Quantitative Comparative Integrated Proteomic and Phosphoproteomic Analysis of Chicken Egg Yolk Proteins under Diverse Storage Temperatures

To
investigate the alterations of egg yolk protein abundances and
their phosphorylation status at different storage temperatures, a
comparative quantitative study of unfertilized chicken egg yolk after
15 days of storage at 4 and 37 °C was performed. Altogether,
445 proteins were identified in our study, of which the abundances
of 154 proteins were significantly changed when comparing high-temperature
storage with low-temperature storage, including 42 up-regulated and
112 down-regulated proteins. In the phosphoproteome, we identified
a total of 137 phosphorylated sites on 326 peptides corresponding
to 51 proteins. The results showed that the degree of phosphorylation
for most egg yolk proteins was enhanced during high-temperature storage.
Furthermore, GO analysis indicated that these phosphoproteins of egg
yolk may be closely related to the binding, catalysis, and transport
functions. The results provide further insights into the effect of
storage temperature on egg proteome changes and their phosphorylation
level. Moreover, this study can provide a theoretical basis for the
improvement of egg quality during storage by phosphorylation modification
in the food industry.