DENATURATION OF BACILLUS-STEAROTHERMOPHILUS ALPHA-AMYLASE BY UREA AND DETERGENTS

被引：4

作者：

BRUMM, PJ

TEAGUE, WM

机构：

[1] Enzyme Bio-Systems Ltd., Arlington Heights, 60005, IL

来源：

BIOTECHNOLOGY LETTERS | 1990年 / 12卷 / 04期

关键词：

D O I：

10.1007/BF01093517

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：

Denaturation of Bacillus stearothermophilus α-amylase by urea and detergents was investigated for the purpose of understanding the mechanism of denaturation of this enzyme. The enzyme was extremely resistant to denaturation by detergents at 60° C, either in the presence or absence of added calcium. Addition of EDTA was necessary to obtain denaturation by detergents. The rate of denaturation of the α-amylase by urea was strongly dependent on the incubation pH and presence or absence of calcium ions. Calcium-binding groups were shown to have pKa values of 5.5 for exogenous calcium and 4.7 to 4.8 for endogenous calcium. A mechanism is proposed for the denaturation of Bacillus stearothermophilus α-amylase. © 1990 Kluwer Academic Publishers.

引用

页码：253 / 258

页数：6

共 6 条

[1]

BRUMM P J, 1988, Food Biotechnology (New York), V2, P67

[2] A REDUCED STABILITY BACILLUS-STEAROTHERMOPHILUS ALPHA-AMYLASE FOR FOOD APPLICATIONS [J].