Underlying mechanisms of egg white thinning in hot spring eggs during storage: Weak gel properties and quantitative proteome analysis

Abstract

As a weakly gelling protein, hot spring egg white underwent thinning during storage. This study explored the mechanism of thinning in hot spring egg white from the perspective of "gel structure and protein composition" using quantitative proteomics, SEM, SDS-PAGE, and other techniques. Quantitative proteomics analysis showed that there were 81 (44 up-regulated and 21 down-regulated) key proteins related to thinning of hot spring egg white. The changes in the relative abundance of proteins such as ovalbumin-related Y, mucin-6, lysozyme, ovomucoid, and ovotransferrin might be important reasons for thinning in hot spring egg white. SEM results indicated that the gel network gradually became regular and uniform, with large pores appearing on the cross-section and being pierced. Along with the decrease in intermolecular electrostatic repulsion, protein molecules gradually aggregated. The particle size gradually increased from 139.1 nm to 422.5 nm. Meanwhile, the surface hydrophobicity, and disulfide bond content gradually increased. These changes might be the reasons for thinning in hot spring egg white during storage. It can provide a new perspective for studying the thinning mechanism of weakly gelling egg whites.

Keywords: Egg white thinning; Hot spring egg; Label-free proteomics; Molecular interactions; Thermal gel properties.