Accumulation of heavy metals is one of the major concerns for the environmental safety because of their toxicity and non-degradability. In particular, cadmium and several cadmium-containing compounds are known as carcinogens and can induce many types of cancer. Among promising strategies of cadmium removal, one emerging technology is the use of tunable, metal binding biopolymers based on elastin-like polypeptides (ELPs). An ELP consisting of the repeating pentapeptide of specific amino acids, Val-Pro-Gly-Xaa-Gly (where the “guest residue” Xaa is any amino except Proline), undergoes a reversible phase transition at a specific temperature (transition temperature, Tt). For effective elimination of cadmium, synthetic phytochelatin (EC), which is a metal-binding protein and has a repetitive motif (Glu-Cys)nGly, was fused with the ELP. We expected that a fusion protein constituting ELP and EC can detect and remove cadmium without any complex process. In this study, a fusion protein was expressed in E.coli and metal binding ability of EC to cadmium was examined quantitatively. In addition, transition temperature variation when the fusion protein binds cadmium was analyzed.
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
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