Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides
- Authors
- Choi, Heelak; Han, Sung-Jin; Won, Jong-In
- Issue Date
- Oct-2020
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Elastin-like polypeptide (ELP); Synthetic phytochelatin (EC); Cadmium adsorption; EC-ELP
- Citation
- ENZYME AND MICROBIAL TECHNOLOGY, v.140
- Journal Title
- ENZYME AND MICROBIAL TECHNOLOGY
- Volume
- 140
- URI
- https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/11530
- DOI
- 10.1016/j.enzmictec.2020.109628
- ISSN
- 0141-0229
- 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. 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.
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Collections - College of Engineering > Chemical Engineering Major > 1. Journal Articles
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