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Biochemistry Research International
Volume 2011 (2011), Article ID 631607, 6 pages
http://dx.doi.org/10.1155/2011/631607
Review Article

Chemical Assistance in Refolding of Bacterial Inclusion Bodies

Medical Biotechnology Research Center, Pasteur Institute of Iran, Tehran 13169 43551, Iran

Received 17 March 2011; Accepted 27 May 2011

Academic Editor: Daniel N. Hebert

Copyright © 2011 Mona Alibolandi and Hasan Mirzahoseini. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Escherichia coli is one of the most widely used hosts for the production of recombinant proteins but insoluble expression of heterologous proteins is a major bottleneck in production of recombinant proteins in E. coli. In vitro refolding of inclusion body into proteins with native conformations is a solution for this problem but there is a need for optimization of condition for each protein specifically. Several approaches have been described for in vitro refolding; most of them involve the use of additives for assisting correct folding. Cosolutes play a major role in refolding process and can be classified according to their function as aggregation suppressors and folding enhancers. This paper presents a review of additives that are used in refolding process of insoluble recombinant proteins in small scale and industrial processes.