Structures and Properties of Antioxidative Peptides Derived from Royal Jelly ProteinFood Chemistry, Volume 113, Issue 1, 1 March 2009, Pages 238-245
Abstract: We previously reported that royal jelly proteins (RJPs) hydrolyzed with protease N show the strong antioxidative activity against the peroxidation of linoleic acid. In this study, 29 antioxidative peptides were isolated from hydrolysate by membrane ultrafiltration, anion-exchange chromatography, gel filtration chromatography, and reverse-phase high performance liquid chromatography…
Analysis of the antioxidative properties of these peptides revealed strong hydroxyl radical scavenging activity, but neither metal-chelating activity nor superoxide-anion radical scavenging activity differed significantly among these peptides…
This suggests that the antioxidant properties of these peptides are due to a combination of these abilities to act as free-radical scavengers. Three tyrosyl dipeptides containing Tyr residues at their C-termini (Lys-Tyr, Arg-Tyr, and Tyr-Tyr) have phenolic hydroxyl groups, which scavenge the free radicals via the mechanism of donating a hydrogen atom from their hydroxyl group.
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