Acetes chinensis obtained from Bo Hai Gulf is a valuable protein source. It was digested by protease produced by Bacillus sp. SM98011. The angintensin I-converting enzyme (ACE) inhibitory activity of hydrolysate was investigated. IC50 value of hydrolysate was 0.98mg/ml. IC50 value of the ultrafiltrate of the hydrolysate with MW cut-off 3000 KDa increased up to 0.22 mg/ml. Peptide fractions in the ultrafiltrate was separated with Sephadex G-15 gel chromatography. The most potent fractions were fractionated by reverse-phase high-performance liquid chromatography (HPLC). The three new inhibitory peptides for ACE were purified and sequenced after successive chromatographic isolation. They were Phe-Cys-Val-Leu-Arg-Pro, Ile-Phe-Val-Pro-Ala-Phe and Lys-Pro-Pro-Glu-Thr-Val, with IC50 values of 13.4 礛, 3.2 礛 and 24.1 礛, respectively. The results demonstrate that Acetes chinensis was a promising protein source for the production of ACE inhibitory peptides ,which can be used as materials for antihypertensive functional foods.