Effect of ultrasound and coagulant types on properties of β-carotene bulk emulsion gels stabilized by soy protein

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

“…Therefore, the protein structure of SPI under high-power treatment was not suitable for combination with LUT. The high ultrasonic pretreatment power might also initiate fractional denaturation and microstructural changes (e.g., occurrence of aggregation or dissociation and/or reassociation) of proteins, which might increase the degree of aggregation and decrease the hydrophobicity to protect the hydrophobic regions of the proteins (Li et al, 2020), [18] . These structural changes were detrimental for the embedding of LUT into the proteins.…”

Comparison of soy protein isolate-(–)-epigallocatechin gallate complexes prepared by mixing, chemical polymerization, and ultrasound treatment

“…1 b-c). The cavitation and mechanical effects of ultrasound unfolded the internal structure and reduced the SPI consistency index [40] , [41] ; therefore, reducing the aggregation of SPI and improving the stability of the SPI-EGCG complexes. Meanwhile, the hydroxyl radicals (H 2 O → H·+OH·) generated by ultrasound reacted with SPI to generate more protein radical binding sites, which promoted the covalent binding of SPI with EGCG.…”

Preparation and Characterization of a Novel Soy Protein Isolate-Sugar Beet Pectin Emulsion Gel and Its Application as a Multi-Phased Nutrient Carrier

“…After simulated gastric digestion, these oil droplets were released partly into the SGF from the gel network. The part of β-carotene which was measured was in the free oil droplets, but those oil droplets did not undergo continued digestion in SSF and SGF [39]. As shown in Figure 6B, during P1, there was no significant release of β-carotene, as observed in all samples.…”