This study aimed to investigate the interaction mechanism between lysozyme and ovomucin. With lysozyme and ovomucin as controls, the turbidity and apparent viscosity of the interaction between lysozyme and ovomucin were studied under six reaction time(10, 20, 30, 40, 50, 60 min), five temperatures(5, 15, 25, 35, 45 ℃), five pH(7.0, 7.5, 8.0, 8.5, 9.0), and five mixing ratios(0.50∶1.00, 0.75∶1.00, 1.00∶1.00, 1.00∶0.75, 1.00∶0.50). The acting force and structure of aggregates were characterized by SDS-PAGE gel electrophoresis, Fourier transform infrared spectroscopy, low-field nuclear magnetic resonance and scanning electron microscope. The results showed that the conditions of best interaction between lysozyme and ovomucin were incubation time of 40 min, reaction 25 ℃, pH of 8.5, with the ratio of 0.75∶1.00. Compared with ovomucin and lysozyme alone, the complex owned more α-helix and β-turn, and less β-pleated sheet and irregular coil. After interaction, the bound water content increased, and the free water decreased. The hydrophobicity of complex was higher than that of lysozyme, but lower than that of ovomucin. There were electrostatic interaction, hydrophobic interaction, hydrogen bond, disulfide bond and other intermolecular forces in the interaction between ovalbumin and lysozyme. After interaction, the microstructure changed and then flocculent structure was showed. It indicated that the protein-protein interactions would lead to great changes in their structure and aggregation state and produced insoluble complex, which might be related to the viscoelasticity of egg white protein.