Phosphoproteomic analysis of duck egg white and insight into the biological functions of identified phosphoproteins.

Phosphorylation of proteins is one of the most important and pleiotropic modifications. It plays a vital role in controlling protein functions. However, the phosphoproteome of duck egg white (DEW) has not been studied yet. To investigate the role of phosphorylation on DEW proteins, a detailed phosphoproteome analysis of DEW was performed using an immobilized metal affinity chromatography enrichment strategy. A total of 92 phosphosites representing 36 phosphoproteins were identified. [S-x-E] and [T-x-E] were found to be the most overrepresented motifs in DEW. The identified phosphoproteins in DEW were mainly involved in the binding, transport activity, biological regulation, and metabolic processes. Gene ontology analysis was used to elucidate the biological functions of DEW phosphoproteins and compare them with those of chicken egg white (CEW), which showed the differences mostly involved molecular functions and biological processes. PRACTICAL APPLICATIONS: These findings provide fundamental insight into the biological functions of identified phosphoproteins of DEW to better understand the roles of phosphorylated DEW proteins for food industries and human health. Phosphoproteomic study of DEW would be valuable for the food and nutrition industry to exploit the potential of this avian proteins in the processing of health benefit products.