Resveratrol inhibits lipid and protein co-oxidation in sodium caseinate-walnut oil emulsions by reinforcing oil-water interface.

Lipid-protein co-oxidation often causes nutrition loss, texture changes, and shortened shelf-life of emulsions. In this study, resveratrol significantly prevented lipid-protein co-oxidation in sodium caseinate (NaCas)-walnut oil emulsions, and the underlying mechanisms were explored in physical and chemical aspects. NaCas-walnut oil emulsions stabilized by resveratrol exhibited excellent physical stability at 55 °C for 12 days or at room temperature for 10 months due to forming a stable interfacial layer composed of resveratrol-modified NaCas. Furthermore, resveratrol binding caused NaCas structure's partial unfolding and a ∼ 8% increase in hydrophobicity, in turn enhancing NaCas' emulsification properties and electrostatic repulsion. Besides, more than 90% of resveratrol was loaded at the interface and enhanced NaCas' Fe chelating, DPPH scavenging abilities, and O quenching by ∼ 22.6%, 5.26 times, and 31.84%, respectively. Simultaneously, resveratrol significantly improved NaCas' oxidative stability, as reflected by the decrease in adsorbed NaCas' intrinsic fluorescence loss and protein carbonyls gain by ∼ 30% and 37%, respectively. Simultaneously, lipid hydroperoxides and TBARS were reduced by ∼ 30% and 20% in the NaCas-walnut oil emulsions containing 6 mM resveratrol than the control. Our findings contribute to further understanding of the possible interaction among lipid, protein, polyphenols, and their oxidative products at the oil-water interface, minimizing lipid-protein co-oxidation and extending functional oils' shelf life. Finally, walnut oil emulsions with high physical and oxidative stabilities using resveratrol were prepared, further broadening resveratrol's application in the food industry.