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

摘要

The gene fesod encoding iron superoxide dismutase from Magnetospirillum AMB-1 with a calculated 22 kDa 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 (Ni~(2+)) 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.