Keywords

Elastin-Like Tag, Reversible Phase Change, Recombinant Protein, Separation And Purification

Abstract

Abstract Elastin-like polypeptide (ELP) is a very promising tag for the isolation and purification of recombinant proteins. This synthetic protein polypeptide is composed of pentapeptide repeating sequence units (VPGXG) connected in series and has temperature-induced reversible phase change properties. After ELP is fused to the target protein, it imparts similar reversible phase transition properties to the recombinant protein. After multiple reversible phase transition cycles (ITC), the ELP fusion protein can be selectively isolated from the protein solution mixture, and then subjected to specific enzyme digestion or changing environmental conditions to trigger self-cleavage of the intein. The ELP tag is removed to obtain a single target protein, enabling simple and rapid isolation and purification of recombinant proteins. Currently, this technology has been successfully used in prokaryotic E. coli and plant expression systems. The maximum yield of ELP-green fluorescent fusion protein expressed in E. coli can reach 1.6 g/L. This non-chromatographic method for separating and purifying recombinant proteins has the advantages of simple technology, fast operation, low cost, and easy expansion. Focus on the principle, technical route and development direction of this technology.

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Original research done by Sun Lihui, Hu Xuejun, Xu Chongbo, Lin Heng

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