Research note: Proteomics profiling reveal key proteins in egg white emulsification

Egg white proteins are widely recognized as excellent natural emulsifiers, yet the molecular mechanisms underlying their emulsification properties remain incompletely understood, particularly regarding the roles of individual proteins in complex natural systems. Using 4D-label-free quantitative proteomics, we systematically investigated protein dynamics during egg white emulsification by comparing egg white (EW) and the aqueous phases of egg white emulsions (EWE-W). Proteomic analysis identified 96 distinct proteins, with 64 showing significant abundance changes during emulsification. Among them, lysozyme, ovomucin and Protein TENP were heavily involved in the formation of the oil-water interface during the emulsification process, leading to a significant decrease in their abundance in EWE-W. In particular, Protein TENP showed the most significant reduction in abundance among all differential proteins. These findings provide new insights for optimizing egg white functionality in food applications and understanding protein-based emulsion systems.