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

Abstract

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. Cur promoted the size and polydispersity index of MC and WP at 4mM but did not alter the morphology of spray-dried MC and WP. The Cur-MC complexes showed better aqueous solubility at pH 2-3 and 6-10 compared to free MC. Combination with MC or WP improved the 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) radical scavenging activity of Cur. In addition, combination with MC and WP promoted cumulative release of Cur during simulated gastrointestinal digestion, especially for WP. Thus, MC and WP in retentates can be good alternative protein-based carriers for Cur delivery, whereas their complexes in powder form have good functional properties that could be used as active food ingredients in several food formulations. PRACTICAL APPLICATION: Microfiltration is a cheap and convenient approach that can be used to easily produce micellar casein (MC), with whey protein (WP) as one byproduct. In this study, we proved that MC and WP in retentates have strong interaction with curcumin (Cur), whereas their complexes have good functional properties. Thus, spray-dried MC-Cur or WP-Cur complexes could be used as active food ingredients in several food formulations.