2021
DOI: 10.1016/j.lwt.2021.110881
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Effects of flexibility and surface hydrophobicity on emulsifying properties: Ultrasound-treated soybean protein isolate

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Cited by 159 publications
(127 citation statements)
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“…However, the protein conformation was changed and protein aggregated again after long-term ultrasonic treatment, resulting in the decrease of α - helix content and irregular coil structure. Similarly, Yan et al confirmed that with increases in the ultrasound time, the protein was partially denatured and re-polymerized through hydrophobic binding and other effects, resulting in the change of secondary structure [52] .…”
Section: Resultsmentioning
confidence: 87%
See 1 more Smart Citation
“…However, the protein conformation was changed and protein aggregated again after long-term ultrasonic treatment, resulting in the decrease of α - helix content and irregular coil structure. Similarly, Yan et al confirmed that with increases in the ultrasound time, the protein was partially denatured and re-polymerized through hydrophobic binding and other effects, resulting in the change of secondary structure [52] .…”
Section: Resultsmentioning
confidence: 87%
“…1 ). According to Yan et al, the shear force produced by ultrasound reduced the particle size of protein and increased the specific surface area of protein, which enhanced the stability of protein solution [33] . Furthermore, the non-covalent bonds which maintained the stability of protein spatial structure was destroyed by cavitation force caused by ultrasonic [34] .…”
Section: Resultsmentioning
confidence: 99%
“…Thus, the increasing interaction between protein and water was beneficial to the solubility [40] . Nevertheless, if the ultrasonic field intensity is unduly strong, the denaturation and aggregation of protein occur, and the solubility decreases [9] , [41] .…”
Section: Resultsmentioning
confidence: 99%
“…Turbidity, the hindered degree of suspended solids to light transmission, represents the aggregation degree of protein in raw soymilk [41] . In Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Surface hydrophobicity (H 0 ) is closely related to the emulsifying properties, stability, and function of the complex/particles [ 41 ], and a balanced surface hydrophobicity has a beneficial effect on surface activity and interfacial performance in emulsions. The surface hydrophobicity of the complexes is shown in Figure 5 .…”
Section: Resultsmentioning
confidence: 99%