Abstract
The consumption of supplements based on dairy or plant proteins may be associated with bioactive potential, including angiotensin-1-converting enzyme inhibitory (ACE-1i) activity, which is linked with blood pressure reduction in vivo. To gain insight into this proposed mechanism, the ACE-1i potential of protein-based supplements, including a selection of dairy (n = 10) and plant (n = 5) proteins were in vitro digested. The total digest was filtered and permeate and retentate were obtained. ACE-1i activity was measured as the ability of proteins (pre-digestion, ‘gastric’, permeate, and retentate) to decrease the hydrolysis of furanacroloyl-Phe-Glu-Glu (FAPGG) substrate for the ACE-1 enzyme. Permeate and retentate of dairy proteins exerted a significantly higher ACE-1i activity (mean of 10 proteins: 27.05 ± 0.2% and 20.7 ± 0.2%, respectively) compared with pre-digestion dairy proteins (16.7 ± 0.3%). Plant protein exhibited high ACE-1i in ‘gastric’ and retentate fractions (mean of five proteins: 54.9 ± 0.6% and 35.7 ± 0.6%, respectively). The comparison of the in vitro ACE-1i activity of dairy and plant proteins could provide valuable knowledge regarding their specific bioactivities, which could inform their use in the formulation of specific functional supplements that would require testing for blood pressure control in human randomly-controlled studies.
Highlights
Peptides derived from animal and plant proteins represent sources of potential health-promoting compounds and activities, such as angiotensin-I-converting enzyme inhibitory activity (ACE-1i) [1,2].The mechanism of action of ACE-1 inhibition is not completely understood, but several studies have demonstrated that the inhibition of ACE can affect various regulatory systems of the body, such as the modulation of blood pressure (BP), the immune system, and central nervous system [3].ACE-1 is a multifunctional enzyme that is localized in various tissues and associated with the renin-angiotensin system that controls BP
All plant protein samples exhibited the highest ACE-1i in the ‘gastric’
The final hydrolysate obtained represented aa pool of those generated during the physiological digestion of proteins in humans
Summary
Peptides derived from animal and plant proteins represent sources of potential health-promoting compounds and activities, such as angiotensin-I-converting enzyme inhibitory activity (ACE-1i) [1,2].The mechanism of action of ACE-1 inhibition is not completely understood, but several studies have demonstrated that the inhibition of ACE can affect various regulatory systems of the body, such as the modulation of blood pressure (BP), the immune system, and central nervous system [3].ACE-1 is a multifunctional enzyme that is localized in various tissues and associated with the renin-angiotensin system that controls BP. Peptides derived from animal and plant proteins represent sources of potential health-promoting compounds and activities, such as angiotensin-I-converting enzyme inhibitory activity (ACE-1i) [1,2]. The mechanism of action of ACE-1 inhibition is not completely understood, but several studies have demonstrated that the inhibition of ACE can affect various regulatory systems of the body, such as the modulation of blood pressure (BP), the immune system, and central nervous system [3]. ACE-1 is a multifunctional enzyme that is localized in various tissues and associated with the renin-angiotensin system that controls BP. ACE-1 converts angiotensin I to the angiotensin II, which is a potent vasoconstrictor. ACE-1 inactivates bradykinin, which has vasodilator activity [4]. ACE inhibitors exert anti-hypertensive effects through preventing bradykinin degradation and, reducing angiotensin-II formation
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