Antioxidant and angiotensin-I converting enzyme inhibitory (ACE-I) activities of bioactive peptide fractions from camel milk fermented by Leuconostoc lactis PTCC 1899 were assessed. The fraction <3 kDa obtained from ultrafiltration showed ACE-I (IC₅₀ = 1.61 ± 0.18 mg mL⁻¹) and ABTS radical scavenging (1883.39 μm TE mg⁻¹ protein) activities and was purified through RP-HPLC. The active peptide, MVPYPQR, with antioxidant (8933.05 μm TE mg⁻¹ peptide) and ACE-I (IC₅₀ = 30 μm) activities was identified. To investigate the ACE-I mechanism of the purified peptide the docking study was performed. The presence of hydrogen bond between Gln 162 (S'1 pocket of ACE) and Arg in the C terminal of the peptide was identified and the peptide could distort the Zn²⁺ tetrahedral geometry of the enzyme. This study showed the ability of Leuc. lactis to produce a novel and safe functional food by hydrolysing the milk proteins during the fermentation.