Tartary buckwheat (Fagopyrum tataricum Gaertn.) albumin was hydrolyzed by alkaline protease, and three new antioxidant peptides (P1, P2, and P3) were successfully separated from the hydrolysate (TBAH). The sequences of the three antioxidant peptides were Gly-Glu-Val-Pro-Trp (GEVPW), Tyr-Met-Glu-Asn-Phe (YMENF), and Ala-Phe-Tyr-Arg-Trp (AFYRW), and their molecular weights were 586.65, 702.79, and 741.85 Da, respectively. All three peptides have a good antioxidant capacity, and P3 (AFYRW) demonstrates the best antioxidant activity of the three. The IC50 values of AFYRW for scavenging hydroxyl radicals (OH·) and (1,1-diphenyl-2-picrylhydrazyl) DPPH· free radicals were 0.65 and 0.64 mM, respectively. In addition, AFYRW exhibits the strongest lipid peroxidation inhibition ability and the highest reducing power. The results of this research indicate that the three isolated peptides can be used in the development of various antioxidant additives in the food and pharmaceutical industries.
Keywords: antioxidant activity; hydrolysis; peptide; tartary buckwheat albumin.
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