Food-Derived Bioactive Peptides with Antioxidative Capacity, Xanthine Oxidase and Tyrosinase Inhibitory Activity

Bioactive peptides (BPs) released by proteases from different food protein sources are often served as antioxidants in food applications. This study aims to investigate 11 BPs derived from fish and egg white as potential natural antioxidants by antioxidant activity assays. The kinetic activity of the BPs against xanthine oxidase (XOD) and tyrosinase was also analyzed. The antioxidative capacity of the BPs indicated that VWWW (VW4, mackerel meat), followed by IRW (IW3, egg white) and VKAGFAWTANQQLS (VS14, tuna backbone protein), possessed the highest antioxidant activity in 1,1-diphenyl-2-picrylhydrazyl radical (DPPH), 2,2 '-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) and reducing power (RP) assays. Both the free-radical scavenging score predicted from the AnOxPePred algorithm and the DPPH, ABTS and RP results indicated that VW4 was the best antioxidant. Furthermore, the XOD and tyrosinase inhibition by three selected peptides exhibited competitive patterns of effective inhibition. The half maximal inhibitory concentrations (IC50) of the peptides for XOD inhibition were 5.310, 3.935, and 1.804 mM for VW4, IW3, and VS14, respectively, and they could serve as competitive natural XOD inhibitors. The IC50 of the peptides for tyrosinase inhibition were 1.254, 2.895, and 0.595 mM for VW4, IW3, and VS14, respectively. Overall, VW4, IW3, and VS14 are potential antioxidants and natural XOD inhibitors for preventing milk-fat oxidation, and anti-browning sources for inhibiting food-derived tyrosinase oxidation.

Automated summary

The study examined 11 bioactive peptides derived from fish and egg white as potential natural antioxidants by conducting antioxidant activity assays. Among them, VWWW (VW4, mackerel meat), IRW (IW3, egg white), and VKAGFAWTANQQLS (VS14, tuna backbone protein) showed the highest antioxidant activity, indicating their potential as antioxidants and natural xanthine oxidase (XOD) inhibitors. Additionally, these peptides displayed competitive inhibition against both XOD and tyrosinase, suggesting their potential applications in preventing milk-fat oxidation and inhibiting food-derived tyrosinase oxidation.