Purification and characterization of a 32-kDa laccase-like stilbene oxidase produced by Botrytis cinerea Pers.:Fr.

被引：0
|
作者：
Pezet, R [1 ]
机构：
[1] Swiss Fed Agr Res Stn Plant Prod Changins, CH-1260 Nyon, Switzerland
来源：
FEMS MICROBIOLOGY LETTERS | 1998年 / 167卷 / 02期
关键词：
Botrytis cinerea; laccase; stilbene oxidase; resveratrol;
D O I：
10.1016/S0378-1097(98)00391-7
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
A 32-kDa laccase-like stilbene oxidase was purified to homogeneity (one single band on SDS-PAGE) from Botrytis cinerea liquid culture medium enriched with pectin. Two major isoforms with pI 4.35 and 4.3 were revealed by isoelectric focusing (IEF). This enzyme oxidizes the grape stilbenic phytoalexins, resveratrol and pterostilbene. Syringaldazine is poorly oxidized by this stilbene oxidase as compared to the rate of stilbene oxidation. This enzyme catalyses the oxidation of resveratrol to epsilon-viniferin. (C) 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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收藏
页码：203 / 208
页数：6
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