Application of molecular chaperone to increase the expression of soluble human-like collagen in Escherichia coli

摘要

Human-like collagen (HLC) is a soluble recombinant protein expressed in Escherichia coli BL21, but the over-expression of recombinant proteins in host cells often leads tomisfolding and aggregation. In order to increase percent of soluble HLC in total HLC, chaperone was introduced. GroEL system cooperated with GroES was found to be beneficial for the enhancement of HLC solubility, and electrophoresis results showed that chaperone was coordinately co-overproduced with recombinant humanlike collagen to optimize de novo folding.When 2.0 g/L of arabinose was added at the start of cultivation, the production of soluble HLC was increased by 55% in Escherichia coli BL21 3.7 pGro7 compared to its parent strain without carrying chaperone plasmid.