Chromatography purification of the promising biomaterial: elastin-like protein genetically expressed in Escherichia coli. (February 2019)

• Record Type: Journal Article
• Authors: Wei, Q; Wang, X X; Yang, S S; Cui, J H; Xie, X; Chen, F L; Li, H M
• Is Part Of: IOP conference series. Volume 479(2019)
• Publication Date: 2019-02
• Subjects: Materials science -- Periodicals; 620.1105
• DOI: 10.1088/1757-899X/479/1/012021
• Languages: English
• ISSNs: 1757-8981

Abstract

Abstract: 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 MGRS ((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%.