Studies on the thermostability and conformation of thermostable α-amylase from Bacillus licheniformis A 4041

被引：0

作者：

Zhao, Y ^{[1
]}

Dong, QC ^{[1
]}

Ma, HW ^{[1
]}

Yan, BS ^{[1
]}

Fei, XF ^{[1
]}

Wang, GY ^{[1
]}

机构：

[1] Jilin Univ, Dept Mol Biol, Changchun 130023, Peoples R China

来源：

CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE | 1998年 / 19卷 / 06期

关键词：

Bacillus licheniformis; thermostability; alpha-amylase; conformation;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The influence of heat on the conformation and stability of alpha-amylase alpha-III fraction from Bacillus Licheniformis A, 4041 was studied by means of the fluorescence and CD spectra, Heated at 80 degrees C for 15 min, the enzyme hardly lost its activity, At the same time, a considerable change of its fluorescence and CD spectra was observed. It was shown that, comparing with the whole conformation of the enzyme molecule, the active site has a relative stability. Heated at 90 degrees C far 15 min, the conformational and active changes resulted by Ca2+ and starch were different. The Ca2+ mainly affects the:whole enzyme molecular conformations, whereas the substrate is important to sustain the activity, It indicates that the structure of enzymatic active site plays an important role to the thermostability of the alpha-III.

引用

页码：921 / 923

页数：3