Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study

► We studied the binding of curcumin, a bioactive hydrophobic molecule, with casein micelles. ► Heating increases the binding of curcumin with the micelles. ► Heat induced aggregates affect the number of binding sites, but with low affinity, and less specificity. ► Curcumin penetrates the inner core of the casein micelles as shown by fluorescence quenching.