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In vitro simulated gastrointestinal digestion of donkeys' milk. Peptide characterization by high performance liquid chromatography-tandem mass spectrometry

AuthorsBermeosolo Bidasolo, Izaro; Ramos, Mercedes ; Gómez-Ruiz, José Ángel
Issue Date2012
CitationInternational Dairy Journal 24(2): 146-152 (2012)
AbstractDonkeys' milk was subjected to in vitro simulated gastrointestinal digestion using pepsin and a mixture of pancreatic enzymes. Analysis of the hydrolysate by high pressure liquid chromatography coupled to tandem mass spectrometry allowed the identification of 46 peptides, of which 30 peptides belonged to β-casein (β-CN). The gastrointestinal digest possessed an important angiotensin converting enzyme (ACE)-inhibitory activity with an IC 50 of 273.0±27.9μgmL -1. The β-CN fragment f(176-185) [VAPFPQPVVP], one of the most abundant peptides in the hydrolysate, was synthesized and its ACE-inhibitory activity measured. This peptide showed very potent activity with an IC 50 of 48.8±2.3μm. To our knowledge, this is the first time that a bioactive peptide from donkeys' milk has been reported. © 2011 Elsevier Ltd.
Identifiersdoi: 10.1016/j.idairyj.2011.04.014
issn: 0958-6946
e-issn: 1879-0143
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