Fermentation and Purification of Recombinant Enterokinase by Producing in E.coli

The optional high cell-density fermentation conditions,purification methods and biological activity of the recombinant enterokinase in E.coli were studied.In E.coli expressing system,the optimized conditions were temperature 37℃ and pH 7.4.When OD600 is 8.0,with 0.3 mmol/L IPTG induced at temperature 30℃,and continued 3h,the recombinant enterokinase was up to 25% of the total amount of the proteins in E.coli.The purified enterokinase reached a purity of above 80% by SDS-PAGE analysis and showed high activity at fusion protein.