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An efficient and easily scaled up method to isolate superoxide dismutase from garlic is proposed. The separation and purification procedure consists of phosphate buffer extraction, heat treatment and a two-stage ultrafiltration process. The enzyme was purified 139-fold with a specific activity of 2867 U/mg protein and a yield of 91%. The native molecular mass of superoxide dismutase estimated by fast protein liquid chromatography on a Superose 6 column was 28 kDa. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed a single band near 14 kDa, suggesting that native enzyme was homo-dimeric. The optimal pH for enzyme activity was found to be 7.0, and at this pH the enzyme exhibited maximum activity at 50 °C in 50 mM sodium phosphate buffer. Among various metal ions examined, Cu2+ and Zn2+ exerted a positive effect on superoxide dismutase activity, whereas Hg2+ was found to be a strong inhibitor. The final purified enzyme had an isoelectric point of 5.1-5.4 and a sheet content of 46%, consistent with the literature values. This shows that the purified SOD folded with a reasonable secondary structure. © 2010 The Institution of Chemical Engineers.

Original publication




Journal article


Food and Bioproducts Processing

Publication Date





294 - 299