CORE
🇺🇦
make metadata, not war
Services
Services overview
Explore all CORE services
Access to raw data
API
Dataset
FastSync
Content discovery
Recommender
Discovery
OAI identifiers
OAI Resolver
Managing content
Dashboard
Bespoke contracts
Consultancy services
Support us
Support us
Membership
Sponsorship
Community governance
Advisory Board
Board of supporters
Research network
About
About us
Our mission
Team
Blog
FAQs
Contact us
In vitro simulated gastrointestinal digestion of donkeys' milk. Peptide characterization by high performance liquid chromatography-tandem mass spectrometry
Authors
Izaro Bermeosolo Bidasolo
José Ángel Gómez-Ruiz
Mercedes Ramos
Publication date
28 August 2014
Publisher
'Elsevier BV'
Doi
Cite
Abstract
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.This work has received financial support from projects AGL2008-01713, Consolider Ingenio 2010 FUN-C Food CSD2007-00063 and P2009/AGR-1469.Peer Reviewe
Similar works
Full text
Available Versions
Digital.CSIC
See this paper in CORE
Go to the repository landing page
Download from data provider
oai:digital.csic.es:10261/1013...
Last time updated on 25/05/2016