Cloning,Expression and Purification of Microcystis viridis Lectin in Escherichia coli |
| |
Authors: | Yuqin Li Xiaoxia Liao Gu Chen Yeeleng Yap Xuewu Zhang |
| |
Affiliation: | (1) College of Light Industry and Food Sciences, South China University of Technology, 381 Wushan Road, Guangzhou, 510640, China;(2) Institute of Biotechnology, College of Chemical Engineering, Xiangtan University, Xiangtan, China;(3) Davos Life Science Pte. Ltd., 16 Tuas South Street 5, Singapore, 637795, Singapore; |
| |
Abstract: | Microcystis viridis lectin (MVL), a sugar-binding protein originally isolated from freshwater blue-green algae Microcystis viridis, has been reported to have potent anti-HIV activity. In this paper, we described the expression and purification of recombinant-MVL (R-MVL) gene in E. coli. The results demonstrated that the R-MVL in shake flask cultures was primarily expressed either in the form of inclusion bodies at 37°C or in the soluble fraction at 23 °C. Secondly, a one-step purification based on nickel-affinity chromatography was employed and 15 mg of highly purified (>95%) R-MVL from 1 l of cell cultures was yielded. The purified R-MVL was then subjected to MALDI-TOF–MS analysis for protein identification. In conclusion, for the first time, the R-MVL was successfully cloned and expressed in E. coli, which is useful for further study and large-scale cost-effective production of MVL protein. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|