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Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides
Enzyme and Microbial Technology ( IF 3.4 ) Pub Date : 2020-10-01 , DOI: 10.1016/j.enzmictec.2020.109628
Heelak Choi 1 , Sung-Jin Han 1 , Jong-In Won 1
Affiliation  

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.

中文翻译:

EC-ELP融合多肽的热特性和镉结合行为

弹性蛋白样多肽 (ELP) 是刺激响应性蛋白质生物聚合物,具有相变行为。通过将它们与合成植物螯合素 (EC) 结合,产生具有温度敏感性和金属结合功能的 EC-ELP 融合蛋白,以生物去除重金属离子。三个不同的 EC 结构域(EC10、EC20、EC30)被整合到 ELP 中,并且 EC-ELP 融合蛋白在大肠杆菌中表达。然后根据 EC 长度研究它们的热性能和金属结合能力。此外,还探讨了重复使用 EC-ELPs 的可行性和重复使用的 EC-ELPs 的镉离子结合亲和力。
更新日期:2020-10-01
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