Interaction between curcumin and ultrafiltered casein micelles or whey protein, and characteristics of their complexes.

This work evaluated the interaction between micellar casein (MC) or whey protein (WP) in ultrafiltration retentate with curcumin (Cur), as well as the physicochemical and functional properties of Cur-MC and Cur-WP complexes. The MC had a higher affinity for Cur than WP, shown by higher binding constants of Cur-MC at various temperatures. Thermodynamic analysis of the binding process indicated that the interaction between Cur and MC or WP was hydrophobic in nature.