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Alcohol oxidase, a flavoprotein from several basidiomycetes species

1968; Elsevier BV; Volume: 151; Issue: 2 Linguagem: Inglês

10.1016/0005-2744(68)90100-9

1878-1454

Frank W. Janssen, Hans W. Ruelius,

Enzyme-mediated dye degradation

1. A novel enzyme designated ‘alcohol oxidase’, has been isolated from the mycelium of a Basidiomycete belonging to the family Polyporaceae. In the presence of O2, this enzyme catalyzes the oxidation of the lower primary alcohols to the corresponding aldehydes and H2O2. Unsaturated alcohols are also good substrates, but branched-chain and secondary alcohols are not attacked. Halogenated ethanols are oxidized, but other substituted ethanols are not. 2. The enzyme was purified to the crystalline state by fractional precipitation with polyethylene glycol. 3. Flavin-adenine dinucleotide was identified as the prosthetic group. 4. The pH optimum is 6.5–9. Below pH 6.5, the enzyme is rapidly inactivated. 5. Gel filtration on Sephadex G-200 suggested that the molecular weight of the enzyme is greater than 300 000. 6. The enzyme may be useful for the colorimetric determination of methanol, ethanol, or other lower alchols.