Millet protein was used as raw material to prepare food-derived peptides with antioxidant activity and angiotensin transferase(ACE) inhibitory activity. Alkaline protease， neutral protease and flavor protease were used to hydrolyze millet protein. Three components with molecular weight < 3， 3-10 ku and > 10 ku were obtained from the hydrolysate obtained by alkaline protease for 4 h， and their antioxidant and ACE inhibitory activities were determined. The results showed that the polypeptides with molecular weight < 3 ku obtained from the hydrolysate obtained by alkaline protease for 4 h after ultrafiltration had the highest antioxidant activity and ACE inhibitory activity， with DPPH scavenging capacity of 38.44%， ABTS free radical scavenging capacity of 81.62%， hydroxyl radical scavenging capacity of 68.49%. The inhibitory activity of ACE was 87.53%. The polypeptides obtained by this method have low molecular weight， high content of functional amino acids， and have good antioxidant and ACE inhibitory activities， which provide a basic for the development of antioxidant peptides and ACE inhibitory peptides， and provide a theoretical basis for the future industrial development.