Journal
JOURNAL OF DAIRY SCIENCE
Volume 88, Issue 10, Pages 3480-3487Publisher
ELSEVIER SCIENCE INC
DOI: 10.3168/jds.S0022-0302(05)73032-0
Keywords
angiotensin-converting enzyme-inhibitory activity; caprine kefir; simulated gastrointestinal digestion; mass spectrometry
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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 beta-casein f(47-52) (DKIHPF), which exhibited an activity 8 times greater after hydrolysis.
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