The effects of rutin (6, 30, and 150 μmol/g_pro) on the physicochemical, structural properties and gel characteristics of myofibrillar protein (MP) under oxidative stress were investigated. The addition of rutin significantly promoted the formation of oxidized MP carbonyl derivatives and dimer tyrosine, but it cannot prevent the loss of sulfhydryl groups (−SH). With increasing rutin concentration, the hydrophobic area was gradually shielded and rutin acted as a quencher to reduce the fluorescence intensity of oxidized MP. Under the oxidative stress, rutin increased the particle size and aggravated the cleavage of protein molecules. SDS-polyacrylamide gel electrophoresis revealed that rutin further aggravated oxidized MP degradation and cross-linked form polymer which cross-linked with protein to the maximum extent at 150 μmol/g_pro rutin content. Moderate cross-linking between protein and rutin could improve the gel strength and water holding capacity (WHC) of oxidized MP gel. For rutin concentrations of 6 and 30 μmol/g_pro, the gels had denser network structures, as observed by scanning electron microscopy.

中文翻译：

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芦丁对氧化应激下肌原纤维蛋白理化及凝胶特性的影响

芦丁（6、30 和 150 μmol/g _pro) 对氧化应激下肌原纤维蛋白 (MP) 的理化、结构特性和凝胶特性进行了研究。芦丁的加入显着促进了氧化 MP 羰基衍生物和二聚体酪氨酸的形成，但不能防止巯基 (-SH) 的丢失。随着芦丁浓度的增加，疏水区逐渐被屏蔽，芦丁作为猝灭剂降低氧化MP的荧光强度。在氧化应激下，芦丁增大了粒径，加剧了蛋白质分子的裂解。SDS-聚丙烯酰胺凝胶电泳显示芦丁进一步加剧氧化MP降解并交联形成聚合物，在150 μmol/g _pro时与蛋白质交联最大程度芦丁含量。蛋白质和芦丁之间的适度交联可以提高氧化 MP 凝胶的凝胶强度和保水能力 (WHC)。对于 6 和 30 μmol/g _{pro 的}芦丁浓度，通过扫描电子显微镜观察，凝胶具有更致密的网络结构。