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dc.contributor.authorDave, Lakshmi A.-
dc.contributor.authorHayes, María-
dc.contributor.authorMora, Leticia-
dc.contributor.authorMontoya, Carlos A.-
dc.contributor.authorMoughan, Paul J.-
dc.contributor.authorRutherfurd, Shane M.-
dc.identifierdoi: 10.3390/ijms17040482-
dc.identifier.citationInternational Journal of Molecular Sciences 17 (4): 482 (2016)-
dc.description.abstractA recently proposed paradigm suggests that, like their dietary counterparts, digestion of gastrointestinal endogenous proteins (GEP) may also produce bioactive peptides. With an aim to test this hypothesis, <i>in vitro</i> digests of four GEP namely; trypsin (TRYP), lysozyme (LYS), mucin (MUC), serum albumin (SA) and a dietary protein chicken albumin (CA) were screened for their angiotensin-I converting (ACE-I), renin, platelet-activating factor-acetylhydrolase (PAF-AH) and dipeptidyl peptidase-IV inhibitory (DPP-IV) and antioxidant potential following simulated <i>in vitro</i> gastrointestinal digestion. Further, the resultant small intestinal digests were enriched to obtain peptides between 3–10 kDa in size. All <i>in vitro</i> digests of the four GEP were found to inhibit ACE-I compared to the positive control captopril when assayed at a concentration of 1 mg/mL, while the LYS < 3-kDa permeate fraction inhibited renin by 40% (±1.79%). The LYS < 10-kDa fraction inhibited PAF-AH by 39% (±4.34%), and the SA < 3-kDa fraction inhibited DPP-IV by 45% (±1.24%). The MUC < 3-kDa fraction had an ABTS-inhibition antioxidant activity of 150 (±24.79) µM trolox equivalent and the LYS < 10-kDa fraction inhibited 2,2-Diphenyl-1-picrylhydrazyl (DPPH) by 54% (±1.62%). Moreover, over 190 peptide-sequences were identified from the bioactive GEP fractions. The findings of the present study indicate that GEP are a significant source of bioactive peptides which may influence gut function.-
dc.description.sponsorshipThe authors acknowledge the financial support provided by the Centre of Research Excellence (CoRE) fund from the Tertiary Education Commission and the Ministry of Education, New Zealand. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.-
dc.description.sponsorshipWe acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI).-
dc.publisherMultidisciplinary Digital Publishing Institute-
dc.relation.isversionofPublisher's version-
dc.titleGastrointestinal Endogenous Protein-Derived Bioactive Peptides: An in Vitro Study of Their Gut Modulatory Potential-
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)-
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