2018
Sanchón, J.; Fernández-Tomé, S.; Miralles, Beatriz; Hernández-Ledesma, B.; Tomé, D.; Gaudichon, C.; Recio, Isidra
Protein degradation and peptide release from milk proteins in human jejunum. Comparison with in vitro gastrointestinal simulation Artículo de revista
En: Food Chemistry, vol. 239, pp. 486-494, 2018, ISSN: 0308-8146.
Resumen | Enlaces | BibTeX | Etiquetas: Digestion, Mass spectrometry, Milk protein digestion, Peptidomic
@article{SANCHON2018486,
title = {Protein degradation and peptide release from milk proteins in human jejunum. Comparison with in vitro gastrointestinal simulation},
author = {J. Sanchón and S. Fernández-Tomé and Beatriz Miralles and B. Hernández-Ledesma and D. Tomé and C. Gaudichon and Isidra Recio},
url = {https://www.sciencedirect.com/science/article/pii/S0308814617311172},
doi = {https://doi.org/10.1016/j.foodchem.2017.06.134},
issn = {0308-8146},
year = {2018},
date = {2018-01-01},
urldate = {2018-01-01},
journal = {Food Chemistry},
volume = {239},
pages = {486-494},
abstract = {Human jejunal digests after oral ingestion of casein and whey protein were collected by a nasogastric tube and protein degradation and peptide release was compared with that found in the digests of the same substrates using a standardised protocol. No intact casein was detected in the jejunal nor in the in vitro samples taken during the intestinal phase, while β-lactoglobulin was found in one hour-jejunal samples in agreement with the in vitro digestion. In vivo and in vitro digests showed comparable peptide profiles and high number of common sequences. A selective precipitation step was used to strengthen the identification of phosphorylated peptides. Most of the sequences found in jejunum, some of them not previously described, were also identified in the simulated digests. Common resistant regions to digestion were identified, revealing that the in vitro protocol constitutes a good approximation to the physiological gastrointestinal digestion of milk proteins.},
keywords = {Digestion, Mass spectrometry, Milk protein digestion, Peptidomic},
pubstate = {published},
tppubtype = {article}
}
Human jejunal digests after oral ingestion of casein and whey protein were collected by a nasogastric tube and protein degradation and peptide release was compared with that found in the digests of the same substrates using a standardised protocol. No intact casein was detected in the jejunal nor in the in vitro samples taken during the intestinal phase, while β-lactoglobulin was found in one hour-jejunal samples in agreement with the in vitro digestion. In vivo and in vitro digests showed comparable peptide profiles and high number of common sequences. A selective precipitation step was used to strengthen the identification of phosphorylated peptides. Most of the sequences found in jejunum, some of them not previously described, were also identified in the simulated digests. Common resistant regions to digestion were identified, revealing that the in vitro protocol constitutes a good approximation to the physiological gastrointestinal digestion of milk proteins.
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