper, we report on the purification and characterization of alcohol dehydrogenase produced by the fungus Rhizopusjavanicus. MATERIALS AND METHODS Organism and growth conditions. R. javanicus

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