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Chickpea chelating peptides inhibit copper-mediated lipid peroxidation

AutorTorres-Fuentes, Cristina ; Alaíz Barragán, Manuel ; Vioque, Javier
Palabras claveChelating peptides
Low-density lipoprotein
Antioxidant peptides
Protein hydrolysate
Fecha de publicación2014
EditorJohn Wiley & Sons
CitaciónJournal of the Science of Food and Agriculture 94: 3181- 3188 (2014)
Resumen© 2014 Society of Chemical Industry. BACKGROUND: Transition metals produce radical oxygen species promoting lipid peroxidation processes that favor the development of cardiovascular and neurodegenerative diseases. In addition, the oxidation of lipids present in food may affect the quality of food products. Therefore antioxidants counteracting these metal pro-oxidant effects may have high potential for the pharmacology and food industries. This study investigated the capability of peptide fractions purified from chickpea protein hydrolysate to inhibit copper-mediated lipid peroxidation in three different lipid substrates: β-carotene, unsaturated fatty acid mixture and low-density lipoprotein. RESULTS: Peptide fractions with the highest histidine content were the most antioxidant. This antioxidant effect is mainly due to the capability of histidine to bind copper and act as a hydrogen donor through its imidazole ring. CONCLUSION: The results suggest that chickpea proteins are a potential source of antioxidant peptides that may be included as ingredients in functional foods with beneficial health effects. In addition, these antioxidant peptides may be useful to protect food products from lipid peroxidation processes and thus increase their quality and shelf life.
Identificadoresdoi: 10.1002/jsfa.6668
issn: 1097-0010
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