Cloning, Expression and Characterization of a Novel Iron Superoxide Dismutase from Magnetospirillum magneticum AMB-1
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 ℃,which was stable in the pH range from 5.4 to 8.2 and at temperature from 25 to 45 ℃.These results suggest that fesod may have very attractive applications in cosmetics industry as an anti ageing protein in a moderate temperature range.
Magnetospirillum magneticum AMB-1 Superoxide dismutase Gene cloning and expression enzymatic characterization
Qilei Wang Xiangqian Li Yemin Xue
Faculty of Life Science & Chemical Engineering, Huaiyin Institute of Technology, Huaian, PR China 22 Department of Food Science and Nutrition, GinLing College, Nanjing Normal University, Nanjing,PR Chi
国内会议
大连
英文
155-160
2012-07-01（万方平台首次上网日期，不代表论文的发表时间）