In order to investigate the hypotensive function of bioactive peptides in Jinhua dry-cured ham， the bioactive peptide components were extracted from Jinhua dry-cured ham， and the bioactive peptides with angiotensin-converting enzyme (ACE) modulating function were identified by isolation and purification. The results showed that after separation by Sephadex G-25 molecular exclusion chromatography， the bioactive peptides of Jinhua dry-cured ham could be divided into four fractions， A， B， C and D. Among them， the ACE inhibitory activity of fraction C was the strongest， reaching 31.8%. After fraction C separation by ion exchange column， the Jinhua dry-cured ham peptides could be divided into four fractions， C1， C2， C3 and C4， among which the ACE inhibitory activity of fraction C2 was significantly higher than other fractions， with an activity as high as 49.0% (P < 0.05). Eight peptides were identified in C2 by Nano-LC-ESI-MS/MS， and the sequence IESDLERAEE had the highest activity with an ACE inhibitory activity of 59.1%. Conclusion: Peptides derived from Jinhua dry-cured have had good effect of regulating ACE activity in vitro， which lay the foundation for further research on its blood pressure regulation function in vivo.