Thermodynamic analysis of Bacillus cereus oligo-1,6-glucosidase and its cumulatively proline-introduced mutant proteins by differential scanning calorimetry

被引：3

作者：

Watanabe, K ^{[1
]}

Fujita, Y ^{[1
]}

Usami, M ^{[1
]}

Takimoto, A ^{[1
]}

Suzuki, Y ^{[1
]}

机构：

[1] Kyoto Prefectural Univ, Dept Appl Biochem, Lab Microbial Physiol & Appl Microbiol, Sakyo Ku, Kyoto 606, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 10卷 / 1-3期

关键词：

Bacillus cereus oligo-1,6-glucosidase; proline-introduced; differential scanning calorimetry;

D O I：

10.1016/S1381-1177(00)00139-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Differential scanning calorimetry (DSC) was used to characterize thermodynamically the stability of Bacillus cereus ATCC7064 oligo-1,6-glucosidase (dextrin 6-alpha-D-glucanohydrolase, EC 3.2.1.10) and its proline-introduced mutants. DSC analysis revealed that the free energy change of unfolding for the mutants cumulatively increased as the number of introduced proline residues increased. The resulting increase in the free energy change was ascribed to the concomitant decrease in the entropy change of polypeptide backbone unfolding in the mutants. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：257 / 262

页数：6

共 10 条

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