Purification and characterization of α-chaconinase of Gibberella pulicaris

被引：9

作者：

Becker, P ^{[1
]}

Weltring, KM ^{[1
]}

机构：

[1] Univ Munster, Inst Bot, D-48149 Munster, Germany

来源：

FEMS MICROBIOLOGY LETTERS | 1998年 / 167卷 / 02期

关键词：

Fusarium; saponin; chaconine; phytoanticipin; fungal metabolism;

D O I：

10.1016/S0378-1097(98)00390-5

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The potato pathogen Gibberella pulicaris (Fusarium sambucinum) is able to metabolize the potato saponin alpha-chaconine by first removing the 1,2-bound L-rhamnose. The catalyzing enzyme, alpha-chaconinase, is inducible by the substrate and alpha-solanine and alpha-tomatine. The protein with a molecular mass of about 95 kDa was purified by fractionated ammonium sulfate precipitation followed by concanavalin A-Sepharose chromatography and chromatofocusing. The enzyme is active over a wide pH and temperature range and is highly substrate specific for alpha-chaconine with a K-m value of 0.97 mM and V-max of 37.13 nkat. alpha-Solanine and alpha-tomatine are not converted by the enzyme. (C) 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：197 / 202

页数：6

共 19 条

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