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.
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页码：253 / 258
页数：6
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