The interaction of protein carrier and polyphenol is variable due to their environmental sensitivity. In this study, the interaction between resveratrol and whey protein isolate (WPI), sodium caseinate (SC) and soy protein isolate (SPI) during storage were systematically investigated from the aspects of polyphenol loading, antioxidant activity and oxidability. It was revealed that resveratrol loaded more in the SPI core and existed both in the core of SC micelles and on the particle surface, while WPI and resveratrol mainly formed in complexes. The loading capacity of the three proteins ranked in order SC > SPI > WPI. ABTS assay showed that the antioxidant activity of the protein carriers in the initial state was SC > SPI > WPI. The results of sulfhydryl, carbonyl and amino acid analysis showed that protein oxidability was SPI > SC > WPI. WPI, with the least oxidation, improved the storage stability of resveratrol, and the impact of SC on resveratrol stability changed from a protective to a pro-degradation effect. Co-oxidation occurred between SPI and resveratrol during storage, which refers to covalent interactions. The data gathered here suggested that the transition between the antioxidant and pro-oxidative properties of the carrier is the primary factor to investigate its protective effect on the delivered polyphenol.