The effect of the plasma membrane on the activity of angiotensin-I converting enzyme (ACE) plays a crucial role in the evaluation of food-derived ACE inhibitory peptides, although these peptides are commonly evaluated in the system with ACE in its free state. In this study, we constructed an in vitro membrane-bound ACE C domain system to simulate the presence of the plasma membrane. The resultant Km and Vmax suggested that the presence of the membrane reduced the affinity between ACE C domain and hippuryl-histidyl-leucine, while it increased the reaction velocity. The ACE inhibitory activity of four egg white peptides and five structurally modified peptides suggested that a moderate hydrophobicity/hydrophilicity of the peptide is beneficial for the improvement of their ACE inhibitory activity in a membrane-bound system. These results also indicated that the N terminal plays a significant role in the ACE inhibitory activity of peptides in the membrane-bound system.
Keywords: ACE inhibitory peptides; egg white peptides; membrane-bound ACE.