Objective： Isolation and identification of antioxidant peptide with high ABTS+· scavenging capacity from tryptic hydrolysate of Ovalipes punctatus waste containing meat scraps. Method： Antioxidant peptides in the hydrolysates were purified using ultrafiltration membrane system， Sephadex G-15 column and semi-preparative reversed-phase high-performance liquid chromatography （semi-preparative RP-HPLC）. Their peptide sequences were identified by ultra-performance liquid chromatography/electrospray ionization time-of-flight tandem mass spectrometry（UPLC-ESI-TOF/MS/MS）. Their structure and ABTS+· scavenging capacity were further verified by the synthetic peptides. Results： Two peptides with high ABTS+· scavenging capacity were purified from hydrolysates， and their peptide sequences were Tyr-Glu-Gly （YEG） and Tyr-Glu（YE）， respectively. The molecular weight of synthetic peptides was 367.35 u and 310.30 u， and their purity was 98.52% and 98.04%， respectively. The synthetic peptides YEG and YE have good ABTS+· scavenging capacity， with IC50 values of 0.456 mg/mL and 0.184 mg/mL， respectively. Furthermore， IC50 value of synthetic peptide YE was 30.30% higher than that of reduced L-glutathione. Conclusion： Antioxidant peptides were existed in the tryptic hydrolysate of Ovalipes punctatus waste containing meat scraps， which provides a theoretical basis for development of antioxidant peptides from Ovalipes punctatus by-products.