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Sequential release of milk protein―derived bioactive peptides in the jejunum in healthy humans

The digestive hydrolysis of dietary proteins leads to the release of peptides in the intestinal tract, where they may exert a variety of functions, but their characterization and quantification are difficult. We aimed to characterize and determine kinetics of the formation of peptides present in the...

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Published in:The American journal of clinical nutrition 2013-06, Vol.97 (6), p.1314-1323
Main Authors: BOUTROU, Rachel, GAUDICHON, Claire, DUPONT, Didier, JARDIN, Julien, AIRINEI, Gheorghe, MARSSET-BAGLIERI, Agnes, BENAMOUZIG, Robert, TOME, Daniel, LEONIL, Joëlle
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cited_by cdi_FETCH-LOGICAL-c430t-a65c8695ffecbb8ede763a8cc9c461b7d5e06f280862c4d27931e32f64c372963
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creator BOUTROU, Rachel
GAUDICHON, Claire
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TOME, Daniel
LEONIL, Joëlle
description The digestive hydrolysis of dietary proteins leads to the release of peptides in the intestinal tract, where they may exert a variety of functions, but their characterization and quantification are difficult. We aimed to characterize and determine kinetics of the formation of peptides present in the jejunum of humans who ingested casein or whey proteins by using mass spectrometry and to look for and quantify bioactive peptides. Subjects were equipped with a double-lumen nasogastric tube that migrated to the proximal jejunum. A sample collection was performed for 6 h after the ingestion of 30 g (15)N-labeled casein (n = 7) or whey proteins (WPs; n = 6). Nitrogen flow rates were measured, and peptides were identified by using mass spectrometry. After casein ingestion, medium-size peptides (750-1050 kDa) were released during 6 h, whereas larger peptides (1050-1800 kDa) were released from WPs in the first 3 h. A total of 356 and 146 peptides were detected and sequenced in the jejunum after casein and WP ingestion, respectively. β-casein was the most important precursor of peptides, including bioactive peptides with various activities. The amounts of β-casomorphins (β-casein 57-, 58-, 59-, and 60-66) and β-casein 108-113 released on the postprandial window were sufficient to elicit the biological action of these peptides (ie, opioid and antihypertensive, respectively). Clear evidence is shown of the presence of bioactive peptides in the jejunum of healthy humans who ingested casein. Our findings raise the question about the physiologic conditions under which these peptides can express their bioactivity in humans. This trial was registered at clinicaltrials.gov as NCT00862329.
doi_str_mv 10.3945/ajcn.112.055202
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The amounts of β-casomorphins (β-casein 57-, 58-, 59-, and 60-66) and β-casein 108-113 released on the postprandial window were sufficient to elicit the biological action of these peptides (ie, opioid and antihypertensive, respectively). Clear evidence is shown of the presence of bioactive peptides in the jejunum of healthy humans who ingested casein. Our findings raise the question about the physiologic conditions under which these peptides can express their bioactivity in humans. 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source ScienceDirect®
subjects Adolescent
Adult
Biological and medical sciences
Caseins - analysis
Caseins - metabolism
Chromatography, Liquid
Diet
Dietary Proteins - administration & dosage
Digestion
Digestive system
Endorphins - analysis
Endorphins - metabolism
Feeding. Feeding behavior
Female
Food and Nutrition
Fundamental and applied biological sciences. Psychology
Humans
Hydrolysis
Intestinal Mucosa - metabolism
Jejunum - metabolism
Kinetics
Life Sciences
Male
Mass spectrometry
Meals
Milk Proteins - analysis
Milk Proteins - metabolism
Nitrogen - analysis
Nitrogen - metabolism
Nutrition
Peptides
Peptides - metabolism
Proteins
Single-Blind Method
Tandem Mass Spectrometry
Vertebrates: anatomy and physiology, studies on body, several organs or systems
Whey Proteins
Young Adult
title Sequential release of milk protein―derived bioactive peptides in the jejunum in healthy humans
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