Abstract
This study aimed to modify egg white protein particles (EPs) through pH-shifting combined with preheating. EPs were subjected to pH treatment (3, 7, 8, and 10) for 1 h with preheating (75 °C for 30 min) and then adjusted to neutral. The thermal stability of the EPs was measured by heating them at 90 °C for 15 min. Particle size distribution revealed that the EPs modified by preheating at pH 10 (EPs10) performed the smallest particle size among all samples, which decreased the aggregation extent of the particles under heat stress. The total sulfhydryl contents of EPs10 did not significantly decrease under heat stress, indicating that intramolecular disulfide bonds were formed and prevented covalent interactions between particles. Solubility and turbidity measurements indicated that EPs10 retained the best physicochemical properties under heat stress among all samples. In terms of emulsification, EPs10 had a higher elastic interfacial protein layer than EPs3 and native egg white protein because of the exposure of hydrophobic and surface free –SH groups. The emulsions of EPs10 showed the best thermal stability among all samples. This research provided a theological basis for heat-stable egg white protein particles and a practical method for the industry to process EWP-based emulsifiers.
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