Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides

被引:8
作者
Choi, Heelak [1 ]
Han, Sung-Jin [1 ]
Won, Jong-In [1 ]
机构
[1] Hongik Univ, Dept Chem Engn, Seoul 04066, South Korea
基金
新加坡国家研究基金会;
关键词
Elastin-like polypeptide (ELP); Synthetic phytochelatin (EC); Cadmium adsorption; EC-ELP; HEAVY-METALS; METALLOTHIONEINS; PEPTIDES; PROTEINS; DOMAIN;
D O I
10.1016/j.enzmictec.2020.109628
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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. coll. 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.
引用
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页数:5
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