African Journal of
Biotechnology

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12487

Review

Co-solute assistance in refolding of recombinant proteins

Susan Mir Najd Gerami2, Safar Farajnia1,2* and Feridoun Mahboudi3
  1Biotechnology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. 2Infectious and Tropical Disease Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. 3Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Email: [email protected]

  •  Accepted: 13 July 2011
  •  Published: 14 September 2011

Abstract

 

Prokaryotic expression system is the most widely used host for the production of recombinant proteins but inclusion body formation is a major bottleneck in theproduction of recombinant proteins in prokaryotic cells, especially in Escherichia coliIn vitro refolding of inclusion body into the the 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 forin vitro refolding; most of them involve the use of additives for assisting correct refolding. Co-solutes play a major role in refolding process and can be classified according to their function as, aggregation suppressors and folding enhancers. Thisstudy presents a review of additives that are used in refolding process of insoluble recombinant proteins in small scale and industrial process.

 

Key words: Refolding, protein aggregation, low-molecular-weight additives, arginine.