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• W2053132153 startingPage "1880" @default.
• W2053132153 abstract "Bixin is the major coloring component of annatto used in manufacturing colored cheeses, but its presence in liquid whey causes undesirable quality of the recovered whey protein ingredients. The objective of this work was to study molecular binding between bixin and three major whey proteins (β-lactoglobulin, α-lactalbumin, and bovine serum albumin) at pH 7.4 using UV–vis absorption spectroscopy, fluorescence spectroscopy, isothermal titration calorimetry, and circular dichroism. These complementary techniques illustrated that the binding is a spontaneous complexation process mainly driven by hydrophobic interactions. The complexation is favored at a lower temperature and a higher ionic strength. At a lower temperature, the binding is entropy-driven, while it changes to an enthalpy-driven process at higher temperatures. The binding also increases the percentage of unordered secondary structures of proteins. Findings from this work can be used to develop whey protein recovery processes for minimizing residual annatto content in whey protein ingredients." @default.
• W2053132153 created "2016-06-24" @default.
• W2053132153 creator A5010776860 @default.
• W2053132153 creator A5058315872 @default.
• W2053132153 date "2012-02-08" @default.
• W2053132153 modified "2023-09-27" @default.
• W2053132153 title "Binding between Bixin and Whey Protein at pH 7.4 Studied by Spectroscopy and Isothermal Titration Calorimetry" @default.
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• W2053132153 doi "https://doi.org/10.1021/jf2050262" @default.
• W2053132153 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22268806" @default.
• W2053132153 hasPublicationYear "2012" @default.
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