In this study， myosin isolated from Nemipterus virgatus was added with 10% potato starch (PS)-ovalbumin (OVA) complex with different ratios to study the interactions between PS-OVA and myosin as well as their effects on the gel properties of myosin. The component interactions in the PS-OVA-myosin composite system were determined by particle size， zeta potential， sulfhydryl group， surface hydrophobicity and UV spectra， and the effect of PS-OVA-myosin interactions on myosin gel was further disclosed by rheological behavior， intermolecular forces， microstructure， etc. The results showed that after adding 10% PS-OVA complex， the UV absorbance， total sulfhydryl content and surface hydrophobicity of the PS-OVA-myosin composite system increased by 5.53%， 24.28% and 17.53%， respectively， and the net charge decreased by 40.75%， indicating that there were non-covalent and covalent interactions such as hydrophobic interaction， hydrogen bond， and disulfide bond in PS-OVA-myosin composite system， which promoted the conformational change of myosin. Simultaneously， with the increase of PS and decrease of OVA in the exogenous compound， the gel strength， hardness， β-sheet content and storage modulus of the PS-OVA-myosin composite gel increased by 7.68%， 20.10%， 11.03% and 12.07%， respectively， and then decreased to 0.94%， 7.77%， 0.08% and 4.99%. When the ratio of PS-OVA was 3 ∶ 7， the composite system had the highest UV absorbance， the smallest net charge， and the largest particle size， sulfhydryl content， and surface hydrophobicity. The gel strength， hardness， and β-sheet content of the composite gel were the highest after heating when the ratio of PS-OVA was 3 ∶ 7， and the gel network was most compact and homogeneous. Conclusion: The PS-OVA complex with mass ratio of 3 ∶ 7 could promote the component interaction of the PS-OVA-myosin composite system， facilitate the aggregation and cross-linking of myosin through the interaction forces such as hydrophobic interactions， hydrogen bonds， disulfide bonds， etc.， fill the myosin gel network， which further improve the gel properties of myosin.