2020
DOI: 10.1016/j.bpc.2019.106267
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Response to the “Comments on ‘Statistical thermodynamics of casein aggregation: Effects of salts and water’ [Biophys Chem. 247 (2019) 34–42]”

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Cited by 4 publications
(1 citation statement)
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“…4,32 The product of the redox initiator, SO 4 2− , as a strongly hydrated ion, can reduce the solubility of casein due to the Hofmeister effect: the interaction of macromolecules and ions removes the water of hydration from the protein and folds the protein, prompting casein to form a three-dimensionally (3D) cured structure through hydrophobic association. 33 In particular, casein micelles are composed of many sub-micelles that can be rearranged by applying shear force. Through this rearrangement of submicelles, casein micelles may undergo plastic deformation and thus show high potential for energy dissipation.…”
Section: Introductionmentioning
confidence: 99%
“…4,32 The product of the redox initiator, SO 4 2− , as a strongly hydrated ion, can reduce the solubility of casein due to the Hofmeister effect: the interaction of macromolecules and ions removes the water of hydration from the protein and folds the protein, prompting casein to form a three-dimensionally (3D) cured structure through hydrophobic association. 33 In particular, casein micelles are composed of many sub-micelles that can be rearranged by applying shear force. Through this rearrangement of submicelles, casein micelles may undergo plastic deformation and thus show high potential for energy dissipation.…”
Section: Introductionmentioning
confidence: 99%