Phosphorylation
is a broad post-translational protein modification,
and the level of phosphorylation of milk proteins is associated with
lactation, coagulation properties, and digestibility. However, phosphoproteins
in bovine milk-based and goat milk-based infant formula have not been
systematically explored. Here, we have analyzed six bovine and six
goat milk-based infant formula using a quantitative phosphoproteomics
approach, from which we identified 200 phosphoproteins with 276 phosphorylation
sites and 156 phosphorylation sites from 75 phosphoproteins, respectively.
Of these, 99 phosphorylation sites from 26 shared phosphoproteins
were differentially expressed between bovine and goat milk-based infant
formula. Especially, CSN1S1 was the most phosphoprotein with 25 quantified
phosphorylation sites. Gene Ontology (GO) and Kyoto Encyclopedia of
Genes and Genomes (KEGG) analyses showed that the identified phosphoproteins
not only provide nutrition to the infant but also have anti-inflammatory,
antipathogenic, and other biological functions. Our results shed light
on the composition, phosphorylation sites, and biological functions
of phosphoproteins in bovine milk and goat milk-based infant formula,
which provide new insights into the key role of protein modifications
during infant development. It also helps us to better understand the
differences in digestibility of infant formula from different animal
milk sources and thus guides the choice of milk source for infant
formula.