Heterologous expression of heat shock proteins confers stress tolerance in Escherichia coli, an industrial cell factory: A short review

Abstract Escherichia coli (E. coli) is one of the most widely used cell factories to produce recombinant proteins and biofuels. For large-scale culture, E. coli cells are exposed to various stressors, and overcoming stressful environments is essential for successful industrial use. This review discusses examples of heat shock proteins (Hsps) that improve the viability and growth of bacterial host cells under diverse stress conditions. Hsps are representative molecular chaperones that protect proteins from denaturation, promote the refolding of partially denatured proteins, and consequently enhance stress tolerance. The genetic introduction of suitable heterologous Hsps in E. coli cells could improve the industrial performance of host cells.