Enhancing the stability and biological activity of curcumin through incorporating zein-sodium alginate-egg white peptides hybrid assemblies

Abstract

Optimizing biological potency by orchestrating the cooperative assembly of diverse polar functional elements holds significant promise in advancing functional foods. Herein, we meticulously engineered hybrid assemblies by leveraging the inherent architectural domains in zein-sodium alginate (Z-SA) framework, aiming for the cooperative assembly of egg white peptide (EWP) and Curcumin (Cur). Results unveiled a synergistic effect in biological activity and physical stability arising from the cooperative assembly of Cur and EWP. This phenomenon can be attributed to Z-EWP, providing ample structural domains for Cur, thereby enhancing its solubility. Moreover, during the assembly process, EWP preferred interaction with the external environment, sacrificing shielding the more active Cur from oxidative damage. Additionally, the lyophilized Cur-Z-EWP-SA demonstrated excellent re-dispersibility and aqueous solubility, allowing for effective re-solubilization in milk and showcasing exceptional stability throughout storage. Furthermore, the functional milk beverage with Cur-Z-EWP-SA exhibited a discernible in vivo anti-inflammatory activity, effectively mitigating ulcerative colitis.