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- W4312084014 endingPage "111391" @default.
- W4312084014 startingPage "111391" @default.
- W4312084014 abstract "Levels of native beta-lactoglobulin (β-lg) in heat-treated milk are often used as a measure of quality deterioration. Most kinetic studies to date on β-lg denaturation have been simplified to a single step model, which limits its application in various processing conditions. Furthermore, this denaturation of β-lg is only an initial stage in a series of interactions to take place. In this work, a multistep model for the denaturation of β-lg and its subsequent reaction with κ-casein was developed. This model was used to rationalize the concentrations of native β-lg and κ-casein determined from HPLC. Notably, this model provides a clear account of the influence of β-lg on the loss of micelle-bound κ-casein. The various reaction rates reveal reactions are limited by the rate at which sulfhydryl-disulfide reactions connect proteins while the effect of intermolecular forces is minimal." @default.
- W4312084014 created "2023-01-04" @default.
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- W4312084014 date "2023-05-01" @default.
- W4312084014 modified "2023-09-27" @default.
- W4312084014 title "Modelling the reaction kinetics of β-lactoglobulin and κ-casein heat-induced interactions in skim milk" @default.
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- W4312084014 doi "https://doi.org/10.1016/j.jfoodeng.2022.111391" @default.
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