Quantitative Comparative Proteomic Analysis of Chicken Egg Vitelline Membrane Proteins during High-temperature Storage.

Zhou, Yu; Qiu, Ning; Mine, Yoshinori; Meng, Yaqi; Keast, Russell; Zhu, Chunxia

To explore the thermally induced alterations in chicken egg vitelline membrane (CEVM) protein abundances, a comparative proteomic analysis of CEVM after 10 days of storage at 30 °C was performed. Altogether, 981 proteins were identified, of which 124 protein abundances were decreased and 79 were increased. Bioinformatic analysis suggested that the altered proteins were related to structure (n = 10), mechanical properties (n = 13), chaperone (n = 15), antibacterial (n = 12), and antioxidant (n = 3). Alterations in abundances of structural proteins, possibly resulting from the disintegration of these complexes, were observed in this study, suggesting a loss in fibrous structure. Several proteins involved in mechanical strength (n = 10), elasticity (n = 3), and chaperone were decreased in abundances, which indicated that deficits in these proteins might affect the CEVM mechanical properties. These findings will extend our understanding of the CEVM deterioration during high-temperature storage from a proteomic perspective.