2022
DOI: 10.1016/j.ultsonch.2022.106089
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Modifying the physicochemical properties, solubility and foaming capacity of milk proteins by ultrasound-assisted alkaline pH-shifting treatment

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Cited by 56 publications
(14 citation statements)
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“…This phenomenon implied that the hydrophobic amino acid residues originally buried inside the protein molecule might be exposed to the molecular surface under the effect of ultrasound, which also suggested that the amino acid residue arrangement of the ultrasound-treated protein was strongly affected. Similar results have been previously observed in other researchers’ studies [ 26 ]. In this study, the ultrasound resulted in stronger intramolecular electrostatic repulsion as well as protein unfolding, thereby exposing hydrophobic amino acids.…”
Section: Resultssupporting
confidence: 93%
“…This phenomenon implied that the hydrophobic amino acid residues originally buried inside the protein molecule might be exposed to the molecular surface under the effect of ultrasound, which also suggested that the amino acid residue arrangement of the ultrasound-treated protein was strongly affected. Similar results have been previously observed in other researchers’ studies [ 26 ]. In this study, the ultrasound resulted in stronger intramolecular electrostatic repulsion as well as protein unfolding, thereby exposing hydrophobic amino acids.…”
Section: Resultssupporting
confidence: 93%
“…The synergistic effects of pH shift and ultrasound on solubility were also revealed in other plant or animal-based proteins. For instance, the solubility of milk casein concentrate was significantly increased from 59.02 % (control) to 99.05 % after ultrasound-assisted pH 12 treatment [47] . Meanwhile, the solubility of pea protein isolates increased from 8.17 % (control) to 57.28 % after ultrasound-assisted pH 10 treatment, while the value was only 9.80 % after a single pH 10 treatment [36] .…”
Section: Resultsmentioning
confidence: 97%
“…According to a previous method reported by Zhao and Laemmli (Laemmli, 1970; Zhao et al ., 2022), SDS‐PAGE was performed on standard electrophoresis apparatus (Bio‐Rad, California, USA). Samples (5 mg·mL −1 ) were diluted with a reducing buffer containing the 1% β‐mercaptoethanol in a 1:1 volume ratio.…”
Section: Methodsmentioning
confidence: 99%