Cloning, Expression and Characterization of a Novel Iron Superoxide Dismutase from Magnetospirillum magneticum AMB-1

Abstract:

The gene fesod encoding iron superoxide dismutase from Magnetospirillum AMB-1 with a calculated 22kDa was cloned and efficiently expressed in Escherichia coli BL21 (DE3). The open reading frame of 597 nucleotides encoded a protein of 199 amino acids without the signal peptide sequence. Recombinant enzyme fesod was purified by IMAC (Ni2+) in a single step to electrophoretic homogeneity presented as a single protein band on SDS-PAGE. The recombinant enzyme displayed maximum activity at 25 °C, which was stable in the pH range from 5.4 to 8.2 and at temperature from 25 to 45 °C. These results suggest that fesod may have very attractive applications in cosmetics industry as an anti ageing protein in a moderate temperature range.

• Periodical: Advanced Materials Research (Volumes 610-613)
• Pages: 124-128
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.610-613.124
• Online since: December 2012
• Authors: Xiang Qian Li, Qi Lei Wang, Ye Min Xue
• Keywords: Enzymatic Characterization, Gene Cloning and Expression, Magnetospirillum Magneticum AMB-1, Superoxide Dismutase

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