LAUSR

Assembling between polyphenols and proteins has been recently spotlighted and this binding is of specific importance in food chemistry since these complexes are typically used in different foodstuffs. A study on the copigmentation among three encapsulation wall-materials, including maltodextrin, gum Arabic, and whey proteins, with mulberry anthocyanins (AC) proved that whey protein (WP) is an outstanding wall-material due to its wrapping and hyperchromicity effects. Additionally, high binding ability of WP with AC was shown to be responsible for its superior copigmentation effects. Accordingly, the underlying shielding mechanism of WP on AC based on their non-covalent assembling was deeply studied using multispectral and computational assays. The fluorometric results demonstrated that a static and heat-stable binding between WP and AC occurred, leading to modification in size, hydrophobicity, and secondary structures of WP. The docking results explained that WP-AC complex was mainly molded via hydrophobic effects of WP surface and subsequently be stabilized by H-bonding and van der Waals forces. These results may contribute to a better understanding on the enhanced colouring proprieties of anthocyanins by using whey proteins.