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The effects of rutin (6, 30, and 150 μmol/gpro) 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/gpro 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/gpro, the gels had denser network structures, as observed by scanning electron microscopy. Practical applications: Polyphenols of the type and dosage can change the properties of the product itself and optimize the quality of product processing. Certain polyphenols may promote the oxidation process of protein‐rich products, but this does not affect the improvement of product quality. The application of natural polyphenols is the promising business direction in the development of Coregonus peled industry. [ABSTRACT FROM AUTHOR]