Related Experiment Video
Updated: Jun 2, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Optimization of Salmonella enteritidis recombinant heat shock protein 60 production
K Rainczak1, J Bajzert, J Galli
1Department of Immunology, Physiopathology and Veterinary Prevention, Wroclaw University of Environmental and Life Sciences, Norwida 31, 50-375 Wroclaw, Poland.
Abstract:
The aim of the study was to optimize conditions for producing Salmonella Enteritidis recombinant heat shock protein 60 (rHsp60). Seven Escherichia coli host strains (Rosetta, Turner, C41, C43, Origami, BL21pLys, Rosetta pLys) were transformed by a recombinant plasmid containing Hsp60 gene from Salmonella Enteritidis, and then cultured and induced by isopropyl-beta-D-thiogalactopyranoside (IPTG). The highest S. Enteritidis rHsp60 yield was obtained using E. coli strain C41. Induction of this strain using IPTG allowed the yield 400 microg of S. Enteritidis Hsp60 protein/2L of culture, but by autoinduction the yield exceeded 800 microg/2L.

