Characterization of ACE‐Inhibitory Peptide Associated with Antioxidant and Anticoagulation Properties

Abstract: A bioactive peptide Arg–Val–Pro–Ser–Leu (RVPSL) obtained from egg white protein was characterized by LC‐MS and further chemically synthesized by the Fmoc solid phase method and investigated in terms of its angiotensin converting enzyme (ACE)‐inhibitory activity, antioxidant property, and anticoagulation activity, as well as its stability in a simulated gastrointestinal digestion. The peptide exhibited an ACE‐inhibitory activity with an IC 50 value of 20 μM. Also, the peptide could efficiently quench the (1,1)‐diphenyl‐2‐picrylhydrazyl free radicals and exhibit high anticoagulation activity with a complete inhibition at 100 mM. Moreover, the peptide has a good stability against protease digestion. These results suggest that the peptide RVPSL may have potential to be used in nutraceuticals and functional food. Practical Application: The present research revealed a novel multifunctional peptide hydrolyzed from egg white protein. The peptide RVPSL was not only able to block the amplification of the coagulation cascade, but also able to inhibit ACE activity.