LAUSR

BACKGROUND In order to study the effects of quercetin on the functionality of myofibrillar proteins (MPs), various levels of quercetin (0, 10, 50, 100 and 200 μmol/g protein) were added to MPs solution and the structure and gel properties of MPs were determined. RESULTS When compared with the control MPs not treated with quercetin, adding 10, 50 and 100 μmol/g quercetin caused a significant (p < 0.05) loss of sulfhydryls; 10 and 50 μmol/g quercetin enhanced the surface hydrophobicity significantly (p < 0.05), and 50, 100 and 200 μmol/g quercetin reduced the fluorescence intensity of tryptophan. The additions of 50, 100 and 200 μmol/g quercetin resulted in a significant (p < 0.05) reduction in MPs solubility. Adding 10, 50 and 100 μmol/g quercetin did not significantly (p > 0.05) change the gel strength and water-holding ability of MPs than control; but 200 μmol/g 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 showed that mildly high levels of quercetin can maintain the gel properties of MPs, which may be due to the moderate MPs cross-linkage and aggregation caused by the covalent and noncovalent interactions of MPs. This article is protected by copyright. All rights reserved.