Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coli.

ABSTRACT: The recovery of active proteins from inclusion bodies usually involves chaotrope-induced denaturation, followed by refolding of the unfolded protein. The efficiency of renaturation is low, leading to reduced yield of the final product. In this work, we report that recombinant proteins can be overexpressed in the soluble form in the host expression system by incorporating compatible solutes during protein expression. Green fluorescent protein (GFP), which was otherwise expressed as inclusion bodies, could be made to partition off into the soluble fraction when sorbitol and arginine, but not ethylene glycol, were present in the growth medium. Arginine and sorbitol increased the production of soluble protein, while ethylene glycol did not. Production of ATP increased in the presence of sorbit

SUBMITTER: Prasad S 

PROVIDER: S-EPMC3127727 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature