Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES

被引：19

作者：

Teshima, T

Kondo, A

Fukuda, H

机构：

[1] KOBE UNIV,FAC ENGN,DEPT SCI & CHEM ENGN,NADA KU,KOBE 657,HYOGO,JAPAN

[2] KOBE UNIV,GRAD SCH SCI & TECHNOL,DIV BIOSCI,NADA KU,KOBE 657,JAPAN

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 1997年 / 48卷 / 01期

关键词：

D O I：

10.1007/s002530051012

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：

Thermally inactivated bovine deoxyribonuclease I (DNase I) and yeast enolase were reactivated by GroEL/ES from Escherichia coli. In both cases, GroEL/ ES was found to have the ability to reactivate inactivated enzymes in an ATP-dependent manner. GroEL/ ES can interact with the enzymes that were denatured at high temperature and convert them to the active conformations. To test the applicability of GroEL/ES to the reactivation processes of thermally inactivated enzymes, GroEL/ES was immobilized using formyl-Cellulofine (GroEL/ES-Cellulofine) and its performance was studied. GroEL/ES-Cellulofine retained a sufficiently high ability to reactivate enzymes. Moreover, GroEL/ES-Cellulofine could be used repeatedly, indicating high durability. These results indicate that immobilized chaperonin is effective for reactivation of enzymes that are thermally inactivated in various bioprocesses.

引用

页码：41 / 46

页数：6

共 15 条

[1] ESSENTIAL ARGINYL RESIDUES IN YEAST ENOLASE [J].