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Updated: Aug 18, 2026
The Multifaceted Benefits of Protein Co-expression in Escherichia coli
Published on: February 5, 2015
[Cloning and expression of superoxide dismutase gene from Deinococcus radiodurans in E. coli]
Ling Meng1, Xin Xu, Dong-li Wang
1Department of Medical Technology, West China School of Public Health, Sichuan University, Chengdu 610041, China.
Objective:
To construct expressing recombinant of Mn-SOD of Deinococcus radiodurans and express the target protein in E. coli BL21(DE3).
Methods:
SOD gene was amplified by PCR from genomic DNA of Deinococcus radiodurans and inserted into expression plasmid pET-30a(+) to create the recombinant pET-SOD. After being analyzed by the restriction endonuclease, the plasmid was transformed into E. coli BL21(DE3), and the recombinant protein was expressed after induction by the isopropyl-beta-D-thiogalactopyranoside (IPTG) and was analyzed with SDS-PAGE.
Results:
The recombinant plasmid pET-SOD was obtained, and the recombinant protein was highly expressed in E. coli BL21(DE3). The activity of recombinant superoxide dismutase was 51,800 U per gram of wet bacteria.
Conclusion:
This study has provided a foundation for further studies and applications of the recombinant Mn-SOD.
