dc.contributor.author | Gerami, SMN | |
dc.contributor.author | Farajnia, S | |
dc.contributor.author | Mahboudi, F | |
dc.date.accessioned | 2018-08-26T08:06:57Z | |
dc.date.available | 2018-08-26T08:06:57Z | |
dc.date.issued | 2011 | |
dc.identifier.uri | http://dspace.tbzmed.ac.ir:8080/xmlui/handle/123456789/50119 | |
dc.description.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 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. | |
dc.language.iso | English | |
dc.relation.ispartof | AFRICAN JOURNAL OF BIOTECHNOLOGY | |
dc.subject | Refolding | |
dc.subject | protein aggregation | |
dc.subject | low-molecular-weight additives | |
dc.subject | arginine | |
dc.title | Co-solute assistance in refolding of recombinant proteins | |
dc.type | Review | |
dc.citation.volume | 10 | |
dc.citation.issue | 53 | |
dc.citation.spage | 10811 | |
dc.citation.epage | 10816 | |
dc.citation.index | Web of science | |
dc.identifier.DOI | https://doi.org/10.5897/AJB10.2047 | |