从以烷烃为生长底物的热带假丝酵母中纯化酒精氧化酶及其某些特性

Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis.

作者信息

Dickinson F M, Wadforth C

机构信息

Department of Applied Biology, University of Hull, U.K.

出版信息

Biochem J. 1992 Mar 1;282 ( Pt 2)(Pt 2):325-31. doi: 10.1042/bj2820325.

DOI:10.1042/bj2820325

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1130782/

Abstract

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 Mr 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-I-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.

摘要

从以烷烃为生长底物的热带假丝酵母的膜组分中纯化得到了均一的乙醇氧化酶。该酶似乎是由两个大小相等、分子量为70000的亚基组成的二聚体。纯化后的酶对光敏感，含有黄素类物质，该物质可通过煮沸和蛋白水解消化相结合的方式释放出来。黄素类物质的具体身份尚不清楚，但它不是黄素单核苷酸（FMN）、黄素腺嘌呤二核苷酸（FAD）或核黄素。该酶对十二烷-1-醇的活性最高，但也能作用于其他长链醇。该酶对长链醛表现出较弱但显著的活性。以癸烷-1-醇为底物进行的详细动力学研究表明，其催化机制为基团转移（乒乓）型。

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