Ovomucin may be the key protein involved in the early formation of egg-white thermal gel.

Clarification of the mechanism of heat-induced gel formation by proteins under natural food systems could provide important references for the regulation of food texture. In the present study, the proteins involved in the early stage (heating at 72 °C for 8 min) of egg-white thermal gel (EWG) formation were studied quantitatively through comparative proteomic analysis. We discovered that the abundance of ovalbumin and ovomucoid increased significantly (p < 0.01), whereas that of ovotransferrin, lysozyme, ovomucin (mucin 5B and mucin 6) decreased significantly (p < 0.01), in the supernatant of EWG. If the initial interaction of egg white proteins was altered by ultrasonic pretreatment, the abundance of ovomucin and lysozyme in the supernatant of EWG increased, and was accompanied by the change from a solid gel to a fluid gel. Based on these results, we hypothesize that ovomucin has a key role in the formation and regulation of EWG properties.