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Updated: Dec 9, 2025

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides
Heelak Choi1, Sung-Jin Han1, Jong-In Won1
1Department of Chemical Engineering, Hongik University, Seoul, South Korea.
Abstract:
Elastin-like polypeptides (ELPs) are stimulus-responsive protein-based biopolymers that exhibit phase transition behavior. By joining them to synthetic phytochelatin (EC), EC-ELP fusion proteins with temperature sensitivity and metal-binding functionality were generated to remove heavy metal ions biologically. Three different EC domains (EC10, EC20, EC30) were incorporated into the ELP, and the EC-ELP fusion proteins were expressed in E. coli. Their thermal properties and metal binding abilities were then investigated according to the EC length. In addition, the feasibility of reusing EC-ELPs and the cadmium ion binding affinity of reused EC-ELPs were explored.
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