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To investigate the effect of cavitation jet pretreatment on soybean protein isolate-resveratrol (SPI-RES) complexes, SPI was subjected to cavitation jet pretreatment (0min, 2min, 4min, 6min, 8min and 10min) before non-covalent binding with RES to form complexes. The binding of SPI to RES was studied through loading amount and encapsulation efficacy. The interaction and binding mechanism between SPI and RES were studied by using fluorescence spectroscopy, Fourier transform infrared spectroscopy, and molecular docking techniques. In addition, the physical and chemical properties and functional characteristics of the SPI-RES complexes were investigated, including ζ-potential, surface hydrophobicity, and antioxidant activity. The results indicated that after a certain period of cavitation jet pretreatment, SPI significantly increased the encapsulation efficacy and loading amount of RES, and the particle size and ζ-potential of complexes was decreased and increased respectively. The fluorescence spectrum indicated that the quenching of SPI by RES was static quenching, and the reaction was spontaneous. Fourier transform infrared spectroscopy indicated that appropriate cavitation jet pretreatment promoted the transition of SPI from ordered to disordered structures, thereby combining more RES. The thermodynamic parameters and molecular docking results indicated that hydrophobic interactions were the main forces and involved hydrogen bonds. In addition, after appropriate cavitation jet pretreatment, the surface hydrophobicity and antioxidant activity of SPI-RES complexes were increased. The research result can provide a preliminary theoretical basis for the exploration of the application field of cavitation jet pretreatment of soybean protein isolate and the development of fat-soluble active substances in health food.