Improved recombinant protein production using heat shock proteins in Escherichia coli.

Recombinant proteins are widely used in biopharmaceutical, biochemical, and agricultural industries. Escherichia coli is one of the most frequently used cell systems to produce recombinant proteins because it has various advantages over its eukaryotic counterparts. Understanding the molecular mechanisms involved in E. coli , which produce recombinant proteins, is essential to develop techniques to enhance production efficiency. This review discusses the strategies that utilize heat shock proteins (Hsps) to successfully produce recombinant proteins in E. coli. The effects of the co-expression and gene deletion of Hsps on the yield, solubility, specific activity, and localization of the recombinant proteins were reviewed to provide information for future studies and propose strategies to overcome the difficulties in producing recombinant proteins in a bacterial system. Furthermore, the possible uses of eukaryotic Hsps from archaea, plants, and animals as co-expression chaperones to compensate for the bacterial system were discussed. • The recombinant protein production can be improved by the co-expression of heat shock proteins (Hsps) in Escherichia coli. • The characteristics of the recombinant protein should be considered when selecting a co-expression Hsp partner. • The yield, solubility, and specific activity of recombinant proteins should be considered independently. • Co-expression of multiple Hsps, Hsp in-frame fusion, or Hsp gene deletion can be efficient strategies. • Heterologous Hsps from other organisms can further improve recombinant protein production in E. coli. [ABSTRACT FROM AUTHOR]