Phycocyanobilin-modified ?-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating

?-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), bioactive pigment of Arthrospira platensis health-promoting effects, covalently binds to BLG at physiological pH. This study investigated effects this covalent modification on functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects against free radical-induced oxidation. Despite similar thermal stabilities BLG–PCB, less susceptible noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group reduced hydrophobicity due hindering hydrophobic residues by PCB, as well heat-induced transition ?-sheet ?-helix, contributed low susceptibility aggregation. has higher resistance pepsin pancreatin digestion than unaltered IgE-binding improved make it useful ingredient in