Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion

Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese.... In this study, several peptides, which had previously been identified in active HPLC fractions from Manchego cheese, were synthesised and their angiotensin converting enzyme (ACE)-inhibitory activities were measured. From 11 peptides, which were selected based on their structures, only two, VRYL and KKYNVPQL, showed considerable ACE-inhibitory activity with IC 50 values of 24.1 and 77.1 μ m , respectively. Subsequently, the impact of the gastrointestinal digestion on ACE-inhibitory activity was evaluated. Some of the peptides selected were resistant to the incubation with pepsin followed by hydrolysis with a pancreatic extract. The ACE-inhibitory activity after simulated digestion did not change drastically except for peptide α s2 -CN f(195-204) (TQPKTNAIPY) that exhibited an activity 6 times greater after simulated digestion. In contrast, after simulated digestion, the activities of peptides VRYL and KKYNVPQL decreased. The peptides not hydrolysed by gastrointestinal enzymes and peptide VRYL, which was only partly hydrolysed, were incubated with ACE and were found to be true inhibitors of the enzyme and to have a competitive inhibition pattern. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Dairy Journal Elsevier

Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion

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Publisher
Elsevier
Copyright
Copyright © 2004 Elsevier Ltd
ISSN
0958-6946
eISSN
1879-0143
D.O.I.
10.1016/j.idairyj.2004.04.007
Publisher site
See Article on Publisher Site

Abstract

In this study, several peptides, which had previously been identified in active HPLC fractions from Manchego cheese, were synthesised and their angiotensin converting enzyme (ACE)-inhibitory activities were measured. From 11 peptides, which were selected based on their structures, only two, VRYL and KKYNVPQL, showed considerable ACE-inhibitory activity with IC 50 values of 24.1 and 77.1 μ m , respectively. Subsequently, the impact of the gastrointestinal digestion on ACE-inhibitory activity was evaluated. Some of the peptides selected were resistant to the incubation with pepsin followed by hydrolysis with a pancreatic extract. The ACE-inhibitory activity after simulated digestion did not change drastically except for peptide α s2 -CN f(195-204) (TQPKTNAIPY) that exhibited an activity 6 times greater after simulated digestion. In contrast, after simulated digestion, the activities of peptides VRYL and KKYNVPQL decreased. The peptides not hydrolysed by gastrointestinal enzymes and peptide VRYL, which was only partly hydrolysed, were incubated with ACE and were found to be true inhibitors of the enzyme and to have a competitive inhibition pattern.

Journal

International Dairy JournalElsevier

Published: Dec 1, 2004

References

  • Angiotensin I-converting enzyme inhibitor from Grifola frondosa
    Choi, H.S.; Cho, H.Y.; Yang, H.C.; Ra, K.S.; Suh, H.J.
  • Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starters cultures
    Gómez-Ruiz, J.A.; Ramos, M.; Recio, I.
  • Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins
    Pihlanto-Leppälä, A.; Rokka, T.; Korhonen, H.

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