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Construction and Application of Membrane-Bound Angiotensin-I Converting Enzyme System: A New Approach for the Evaluation of Angiotensin-I Converting Enzyme Inhibitory Peptides
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DOI：10.1021/acs.jafc.9b08082.png)
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Abstract
En 中文
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 K-m, and V-max 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
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