Analysis on the Substrate Speciticity and Stability of Hansenula Polymorpha Alcohol Oxidase

공광훈; 조현영; 김은호; 제갈향

오늘 하루 그만보기

P-ISSN1225-0163
E-ISSN2288-8985
SCOPUS, ESCI, KCI

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P-ISSN 1225-0163
E-ISSN 2288-8985

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Vol.17, No.1

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Analysis on the Substrate Speciticity and Stability of Hansenula Polymorpha Alcohol Oxidase

Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985

2004, v.17 no.1, pp.37-44

& (2004). Analysis on the Substrate Speciticity and Stability of Hansenula Polymorpha Alcohol Oxidase. , 17(1), 37-44.

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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 ℃. 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.