In this study， the non-covalent complexation between EC and apoRBF， and the effects on the structural and functional properties of proteins were investigated using a combination of fluorescence， circular dichroism (CD) spectra， transmission electron microscopy (TEM)， dynamic light scattering (DLS). The fluorescence results showed that EC did not change the characteristic emission peak of apoRBF at 330 nm， and the fluorescence intensity of apoRBF decreased with an increase in EC concentration， suggesting EC interacts with apoRBF， causing changes in the tertiary/quaternary structure of the protein， while having no effect on its primary and secondary structure. The fluorescence fitting results showed the binding constant K and the number of binding sites n between EC and apoRBF were 3.65×104 mol/L and 98.5， respectively. After dialysis at 4 ℃ and 40 ℃ for 12 h， the release rates of EC in FEC were 29.1% and 45.9%， respectively， which were lower than those of free EC， indicating that ECs bond to apoRBF， and lower temperature was more conducive to the binding of EC molecules and proteins. After incubation with simulated gastrointestinal fluid for 2 hours， the release rates of EC in FEC were 68.6% and 32.2%， respectively. Compared with the release rate of free EC， it showed a relatively slow and sustained release process， indicating the binding of EC to apoRBF can significantly inhibit the degradation of apoRBF by the protease(s) in simulated gastrointestinal fluid. Additionally， the antioxidant ability of EC in ferritin-EC complex(FEC) was retained but slightly decreased. This study clarified the interaction mechanism between polyphenols and phytoferritin， providing the theoretical reference for the application of non-covalent complexes between (-)-epicatechin and phytoferritin.