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Analysis on the Substrate Specificity and Stability of Hansenula polymorpha Alcohol Oxidase  

Jegal, Hyang (Department of Chemistry, Chung-Ang University)
Cho, Hyun-Young (Department of Chemistry, Chung-Ang University)
Kim, Eun-Ho (Department of Chemistry, Chung-Ang University)
Kong, Kwang-Hoon (Department of Chemistry, Chung-Ang University)
Publication Information
Analytical Science and Technology / v.17, no.1, 2004 , pp. 37-44 More about this Journal
Abstract
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 $50^{\circ}C$. The midpoint of the temperature-stability curve for the enzyme was approximately $52^{\circ}C$ and the enzyme was not completely inactivated even at $65^{\circ}C$ 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.
Keywords
alcohol oxidase; Hansenula polymorpha; inducible expression; substrate specificity; stability;
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