Abstract
In many cases the expressed protein is insoluble and accumulates in so-called inclusion bodies. Several strategies have been developed to improve the solubility of the expressed protein. Disulfide isomerase DsbA could effectively assist proteins folding,both in vivo coexpressed with the target protein,and in vitro replenished as foldases.Moreover,DsbA also has the chaperone-like activity in the assistant refolding of genetically engineered inclusion bodies.Coexpression of DsbA with the target protein could lead to higher levels of soluble protein. In this work, a significantly improved, recombinant Escherichia coli has been developed to degrade the toxic organophosphorus compound, methyl parathion, to non-toxic materials by coexpression of disulfide isomerase DsbA and Methyl Parathion Hydrolase (MPH)-GFP fusion protein. Whole cells expressing DsbA had significant enhancement of MPH activity compared to DsbA-free system and could be easily detected.
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This work was financially supported by the 863 Hi-Tech Research and Development Program of the People’s Republic of China (No. 2007AA06Z335; No. 2009AA06A417).
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Yang, J., Yang, C. & Qiao, C. Overexpression of protein disulfide isomerase DsbA enhanced detoxification of organophosphates and enhanced detectability in the environment following degradation of pesticide residues. World J Microbiol Biotechnol 27, 785–790 (2011). https://doi.org/10.1007/s11274-010-0517-1
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DOI: https://doi.org/10.1007/s11274-010-0517-1