Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.
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.
Quirós
A
A
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, Spain.
Hernández-Ledesma
B
B
Ramos
M
M
Amigo
L
L
Recio
I
I
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis / Q000494:pharmacology*; D000818:Animals; D002364:Caseins / Q000737:chemistry / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D043302:Cultured Milk Products / Q000737:chemistry*; D004063:Digestion; D005285:Fermentation; D041981:Gastrointestinal Tract / Q000378:metabolism; D006041:Goats; D006868:Hydrolysis; D007778:Lactobacillus / Q000378:metabolism; D013058:Mass Spectrometry; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000378:metabolism
D000806:Angiotensin-Converting Enzyme Inhibitors; D002364:Caseins; D010455:Peptides