2023
DOI: 10.1016/j.ultsonch.2023.106457
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Effects of homogeneous and ultrasonic treatment on casein/phosphatidylcholine complex-emulsions: Stability and bioactivity insights

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Cited by 5 publications
(5 citation statements)
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“…The overall trends in all samples were similar. Compared to the initial emulsion, the average particle size increased after the oral digestion stage, indicating that the mucin promoted bridging flocculation of a small number of droplets [19] . After the simulated gastric digestion, the particle size continued to increase because the complex gastric environment dramatically changed the OB structures.…”
Section: Resultsmentioning
confidence: 97%
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“…The overall trends in all samples were similar. Compared to the initial emulsion, the average particle size increased after the oral digestion stage, indicating that the mucin promoted bridging flocculation of a small number of droplets [19] . After the simulated gastric digestion, the particle size continued to increase because the complex gastric environment dramatically changed the OB structures.…”
Section: Resultsmentioning
confidence: 97%
“…It is worth noting that at all digestion stages, the average particle size of the control group was significantly larger than that of the ultrasonically treated OBs, and the 200 W treated OBs had the smallest average particle size. Moreover, an appropriate ultrasonic cavitation can effectively alter protein structure, dissociate the protein subunits, and inhibit the formation of aggregates [19] . The cavitation effect commonly used in food industry induces sonomechanical and sonochemical process, causing unfolding in the native structure of proteins which is desirable for protein functionality, including improving solubility, emulsibility and digestibility [47] .…”
Section: Resultsmentioning
confidence: 99%
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“…2B), indicating that negatively charged groups rather than positively charged groups were present on the protein surface. The zeta potential of treated SPP was gradually decreased with ultrasonic duration increasing, which might be a result of the ultrasound unfolding of the protein structure, exposing more negative charges on the protein surface and increasing the effective charge, 33 thus increasing its stability in solution. However, the SPP solution before and after ultrasound treatment was still a relatively unstable system, even though the size of treated SPP particles was significantly smaller than the control ( P < 0.05).…”
Section: Resultsmentioning
confidence: 99%