Method for enhancing solubility of the expressed recombinant proteins in

The production of correctly folded protein in 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 solu...

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Bibliographic Details
Published inBioTechniques Vol. 37; no. 3; pp. 418 - 423
Main Authors Ghosh, Sudip, Rasheedi, Sheeba, Rahim, Sheikh Showkat, Banerjee, Sharmistha, Choudhary, Rakesh Kumar, Chakhaiyar, Prachee, Ehtesham, Nasreen Z, Mukhopadhyay, Sangita, Hasnain, Seyed E
Format Journal Article
LanguageEnglish
Published Future Science Ltd 01.09.2004
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Summary:The production of correctly folded protein in 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 . This method can also be used to enhance the solubility of other heterologous recombinant proteins expressed in a bacterial system.
ISSN:0736-6205
1940-9818
DOI:10.2144/04373ST07