PURIFICATION AND SOME PROPERTIES OF ALCOHOL OXIDASE FROM ALKANE-GROWN CANDIDA-TROPICALIS

被引：17
作者：
DICKINSON, FM
WADFORTH, C
机构：
[1] Department of Applied Biology, University of Hull, Hull HU6 7RX, Cottingham Road
来源：
BIOCHEMICAL JOURNAL | 1992年 / 282卷
关键词：
D O I：
10.1042/bj2820325
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Alcohol oxidase was purified to homogeneity from membrane fractions obtained from alkane-grown Candida tropicalis. The enzyme appears to be a dimer of equal-sized subunits of M(r) 70000. The purified enzyme is photosensitive and contains flavin-type material which is released by a combination of boiling and proteolytic digestion. The identity of the flavin material is not yet known, but it is not FMN, FAD or riboflavin. The enzyme is most active with dodecan-1-ol, but other long-chain alcohols are also attacked. The enzyme shows a weak, but significant activity towards long-chain aldehydes. Detailed kinetic studies with decan-1-ol as substrate suggest a group-transfer (Ping-Pong)-type mechanism of catalysis.
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页码：325 / 331
页数：7
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