Antioxidant peptides were prepared from Perilla meal protein by hydrolysis with Alcalase， and were enriched by ultrafiltration centrifugation， gel filtration chromatography and reverse phase chromatography. The results showed that compared with the other three proteases， the hydrolysis degree of alcalase to perilla meal protein was the highest， about (25.94±0.21)%. The hydrolysate of perilla meal protein treated by alcalase had the best antioxidant activity， and the scavenging rate of DPPH free radical was about (91.01±0.73)%. The smallest molecular weight component F1 (less than 3 ku) of hydrolysate supernatant separated by ultrafiltration and centrifugation had the strongest antioxidant activity. The F1 component was separated by Sephadex G-25 gel filtration chromatography to obtain three components P1， P2 and P3 in order of molecular weight， among which P3 component with the smallest molecular weight had the highest antioxidant activity. Among the four components of P3 separated by reversed-phase chromatography， P3-4 eluting was the most hydrophobic and had the highest DPPH· scavenging capacity， and the DPPH· scavenging rate of P3-4 with concentration of 3 μg/mL was(58.8±0.78)%. By LC-MS-MS identification， the antioxidant peptide in component P3-4 was confirmed as a dodeceptide， whose amino acid sequence was Lys-Leu-Lys-Asp-Ser-Phe-Glu-Arg-Gln-GlY-Met-Val， and the molecular weight was 1 437.8 u. The results of this study provide a theoretical reference for further development of Perilla protein resources and research of Perilla antioxidant peptides.