Anti-glycation and anti-hardening effects of microencapsulated mulberry polyphenols in high-protein-sugar ball models through binding with some glycation sites of whey proteins.

Assembling between polyphenols and proteins has been freshly spotlighted. We studied the antiglycation and anti-hardening effects of microencapsulated mulberry polyphenols (MMPs) in a high-protein-sugar ball (HPSB) model during storage using multi-dimensional approaches, including UPLC-ESI-MS/MS, SDS-PAGE, MALDI-TOF-MS, FTIR, and a molecular docking study. It was found that MMPs significantly relegated the browning development, AGEs, and/or CML levels of HPSB after 45 d of storage at 45 °C. MMPs also downgraded the protein insolubility, aggregation, oligomerization, and glycoxidation during late-storage. A molecular docking scrutiny proved that cyanidin 3-O-rutinoside and quercetin 3-O-rutinoside interacted with whey proteins subunits via H-bonding and π-π interactions. This binding blocked some glycation residues of whey proteins especially lysyl residues, namely Lys5, 16, 60, 69, 93, 94, and 122. Our data disclosed that MMPs could be valorized as promising antiglycative ingredients to mitigate AGEs-generation and other subsequent unwanted changes in protein-rich food matrices.