Naringenin (Nar), a natural flavonoid compound, exhibits diverse bioactivities. However, its application and development are limited by poor water solubility and stability. Soybean protein, a plant-based protein, is commonly used as a carrier for natural bioactive compounds, providing protection and delivery functions. In this study, heat-treated soybean 7S [H7S(pH 7.4),H7S(pH 2.0)]and 11S [H11S(pH 7.4),H11S(pH 2.0)] proteins were prepared at pH 7.4 and 2.0 to investigate their interaction mechanisms with Nar and to analyze the effects of complex formation on Nar's stability and bioaccessibility. Fluorescence spectroscopy results indicated that Nar formed a 1∶1 complex with H7S/H11S through a static quenching mechanism. The binding forces between H7S and Nar, as well as H11S (pH 2.0) and Nar, were dominated by hydrogen bonds and van der Waals forces (ΔH⁰<0, ΔS⁰<0), whereas the primary interactions between H11S (pH 7.4) and Nar involved hydrogen bonds and hydrophobic interactions (ΔH⁰<0, ΔS⁰>0). Three-dimensional fluorescence spectroscopy, UV-Vis absorption spectroscopy, and infrared spectroscopy analyses revealed that their interaction altered the secondary structure of the proteins and increased the polarity of the microenvironment surrounding tryptophan and tyrosine residues. The maximum encapsulation efficiency of Nar by H7S/H11S reached 90.37%, and the formation of complexes significantly enhanced Nar's water dispersibility, with maximum solubility increasing by 34.85-fold (in PBS with pH 7.4) and 48.84-fold (in PBS with pH 2.0), respectively. ABTS⁺ radical scavenging and FRAP assays demonstrated that the antioxidant capacity of the complexes was significantly higher than that of free Nar. Additionally, the complexes improved Nar's hydrophilicity by reducing interfacial tension between Nar and the release medium, thereby promoted its release. The maximum release rates of Nar in PBS dialysis medium increased by 49.37% (pH=7.4) and 48.55% (pH=2.0) compared to its free state, with the release mechanism being non-Fickian diffusion, where the release rate was influenced by protein swelling and Nar's diffusion path. Simulated digestion experiments showed that the complexes hindered digestive enzymes from contacting Nar, increasing its retention rate by 150.24% and improving bioaccessibility by 3.69-fold. The inhibitory effect of the complexes on enzyme activity exhibited a positive correlation with the release rate but was also influenced by the steric hindrance of the proteins. Except for the H7S-Nar complex prepared at pH 2.0, all other complexes enhanced Nar's inhibitory effect on α-amylase activity, while slightly reducing its inhibitory activity against α-glucosidase. These findings provided new insights for further expanding the application of Nar in the food industry. 〖