Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification

Abstract

The most important factors restricting research and application in the food industry are the poor solubility and emulsification of pea protein isolate (PPI). This study investigates the effect of high-intensity ultrasound (HIU, 0–600 W) and pH-shifting treatment, alone or combined, on the structure, solubility, and emulsification of PPI, as well as its potential mechanism. The results revealed that the PPI solubility significantly increases when treated with the combination, corresponding to a decrease in the protein particle size, especially at 500 W of HIU power (p < 0.05). Correspondingly, the emulsion prepared from it was less prone to phase separation during storage. According to the structural analysis, the structural changes caused by protein unfolding (i.e., the exposure of hydrophobic and polar sites and the loss of the α-helix) seemed to be the primary reasons for increased PPI solubility. In addition, confocal laser scanning microscopy indicated that the combination treatment accelerated the adsorption of PPI at the oil/water interface and strengthened the compactness of the interface film. Improved interfacial properties and intermolecular forces played a critical role in the resistance to droplet coalescence in PPI emulsion. In conclusion, ultrasound and pH-shifting treatments have a synergistic effect on improving the solubility and emulsification of PPI.

Keywords

• Pea protein
• High-intensity ultrasound
• pH-shifting
• Solubility
• Emulsifying