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• A lipid and protein co-oxidation model containing fish oil and WPI was established. • Resveratrol significantly suppressed lipid oxidation and protein carbonylation. • Formation of MDA-bound proteins in WPI was restrained by resveratrol. • Decrease in protein digestibility under oxidation was mitigated by resveratrol. • Phenol-protein interactions also contribute to physicochemical changes in WPI. In this study, the impact of resveratrol (RES) on co-oxidation of lipid and protein in a fish oil-fortified whey protein isolate (WPI) emulsion was investigated. Oil-in-water (O/W) emulsions containing 1% fish oil, 6 mg/mL of WPI and RES (0.08 ~ 2 mM) were oxidatively stressed using a Fenton system at 25 °C for 24 h. The incorporation of RES significantly suppressed lipid oxidation (TBARS) and protein carbonylation. Oxidation-induced decrease on protein sulfhydryl content and surface hydrophobicity were partially attenuated by RES, but protein tryptophan fluorescence was further decreased with the increased concentration of RES. Visualization of protein patterns and MDA-bound protein suggested that RES is capable of inhibiting protein modification induced by secondary products of lipid oxidation. Significant decrease in protein digestibility under oxidizing condition was also mitigated by RES. Our study contributes to the exploration of complicated interactions between oxidized lipids and proteins when phenolic compounds are present. [ABSTRACT FROM AUTHOR]