Display omitted •Polyphenols were able to covalently bond with glycated myofibrillar protein (MP).•Physicochemical properties of ternary conjugates depended on nature of polyphenols.•Adducted polyphenols altered the conformation characteristics of glycated MP.•MP-dextran (DX)-polyphenol ternary adducts had higher thermal stability.•MP-DX-polyphenol ternary adducts had higher antioxidative capacity. In the present study, three types of polyphenols, namely, (−)-epigallocatechin-3-gallate (EGCG), catechin (C), and gallic acid (GA), were grafted to myofibrillar protein (MP)-dextran (DX) conjugate through a free radical-mediated adduction method. The analysis of secondary structure showed that conjugation of polyphenols induced a decrease in contents of α-helix structures. The surface hydrophobicity of MP-DX conjugate was increased after polyphenols were covalently adducted, while that of the free amino, thiol groups, and tyrosine residues were decreased, especially with the addition of EGCG (p < 0.05). Analysis of rheological properties showed that covalently linking of polyphenols decreased the thermal gelling capacity by inhibiting myosin-head aggregation and myosin tails interaction. Moreover, polyphenol adduction was able to remarkably improve the thermal stability and antioxidant activity of MP-DX conjugate. The findings regarding enhanced functionalities evidence potential of applying the ternary adduct as a novel antioxidant.