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Xu, Yujuan; Han, Minyi; Huang, Mingyuan; Xu, Xinglian
Food chemistry, 08/2021, Volume: 352Journal Article
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.
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