Modification of functional properties of perilla protein isolate by high-intensity ultrasonic treatment and the stability of o/w emulsion

Effects of ultrasonic pretreatment of soybean protein isolate on the binding efficiency, structural changes, and bioavailability of a protein-luteolin nanodelivery system

“…This could promote the structural relaxation and flexibility of protein molecules, enhance the protein-water interaction and protein LUT interaction, and increase the solubility of LUT Ma et al [35] . With increasing ultrasonic pretreatment power, some unfolded SPI self-aggregates through protein–protein molecular interactions (hydrophobic interactions and S-S bonds) to form dimers, trimers or precipitates, resulting in a decrease in molecular flexibility, which affects the solubility and LUT binding ability and results in a decrease in LUT solubility [61] .

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

“…HIU treatment can reduce the particle size, increase solubility and improve the emulsification characteristics of protein. In Zhao et al's study, the solubility, foaming and emulsification of perilla protein isolate (PPI) were improved after ultrasonic treatment [15] . Meanwhile, the interfacial waves and cavitation bubbles generated by the sound field broke up the oil droplets, reducing the emulsion droplet size [16] , [17] .…”

Recent advances in modified food proteins by high intensity ultrasound for enhancing functionality: Potential mechanisms, combination with other methods, equipment innovations and future directions

“…S1 ). Later, Zhao et al [30] found that the FE and FS of perilla protein isolate enhanced with increasing ultrasound power, reaching a maximum of 50% and 30.5% at 750 W, respectively. These studies may provide significant inspiration for the development of HIU induced plant-based ice cream.…”

“…Under the acoustic cavitation effects of HIU, these behaviors are transformed to some extent by each other. For example, the percentage of α-helix of perilla isolated protein enhanced with the increase of ultrasonic power, but the percentage of β-fold, β-turn gradually decreased [30] . This may be attributed to the increased chance of collision between protein molecules under the effects of mechanical vibrations and turbulence generated by the collapse of cavitation bubbles, and the increase in the percentage of α-helix indicates that the protein structure becomes denser under the ultrasonic field.…”

“…This is attributed to the cavitation effect of HIU which improves the surface hydrophobicity and molecular flexibility of protein molecules, enhances the solubility of protein molecules, reduces the particle size of protein particles, and thus improves the absorption ability of proteins in the interface. However, it should be noted that excessive sonication can also reduce foam stability due to protein reaggregation resulting in its desorption from the gas–water interface [30] .…”