2021
DOI: 10.1016/j.ultsonch.2021.105756
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Emulsion gels stabilized by soybean protein isolate and pectin: Effects of high intensity ultrasound on the gel properties, stability and β-carotene digestive characteristics

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Cited by 101 publications
(46 citation statements)
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“…The trends of T 22 were similar to that of T 23 . Yang, Zhou, Guo, Feng, Wang, Wang, Ma, and Sun [ 23 ] reported that shorter relaxation times were conducive to the combination between water and proteins, so the lowest T 22 in L. casei -G reflected that more free water was retained in the gel structure caused by the binding of water to SPI promoted by EPS. It is worth noting that the A 22 value was highest, but the A 23 value was the lowest when the fermentation strain was L. casei .…”
Section: Resultsmentioning
confidence: 99%
“…The trends of T 22 were similar to that of T 23 . Yang, Zhou, Guo, Feng, Wang, Wang, Ma, and Sun [ 23 ] reported that shorter relaxation times were conducive to the combination between water and proteins, so the lowest T 22 in L. casei -G reflected that more free water was retained in the gel structure caused by the binding of water to SPI promoted by EPS. It is worth noting that the A 22 value was highest, but the A 23 value was the lowest when the fermentation strain was L. casei .…”
Section: Resultsmentioning
confidence: 99%
“…At present, HIU is successfully applied to improve the emulsification, foaming, viscosity and gelation characteristics of proteins. For instance, a better emulsifying property of soybean protein, walnut protein and myofibrillar protein was obtained after HIU treatment [10] , [13] , [15] . The foaming ability of whey protein and the gelation property of soybean protein were enhanced by HIU treated [16] .…”
Section: Introductionmentioning
confidence: 99%
“…The extents of protein digestion in the gastrointestinal tract depends on the contents of Phe, Tyr, Trp, Lys, and Arg, the target cleavage sites of pepsin or trypsin, which was affected by the exposure of amino acids in protein side chain through protein unfolding and aggregation during UHP treatment. Ultrahigh pressure would break the chemical bonds and forces like hydrogen bonds, disulfide bonds, hydrophobicity, and Van der Waals forces as forementioned ( 37 ). The results were consistent with particle size, surface hydrophobicity, and solubility ( 38 ).…”
Section: Resultsmentioning
confidence: 99%