Formation of disulfide-bridged dimers during thermoinactivation of glucoamylase from Aspergillus niger

被引：12

作者：

Sasvári, Z ^{[1
]}

Asbóth, B ^{[1
]}

机构：

[1] Inst Biochem & Prot Res, Agr Biotechnol Ctr, H-2101 Godollo, Hungary

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1998年 / 22卷 / 06期

基金：

匈牙利科学研究基金会;

关键词：

glucoamylase; disulfide exchange; thermoinactivation;

D O I：

10.1016/S0141-0229(97)00235-4

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In the course of thermoinactivation of the smaller izoenzyme and of a truncated form of glucoamylase from Aspergillus niger, we observed the formation of disulfide-linked dimers. Molecular modelling studies indicated and the cyanogen bromide cleavage pattern gave corroborating evidence that it is the Cys 222-449 intramolecular disulfide bond that opens up and reforms intermolecularly to yield dimers. Since the dimer displayed the same activity as the native enzyme toward maltopentaose and soluble starch and showed increased thermostability at temperatures above 68 degrees C, it appears a prospective candidate for industrial usage. (C) 1998 Elsevier Science Inc.

引用

页码：466 / 470

页数：5

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