Comprehensive analysis of Pigeon egg proteins: Composition, function, and health significance

Abstract

Pigeon eggs have been used as a valuable source of high-quality proteins, which play a crucial role to regulate metabolism, immunity, and other physiological functions in humans. However, the specific composition and function of pigeon egg proteins remain underexplored. In this study, a comprehensive into the common proteome and modified proteins (phosphorylated proteins and N-glycosylated proteins) of whole pigeon eggs was carried out using proteomics. The results showed that a total of 189 proteins were identified, including 27 phosphorylated proteins (containing 90 phosphorylation modification sites) and 73 N-glycosylated proteins (containing 203 N-glycosylation modification sites). Motif analysis indicated that serine (Ser) accounted for 72.6% of the phosphorylation events, while the sequence "N-X-T" emerged as the predominant motif for N-glycosylation, representing 58.7% of such modifications. Functional enrichment analysis further demonstrated that the majority of pigeon egg proteins, modified proteins were involved in binding and catalytic activities and contributed to enzyme activity regulation and inhibition. Pigeon egg proteins were predominantly associated with the lysosomal pathway, as outlined in the KEGG database. This study could pave the way for the development of innovative food products and nutritional interventions based on pigeon egg proteins.