Synergistic inhibition of lipid oxidation by pea protein hydrolysate coupled with licorice extract in a liposomal model system.

Abstract

Fourteen pea protein hydrolysates (PPHs) were prepared using different proteases and tested for antioxidant activity in a liposomal model system under oxidative stress (100 μM FeCl3/2 mM ascorbate). Almost all PPHs inhibited lipid oxidation, and those prepared from heated protein with Flavourzyme (Fla-PPH) or Protamex (Pro-PPH) were the most effective. Remarkable synergistic effects were observed on both Fla-PPH and Pro-PPH with licorice extract (LE). Electron microscopy revealed a self-assembled network that appeared to provide crucial protection of liposome against oxidation. The presence of LE enhanced the antioxidant potential by producing a more compact network apparently via PPH-LE complexation. Zeta-potential measurements suggested electrostatic interactions are important driving forces for the accumulation of active peptides at the liposome interface. Peptides rich in leucine, lysine, glutamic acid, glutamine, valine, or proline with a hydrophobic N-terminus, as identified by mass spectrometry, were implicated in the antioxidative protection.