This study investigated the protective effect of ferulic acid (FA) on the digestibility of oxidized beef myofibrillar protein (MP). MP were treated with varying concentrations of FA (20, 40, and 80 μmol/g pro) and then exposed to oxidation. The results showed that FA inhibited carbonyl in a dose-dependent manner. Fluorescence spectroscopy and molecular docking studies revealed FA was bonded to MP via hydrophobic interactions and hydrogen bonds. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and transmission electron microscope analysis indicated that FA mitigated the aggregation of oxidized MP. Peptidomic analysis showed FA protected 34.24% peptides recover from oxidation loss, and theses recovered peptide were mainly distributed in hydrophobic regions and lysine sites. In vitro digestion showed FA remarkably improved digestibility of oxidized MP (P < 0.05), with 80 μmol/g pro FA mitigating 67.85% loss in digestibility. Overall, FA effectively preserved the release of peptides by inhibiting hydrophobic aggregation and oxidation of lysine residues, thereby alleviating the decrease in digestibility of oxidized MP.