Antioxidative activities of some peptides isolated from hydrolyzed potato protein extract

Three peptides (5A, 5C and 6C), purified from potato protein hydrolysate fractions, possessed antioxidative activities. Isolation and purification were carried out using gel permeation chromatography and successive reverse-phase HPLC. These three peptide fractions were sequenced and identified as Phe-Gly-Glu-Arg, Phe-Asp-Arg-Arg and Phe-Gly-Glu-Arg-Arg, respectively. The fractions 5A, 5C and 6C inhibited linoleic acid oxidation by 55.3%, 58.5% and 61.7% using beta-carotene decolorization assay system, while the inhibition ratio was 32.1%, 93.0% and 93.4% in the ferric thiocyanate assay system, respectively. The peptide fractions 5A, 5C and 6C also repressed lipid oxidation by 24.2%, 14.7% and 26.4% in the erythrocyte membrane ghost assay system, respectively. Oral administration of 100 mg/kg of body weight of the chemically synthesized peptides, 5A, 5C and 6C to rats (male Wistar) 30 min prior to ethanol injection reduced ethanol-induced gastric mucosal damage by 67.9%, 57.0% and 60.3%, respectively. Conclusively, these peptides have shown real potent antioxidative activities and could further be investigated for potential use as food additives. (C) 2009 Elsevier Ltd. All rights reserved.