Abstract
An antioxidant peptide was purified using consecutive chromatographic methods from chickpea protein hydrolysates (CPH). This peptide was designated as Fra.7. It had a molecular weight of 717.37Da, and its amino acid sequence was identified as Asn-Arg-Tyr-His-Glu by an ABI 4700 proteomics analyser. This antioxidant peptide was identified for the first time from food-derived protein hydrolysates. The molar ratio of the five amino acids in the sequence was 1:1:1:1:1. This antioxidant peptide efficiently quenched the free radical sources 1,1-diphenyl-2-pycryl-hydrazyl (DPPH), hydroxyl, and superoxide free radicals. The Cu2+ and Fe2+ chelating activities were 76.92% and 63.08% at the peptide concentration of 50μgmL−1, respectively. Furthermore, the inhibition of the Fra.7 on lipid peroxidation was greater than that of α-tocopherol. The inhibition ratio of the linoleic acid autooxidation was 88.81% at the eighth day of analysis.
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