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Co-solute assistance in refolding of recombinant proteins
Author(s) -
Mir Najd Gerami Susan,
Safar Farajnia,
Mahboudi Feridoun
Publication year - 2011
Publication title -
african journal of biotechnology
Language(s) - English
Resource type - Journals
ISSN - 1684-5315
DOI - 10.5897/ajb10.2047
Subject(s) - recombinant dna , inclusion bodies , escherichia coli , chemistry , protein folding , in vitro , biochemistry , protein aggregation , folding (dsp implementation) , engineering , electrical engineering , gene
Prokaryotic expression system is the most widely used host for the production of recombinant proteins but inclusion body formation is a major bottleneck in the production of recombinant proteins in prokaryotic cells, especially in Escherichia coli . In 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 for in 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. This study 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.

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