Chromatography purification of the promising biomaterial: elastin-like protein genetically expressed in Escherichia coli

摘要

Inverse transition cycling is the most popular purification method for elastin-like polypeptides, a promising biomaterial with high biocompatibility and functional properties. However this mean depends on the high concentration of elastin-like protein in solution, large molecule weight or high-salt concentration. To overcome the defects of inverse transition cycling, we successfully developed a chromatographic method to effectively purify the recombinant elastin-like proteins expressed in Escherichia coli BL21(DE3), with formulation of MORS ((VPGVG)10S)5 and a transition temperature higher than 40 °C. Ion-exchange chromatography was carried out to remove the most charged proteins from cell lysis prior to hydrophobic proteins were isolated using reverse phase chromatography. A maximum quantity of 303.92 ± 10.17 mg per liter of culture was obtained for the recombinant elastin-like proteins and the purity of the recombinant ELP50 was more than 95%.