2020
Santos-Hernández, Marta; Miralles, Beatriz; Amigo, Lourdes; Recio, Isidra
Peptidomic data of egg white gastrointestinal digests prepared using the Infogest Harmonized Protocol Artículo de revista
En: Data in Brief, vol. 31, pp. 105932, 2020, ISSN: 2352-3409.
Resumen | Enlaces | BibTeX | Etiquetas: Characterization, Egg white protein, Maldi-tof, Mass spectrometry, Peptidomics
@article{SANTOSHERNANDEZ2020105932,
title = {Peptidomic data of egg white gastrointestinal digests prepared using the Infogest Harmonized Protocol},
author = {Marta Santos-Hernández and Beatriz Miralles and Lourdes Amigo and Isidra Recio},
url = {https://www.sciencedirect.com/science/article/pii/S235234092030826X},
doi = {https://doi.org/10.1016/j.dib.2020.105932},
issn = {2352-3409},
year = {2020},
date = {2020-01-01},
journal = {Data in Brief},
volume = {31},
pages = {105932},
abstract = {These data are related to the research article entitled “Induction of CCK and GLP-1 release in enteroendocrine cells by egg white peptides generated during gastrointestinal digestion”. In this article, the peptide and free amino acid profile of egg white gastrointestinal in vitro digests is shown. Egg white proteins were digested following the INFOGEST gastrointestinal digestion protocol. Different time points of gastric and intestinal digestion were characterized regarding protein, peptide and amino acid content. Protein degradation was followed by SDS-PAGE where some electrophoretic bands were identified by MALDI-TOF/TOF after tryptic digestion. Moreover, the molecular weight distribution of egg white peptides found at different times of gastrointestinal digestion was performed using MALDI-TOF. Peptides identified from the most abundant egg white proteins by tandem mass spectrometry were represented using a peptide profile tool and raw data are given in table format. These results reveal the protein regions resistant to digestion and illustrate the free amino acid profile of egg white protein at the end of the digestion process. These data can be used for nutritional purposes and to identify allergen epitopes or bioactive sequences.},
keywords = {Characterization, Egg white protein, Maldi-tof, Mass spectrometry, Peptidomics},
pubstate = {published},
tppubtype = {article}
}
These data are related to the research article entitled “Induction of CCK and GLP-1 release in enteroendocrine cells by egg white peptides generated during gastrointestinal digestion”. In this article, the peptide and free amino acid profile of egg white gastrointestinal in vitro digests is shown. Egg white proteins were digested following the INFOGEST gastrointestinal digestion protocol. Different time points of gastric and intestinal digestion were characterized regarding protein, peptide and amino acid content. Protein degradation was followed by SDS-PAGE where some electrophoretic bands were identified by MALDI-TOF/TOF after tryptic digestion. Moreover, the molecular weight distribution of egg white peptides found at different times of gastrointestinal digestion was performed using MALDI-TOF. Peptides identified from the most abundant egg white proteins by tandem mass spectrometry were represented using a peptide profile tool and raw data are given in table format. These results reveal the protein regions resistant to digestion and illustrate the free amino acid profile of egg white protein at the end of the digestion process. These data can be used for nutritional purposes and to identify allergen epitopes or bioactive sequences.
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