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

Effect of high-intensity ultrasound on the physicochemical properties, microstructure, and stability of soy protein isolate-pectin emulsion

“…Compared with the untreated emulsion, the EAI and ESI of the HIU-treated emulsions increased with increasing HIU powers from 0 to 450 W. The emulsion treated at 450 W had the best emulsifying properties, and the EAI and ESI increased by 69.69% and 145.66%, respectively. Wang et al [23] found that HIU treatment could effectively reduce the particle size of the complex and improve the dispersion and solubility of the complex. In addition to modifying proteins and polysaccharides, HIU usually generates powerful micro jets to make the emulsion system more uniform.…”

Effect of high-intensity ultrasonic treatment on the emulsion of hemp seed oil stabilized with hemp seed protein

“…With the increase of HIU power, the particle size and PDI showed a trend of increasing and then decreasing, reaching the minimum at 450 W. At this power, the D43 of the emulsion was 497.66 ± 3.17 nm and the PDI was 0.297 ± 0.042, and the particles in the emulsion had similar sizes and were uniformly distributed. This reduction may be due to cavitation effects, turbulence and strong shear forces generated by HIU treatment, which disrupt some of the larger insoluble protein aggregates and allow HPI to be more uniformly dispersed in the emulsion [29] . The HIU treatment at high power (600 W) showed a slight but significant increase, a phenomenon that occurred probably owing to the re-agglomeration of particles in the emulsion.…”

Plant Protein-Based Delivery Systems: An Emerging Approach for Increasing the Efficacy of Lipophilic Bioactive Compounds

“…The ultrasound treatment (0, 150, 300, 450, and 600 W for 15 min) also enhanced the solubility and dispersibility in the water of the soy protein isolate-pectin complexes. The solubility increased from 46.42% (untreated sample) to 89.88% after sonication at 600 W [ 103 ]. The cavitation generated during sonication can destroy the non-covalent bonds that maintain proteins’ spatial structure, promoting their unfolding and reducing the complex size and, thereby, improving the complex solubility and dispersion in an aqueous solution [ 103 ].…”

“…The solubility increased from 46.42% (untreated sample) to 89.88% after sonication at 600 W [ 103 ]. The cavitation generated during sonication can destroy the non-covalent bonds that maintain proteins’ spatial structure, promoting their unfolding and reducing the complex size and, thereby, improving the complex solubility and dispersion in an aqueous solution [ 103 ]. On the other hand, dry heating at 75 and 100 °C promoted a gradual reduction in the solubility of the bean protein concentrate with increasing temperature [ 104 ].…”