BACKGROUND: To study the effects of quercetin on the functionality of myofibrillar proteins (MPs), various levels of quercetin (0, 10, 50, 100 and 200 ∼mol g −1 protein) were added to MP solution and the structure and gel properties of MPs were determined.RESULTS: Compared with the control MPs not treated with quercetin, adding 10, 50 and 100 ∼mol g −1 quercetin caused a significant (P < 0.05) loss of sulfhydryls; 10 and 50 ∼mol g −1 quercetin enhanced the surface hydrophobicity significantly (P < 0.05), and 50, 100 and 200 ∼mol g −1 quercetin reduced the fluorescence intensity of tryptophan. Additions of 50, 100 and 200 ∼mol g −1 quercetin resulted in a significant (P < 0.05) reduction in MP solubility. Adding 10, 50 and 100 ∼mol g −1 quercetin did not significantly (P > 0.05) change the gel strength and water-holding ability of MPs than control, but 200 ∼mol g −1 quercetin declined the gel properties significantly (P < 0.05). The microstructure and dynamic rheological properties confirmed the results of the gel properties of MPs affected by various levels of quercetin. CONCLUSION:The results obtained in the present study show that mildly high levels of quercetin can maintain the gel properties of MPs, which may be a result of the moderate MP cross-linkage and aggregation caused by the covalent and non-covalent interactions of MPs.