analysis of methods to improve the solubility of recombinant bovine sex determining region y protein

Background: inclusion body formation in e. coli is a significant problem in recombinant protein production. the aim of this study was to improve the solubility of recombinant bovine sex determining region y protein (sry) in bl21 (de3) e. coli cells.methods: in this research two recombinant bovine sry (rbsry) sequences were analyzed; these were wild-type sry (wtbsry) and codon-optimized sry (cobsry). their expression in various culture conditions was examined; these differences included iptg concentrations, temperatures, and media stabilizers.results: iptg and temperature significantly affected rbsry solubility (p < 0.001). the optimum iptg concentration and temperatures for wtbsry and cobsry induction were 0.3 mm at 27 and 32 °c, respectively. in addition, arginine and sorbitol concentrations significantly affected rbsry solubility (p < 0.01). solubility of rbsry protein was highest from the cobsry construct in the presence 0.2 m arginine and 0.3 m sorbitol. the highest inclusion body production occurred with high glucose concentrations.conclusions: we found that modifications in temperature and iptg and stabilizer concentrations affected rbsry solubility.