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

3rd International Conference on New Material and Chemical Industry

材料科学;化学工业

Wei, Q.^1^2 ; Wang, X.X.^1 ; Yang, S.S.^1 ; Cui, J.H.^1 ; Xie, X.^1 ; Chen, F.L.^1 ; Li, H.M.^1

Lab of Tissue Engineering, Provincial Key Laboratory of Biotechnology of Shaanxi, College of Life Sciences, Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of China, Northwest University, Taibai North Rd 229, Xi'an, Shaanxi Province

710069, China^1

Medical College, Xi'An Peihua University, University avenue west, Xi'an, Shaanxi Province

710118, China^2

关键词: Chromatographic methods;    Chromatography purifications;    Elastin-like polypeptides;    Escherichia coli bl21;    Functional properties;    High salt concentration;    Ion exchange chromatography;    Reverse phase chromatography;   

Others  :  https://iopscience.iop.org/article/10.1088/1757-899X/479/1/012021/pdf
DOI  :  10.1088/1757-899X/479/1/012021

学科分类：材料科学（综合）

来源: IOP

【 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 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%.