Abstract: In order to study the effects of ferulic acid (FA) on ·OH-induced oxidation and gel properties of myofibrillar proteins (MPs), porcine MPs was used as the research object and a new system of MPs-Fenton oxidation was established by using Fenton oxidation system to simulate the actual meat oxidation environment. The effects of different concentrations of FA (0, 0.01, 0.25, 0.50 mg/g protein) on the oxidation and gel properties of MPs were studied. The results showed that the contents of carbonyl were reduced significantly (P<0.05) by the addition of FA, and the inhibition effect of FA was concentration-dependent. The inhibitory rate of high concentration of FA (0.50 mg/g) on the content of carbonyl was up to 38.2%. High concentration of FA (0.50 mg/g) further promoted the loss of sulfhydryl group of MPs, and the content of total sulfhydryl group of MPs was significantly reduced by 4.02% (P<0.01) after oxidation for 12 hours by ·OH. The solubility of MPs decreased after oxidation and became more obvious with the increase of FA concentration, indicating that the addition of FA could promote the further unfolding of the protein structure and play a mediating role in regulating the oxidation state of MPs. The gel strength of MPs was significantly reduced after oxidation (P<0.05), and the gel elasticity was enhanced, the elasticity was the strongest with the addition of the 0.01 mg/g FA , and then decreased with the increase of FA concentration. The addition of high concentration FA could increase the cooking loss, water loss and the poor water holding capacity of MPs gel, and the structure of MPs was changed by oxidation, which formed a weakly gel network structure. FA with an appropriate amount could inhibit the oxidation of MPs and improve the gel quality, as well as high concentration of FA could weaken the gelation ability and gel quality of MPs.