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J. Dairy Sci. 88:3480-3487
© American Dairy Science Association, 2005.

Angiotensin-Converting Enzyme Inhibitory Activity of Peptides Derived from Caprine Kefir

A. Quirós, B. Hernández-Ledesma, M. Ramos, L. Amigo and I. Recio

Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, Spain

Corresponding author: I. Recio; e-mail: recio{at}ifi.csic.es.

In this study, a potent angiotensin-converting enzyme (ACE)-inhibitory activity was found in a commercial kefir made from caprine milk. The low molecular mass peptides released from caseins during fermentation were mainly responsible for this activity. Sixteen peptides were identified by HPLC-tandem mass spectrometry. Two of these peptides, with sequences PYVRYL and LVYPFTGPIPN, showed potent ACE-inhibitory properties. The impact of gastrointestinal digestion on ACE-inhibitory activity of kefir peptides was also evaluated. Some of these peptides were resistant to the incubation with pepsin followed by hydrolysis with Corolase PP. The ACE-inhibitory activity after simulated digestion was similar to or slightly lower than unhydrolyzed peptides, except for peptide ß-casein f(47-52) (DKIHPF), which exhibited an activity 8 times greater after hydrolysis.

Key Words: angiotensin-converting enzyme-inhibitory activity • caprine kefir • simulated gastrointestinal digestion • mass spectrometry

Abbreviation key: ACE = angiotensin-converting enzyme, IC50 = protein concentration needed to inhibit the original ACE activity by 50%, MS/MS = tandem mass spectrometry, RP-HPLC = reverse phase-HPLC, WSE = water-soluble extract




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