Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 68, Issue 20, Pages 5723-5731Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.9b08082
Keywords
ACE inhibitory peptides; egg white peptides; membrane-bound ACE
Funding
- National Natural Science Foundation of China [31972096, 31601486]
- Jilin Scientific and Technological Development Program [20180520045JH]
- Jilin Province and School Co-construction [SF2017-6-4]
- Program for JLU Science and Technology Innovative Research Team [2017TD-29]
- Fundamental Research Funds for the Central Universities
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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.
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