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- Title
Purification and characterization of superoxide dismutase from garlic.
- Authors
Jianguo Liu; Jingbing Wang; Mengmeng Yin; Hu Zhu; Jianren Lu; Zhanfeng Cui
- Abstract
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 l4kDa, 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 50mM 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.
- Subjects
SUPEROXIDE dismutase; GARLIC; ULTRAFILTRATION; ENZYMES; LIQUID chromatography; POLYACRYLAMIDE gel electrophoresis; ISOELECTRIC focusing
- Publication
Food & Bioproducts Processing: Transactions of the Institution of Chemical Engineers Part C, 2011, Vol 89, Issue 4, p294
- ISSN
0960-3085
- Publication type
Article
- DOI
10.1016/j.fbp.2010.07.003