- P-ISSN 1225-0163
- E-ISSN 2288-8985
An alcohol oxidase from Hansenula polymorpha was strongly induced when cells were grown with 0.5% methanol supplementation as the carbon source. The induced Hansenula polymorpha alcohol oxidase was purified to electrophoretic homogeneity by using DEAE-Sephacel and Mono Q column chromatographys. The enzyme oxidized mainly primary aliphatic alcohols and exhibited high substrate specificity towards ethanol and methanol. The activity of the enzyme optimally proceeded at pH 8.5 and 50 ℃. The midpoint of the temperature-stability curve for the enzyme was approximately 52 ℃ and the enzyme was not completely inactivated even at 65 ℃ temperature. The enzyme showed resistance toward detergents and highly stable over 7 weeks of storage condition. This Hansenula polymorpha alcohol oxidase may be useful for the enzymatic determination of alcohol and for the industrial production of alcohols and aldehydes.
(1987) Proceedings of the 5th International Symposium on Microbial Growth on C1 Compounds,