Abstract In this study, the effects of phosphorylated ovalbumin (PP-OVA) on heat-induced aggregation of native ovalbumin (N-OVA) were investigated. Results showed that PP-OVA effectively suppressed N-OVA aggregation, and the inhibited ability is little weakened when the ionic strength ranged from 10 to 100 mmol/L. Dynamic light scattering analysis showed that the size of the formed N-OVA aggregates decreased in the presence of PP-OVA. Transmission electron micrographs further showed that the N-OVA/PP-OVA mixture exhibited a more uniform size distribution than N-OVA alone. After heat treatment solution of N-OVA, the ζ-potential increased with PP-OVA increased, suggesting that the system became more stable. The result of native-PAGE suggested that the N-OVA/PP-OVA aggregates possess a well-solubility and homogeneity. These results indicate that PP-OVA exhibits a chaperone-like activity under heating, and provide an insight into the possible mechanism through which PP-OVA stabilizes proteins to resist heat-induced N-OVA aggregation.