In this study, effects of the synergistic modification of enzymatic hydrolysis and phosphorylation on the functional properties and structural characterization of ovalbumin were studied. Comparison of functional properties of before and after the synergistic modification of ovalbumin, and the structural changes of the synergistic modification ovalbumin were analyzed by FT-IR, DSC and SEM. The results showed that the solubility, gel strength and emulsifying properties of the synergistic modification ovalbumin were higher than both the enzymatic hydrolyzed and unmodified ovalbumin, whereas the foaming and its stability were reduced. Moreover, the enzymatic hydrolysis of the ovalbumin peptide chain caused more amino acid residues to be exposed, therefore the a-helix and β-turns increased accordingly. The synergistic modification of ovalbumin thermal denaturation temperature increased by 7.13 ℃ and 10.19 ℃, respectively, compared with the enzymatic hydrolyzed and unmodified one. In addition, due to the embedding of phosphate groups, collaborative modified molecular structure consisted of a spherical body into a laminated sheet structure.