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Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides

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Abstract
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 IV 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.
Keywords
Gelatin hydrolysate, SKIN, antihypertensive peptides, FOOD, angiotensin I-converting enzyme (ACE), VITRO, BLOOD-PRESSURE, CELLS, WHEY-PROTEIN, ORAL INGESTION, aortic rings, HYPERTENSIVE-RATS, spontaneously hypertensive rats, gastrointestinal and mucosal digestion, blood pressure

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Citation

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Chicago
Herregods, Griet, John Van Camp, Nicole Morel, Bart Ghesquière, Kris Gevaert, Lieselot Vercruysse, Stephan Dierckx, Erwin Quanten, and Guy Smagghe. 2011. “Angiotensin I-converting Enzyme Inhibitory Activity of Gelatin Hydrolysates and Identification of Bioactive Peptides.” Journal of Agricultural and Food Chemistry 59 (2): 552–558.
APA
Herregods, G., Van Camp, J., Morel, N., Ghesquière, B., Gevaert, K., Vercruysse, L., Dierckx, S., et al. (2011). Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 59(2), 552–558.
Vancouver
1.
Herregods G, Van Camp J, Morel N, Ghesquière B, Gevaert K, Vercruysse L, et al. Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. 2011;59(2):552–8.
MLA
Herregods, Griet, John Van Camp, Nicole Morel, et al. “Angiotensin I-converting Enzyme Inhibitory Activity of Gelatin Hydrolysates and Identification of Bioactive Peptides.” JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 59.2 (2011): 552–558. Print.
@article{1184392,
  abstract     = {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 IV 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.},
  author       = {Herregods, Griet and Van Camp, John and Morel, Nicole and Ghesqui{\`e}re, Bart and Gevaert, Kris and Vercruysse, Lieselot and Dierckx, Stephan and Quanten, Erwin and Smagghe, Guy},
  issn         = {0021-8561},
  journal      = {JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY},
  language     = {eng},
  number       = {2},
  pages        = {552--558},
  title        = {Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides},
  url          = {http://dx.doi.org/10.1021/jf1037823},
  volume       = {59},
  year         = {2011},
}

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