Quantitative phosphoproteome analysis reveals differential whey phosphoproteins of bovine milk during lactation.

Whey proteins in bovine milk, as the most widely used nutritional components for infant formulae, have been paid more attention. However, the phosphorylation of proteins in bovine whey during lactation has not been thoroughly researched. In this study, a total of 185 phosphorylation sites on 72 phosphoproteins were identified in bovine whey during lactation. 45 differentially expressed whey phosphoproteins (DEWPPs) in colostrum and mature milk were focused on by bioinformatics approaches. Gene Ontology annotation indicated that blood coagulation, extractive space, and protein binding played a key role in bovine milk. The critical pathway of DEWPPs was related to the immune system according to KEGG analysis. Our study investigated the biological functions of whey proteins from a phosphorylation perspective for the first time. The results elucidate and increase our knowledge of differentially phosphorylation sites and phosphoproteins in bovine whey during lactation. Additionally, the data might offer fresh insight into the development of whey protein nutrition.