Modification of rapeseed protein by ultrasound-assisted pH shift treatment: Ultrasonic mode and frequency screening, changes in protein solubility and structural characteristics

Improving the Solubility and Digestibility of Potato Protein with an Online Ultrasound-Assisted PH Shifting Treatment at Medium Temperature

“…However, extending the ultrasonication time might result in refolding of the potato protein and decrease its solubility. Our results were consistent with other studies showing that a higher input energy led to the formation of aggregates and loss of solubility [24,25].…”

Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

“…With increasing treatment power, a considerable amount of heat was generated, thereby promoting SPI aggregation. Therefore, the selection of appropriate HIU treatment conditions can effectively improve the particle size of the SPI-PC complex [41] .…”

Ultrasonic pre-treatment modifies the pH-dependent molecular interactions between β-lactoglobulin and dietary phenolics: Conformational structures and interfacial properties

“…Ultrasound treatment uniquely affected the emission spectra of β-LG ( Supplementary Fig. S1 ): taking ULG-35 as an example, at neutral pH, sonication increased the fluorescent intensity of β-LG ascribed to protein conformational rearrangement and exposure of burried hydrophobic domains [17] ; while at acidic pH, the fluorescence intensity was slightly decreased, which could be due to the intermolecular aggregation induced by a combined effect of extreme pH and ultrasonic actions [14] . Albeit in different degrees, the presence of EGCG/CA quenched the fluorescence intensity of β-LG in a dose-dependent manner, indicating that the interactions with two phenolics influenced the protein fluorophore.…”