In vitro simulated gastrointestinal digestion of donkeys' milk. Peptide characterization by high performance liquid chromatography-tandem mass spectrometry
Donkeys' 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.
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| Format: | artículo biblioteca |
| Published: |
Elsevier
2012
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| Online Access: | http://hdl.handle.net/10261/101361 http://dx.doi.org/10.13039/501100004837 http://dx.doi.org/10.13039/100012818 |
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