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Arg-Val-Pro-Ser-Leu-Met、Thr-Pro-Ser-Pro-Arg和Asp-Leu-Gln-Gly-Lys,。Antihypertensive peptides were derived from egg white, and then were purified and their primary structure was identified. Egg white hydrolysis process model was established by examining the substrate concentration, E/S, hydrolysis temperature and pH value on the impact of the hydrolysis degree, combined with multivariate linear regression combination of design and quadratic regression orthogonal design. Hydrolysates were purified by gel chromatography, and were characterized by liquid chromatography tandem mass spectrometry. The results showed that the optimal enzymatic hydrolysis process was the substrate concentration of 8%, pH value of 10.73, E/S of 12.14% and temperature of 56.80℃. Hydrolysates were purified by sephadex G-25,the 50% inhibitory concentration as 0.18mg/mL.Liquid chromatography-quadrupole-linear ion trap tandem mass spectrometry confirmed the structure of the active peptides in the component, the amino acid sequences were Arg-Val-Pro-Ser-Leu-Met, Thr-Pro-Ser-Pro-Arg, and Asp-Leu-Gln-Gly-Lys, respectively. 