Method for enhancing solubility of the expressed recombinant proteins in Escherichia coli

被引：37

作者：

Ghosh, S

Rasheedi, S

Rahim, SS

Banerjee, S

Choudhary, RK

Chakhaiyar, P

Ehtesham, NZ

Mukhopadhyay, S

Hasnain, SE

机构：

[1] Indian Council Med Res, Natl Inst Nutr, Hyderabad 500007, Andhra Pradesh, India

[2] CDFD, Hyderabad, Andhra Pradesh, India

[3] Jawaharlal Nehru Ctr Adv Sci Res, Bangalore, Karnataka, India

来源：

BIOTECHNIQUES | 2004年 / 37卷 / 03期

关键词：

D O I：

10.2144/04373ST07

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The production of correctly folded protein in Escherichia coli is often challenging because of aggregation of the overexpressed protein into inclusion bodies. Although a number of general and protein-specific techniques are available, their effectiveness varies widely. We report a novel method for enhancing the solubility of overexpressed proteins. Presence of a dipeptide glycylglycine, in the range of 100 mM to 1 M in the medium was found to significantly enhance the solubility, (up to 170-fold) of the expressed proteins. The method has been validated using mycobacterial proteins, resulting in improved solubilization, which were otherwise difficult to express as soluble proteins in E. coli. This method can also be used to enhance the solubility of other heterologous recombinant proteins expressed in a bacterial system.

引用

页码：418 / +

页数：4

共 23 条

[1] PURIFICATION AND CHARACTERIZATION OF RECOMBINANT HUMAN P50(CSK) PROTEIN-TYROSINE KINASE FROM AN ESCHERICHIA-COLI EXPRESSION SYSTEM OVERPRODUCING THE BACTERIAL CHAPERONES GROES AND GROEL [J].