Herregods, Griet
Van Camp, John
Morel, Nicole
[UCL]
Ghesquière, Bart
Gevaert, Kris
Vercruysse, Lieselot
Dierckx, Stephan
Quanten, Erwin
Smagghe, Guy
In this project we report on the angiotensin I-converting enzyme (ACE)-inhibitory activity of a bovine gelatin hydrolysate (Bh2) that was submitted to further hydrolysis by different enzymes. The thermolysin hydrolysate (Bh2t) showed the highest in vitro ACE inhibitory activity, and interestingly a marked in vivo blood pressure-lowering effect was demonstrated in spontaneously hypertensive rats (SHR). In contrast, Bh2 showed no effect in SHR, confirming the need for the extra thermolysin hydrolysis. Hence, an angiotensin I-evoked contractile response in isolated rat aortic rings was inhibited by Bh2t, but not by Bh2, suggesting ACE inhibition as the underlying antihypertensive mechanism for Bh2t. Using mass spectrometry, seven small peptides, AG, AGP, VGP, PY, QY, DY and IY or LY or HO-PY were identified in Bh2t. As these peptides showed ACE inhibitory activity and were more prominent in Bh2t than in Bh2, the current data provide evidence that these contribute to the antihypertensive effect of Bh2t. © 2010 American Chemical Society.
Bibliographic reference |
Herregods, Griet ; Van Camp, John ; Morel, Nicole ; Ghesquière, Bart ; Gevaert, Kris ; et. al. Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. In: Journal of Agricultural and Food Chemistry, Vol. 59, no. 2, p. 552-558 (2011) |
Permanent URL |
http://hdl.handle.net/2078.1/163533 |