2022
Vivanco-Maroto, Santiaga María; Santos-Hernández, Marta; Sanchón, Javier; Picariello, Gianluca; Recio, Isidra; Miralles, Beatriz
In vitro digestion of milk proteins including intestinal brush border membrane peptidases. Transepithelial transport of resistant casein domains Artículo de revista
En: Food Research International, vol. 157, pp. 111238, 2022, ISSN: 0963-9969.
Resumen | Enlaces | BibTeX | Etiquetas: Absorption, Brush border membrane, Caco-2 cell, Casein, Mass spectrometry, Peptidomics, Whey
@article{VIVANCOMAROTO2022111238,
title = {In vitro digestion of milk proteins including intestinal brush border membrane peptidases. Transepithelial transport of resistant casein domains},
author = {Santiaga María Vivanco-Maroto and Marta Santos-Hernández and Javier Sanchón and Gianluca Picariello and Isidra Recio and Beatriz Miralles},
url = {https://www.sciencedirect.com/science/article/pii/S0963996922002952},
doi = {https://doi.org/10.1016/j.foodres.2022.111238},
issn = {0963-9969},
year = {2022},
date = {2022-01-01},
urldate = {2022-01-01},
journal = {Food Research International},
volume = {157},
pages = {111238},
abstract = {The use of enzymes from the brush border membrane (BBM) in simulated gastrointestinal digestion of milk proteins has been evaluated. With this purpose, the resistant sequences from casein and milk whey proteins after INFOGEST in vitro digestion with and without BBM have been analyzed by tandem mass spectrometry. The use of BBM revealed additional cleavages to those found with pancreatic enzymes, although the number of total identified peptides decreased due to the reduction of the peptide size. These new cleavages were mainly attributed to the activity of amino- and carboxy-peptidases, which was also reflected in the higher concentration of free amino acids found in the gastrointestinal digests with BBM. The peptidome of the simulated gastrointestinal digests was compared with that previously obtained in digests aspirated from human jejunum after oral administration of the same substrates. The addition of BBM did not change significantly the peptide profile, although it allowed the identification of peptides found in human digests. However, none of the models was able to reproduce the large variety of peptides found in vivo. In addition, in vitro transepithelial transport of six β-casein derived peptides resistant to gastrointestinal digestion, including the opioid β-casomorphin-7, was also evaluated. The results point to the importance of the nature of the N- and C-terminal end for the transport rate through the Caco-2 cell monolayer. Therefore, the use of BBM as a supplementary step after simulated pancreatic digestion can be considered in bioavailability studies since the final sequence can determine the absorption of peptides.},
keywords = {Absorption, Brush border membrane, Caco-2 cell, Casein, Mass spectrometry, Peptidomics, Whey},
pubstate = {published},
tppubtype = {article}
}
The use of enzymes from the brush border membrane (BBM) in simulated gastrointestinal digestion of milk proteins has been evaluated. With this purpose, the resistant sequences from casein and milk whey proteins after INFOGEST in vitro digestion with and without BBM have been analyzed by tandem mass spectrometry. The use of BBM revealed additional cleavages to those found with pancreatic enzymes, although the number of total identified peptides decreased due to the reduction of the peptide size. These new cleavages were mainly attributed to the activity of amino- and carboxy-peptidases, which was also reflected in the higher concentration of free amino acids found in the gastrointestinal digests with BBM. The peptidome of the simulated gastrointestinal digests was compared with that previously obtained in digests aspirated from human jejunum after oral administration of the same substrates. The addition of BBM did not change significantly the peptide profile, although it allowed the identification of peptides found in human digests. However, none of the models was able to reproduce the large variety of peptides found in vivo. In addition, in vitro transepithelial transport of six β-casein derived peptides resistant to gastrointestinal digestion, including the opioid β-casomorphin-7, was also evaluated. The results point to the importance of the nature of the N- and C-terminal end for the transport rate through the Caco-2 cell monolayer. Therefore, the use of BBM as a supplementary step after simulated pancreatic digestion can be considered in bioavailability studies since the final sequence can determine the absorption of peptides.
2021
Miralles, Beatriz; Sanchón, J.; Sánchez-Rivera, L.; Martínez-Maqueda, D.; Gouar, Y. Le; Dupont, D.; Amigo, L.; Recio, Isidra
Digestion of micellar casein in duodenum cannulated pigs. Correlation between in vitro simulated gastric digestion and in vivo data Artículo de revista
En: Food Chemistry, vol. 343, pp. 128424, 2021, ISSN: 0308-8146.
Resumen | Enlaces | BibTeX | Etiquetas: Amino acids, Casein, Digestion, Peptidomics, Pig duodenum
@article{MIRALLES2021128424,
title = {Digestion of micellar casein in duodenum cannulated pigs. Correlation between in vitro simulated gastric digestion and in vivo data},
author = {Beatriz Miralles and J. Sanchón and L. Sánchez-Rivera and D. Martínez-Maqueda and Y. Le Gouar and D. Dupont and L. Amigo and Isidra Recio},
url = {https://www.sciencedirect.com/science/article/pii/S030881462032286X},
doi = {https://doi.org/10.1016/j.foodchem.2020.128424},
issn = {0308-8146},
year = {2021},
date = {2021-01-01},
urldate = {2021-01-01},
journal = {Food Chemistry},
volume = {343},
pages = {128424},
abstract = {Correlation and validation of the results of simulated gastrointestinal digestion of food compounds towards in vivo data is essential. The objective of this work was to monitor the digestion of milk micellar casein in the porcine upper intestinal tract and to match the outcome with the gastric in vitro digestion following the Infogest harmonized protocol. In pig duodenum, small amounts of intact caseins were present in all samples, while caseins were observed up to 60 min of gastric in vitro digestion. The peptide profile generated after in vitro and in vivo digestion showed clear similarities with specific overrepresented regions rich in proline and other hydrophobic residues. The statistical comparison of the in vivo and in vitro peptidome resulted in satisfactory correlation coefficients, up to 0.8. Therefore, the in vitro protocol used was a robust and simple model that provides a similar peptide profile than that found in porcine duodenum.},
keywords = {Amino acids, Casein, Digestion, Peptidomics, Pig duodenum},
pubstate = {published},
tppubtype = {article}
}
Correlation and validation of the results of simulated gastrointestinal digestion of food compounds towards in vivo data is essential. The objective of this work was to monitor the digestion of milk micellar casein in the porcine upper intestinal tract and to match the outcome with the gastric in vitro digestion following the Infogest harmonized protocol. In pig duodenum, small amounts of intact caseins were present in all samples, while caseins were observed up to 60 min of gastric in vitro digestion. The peptide profile generated after in vitro and in vivo digestion showed clear similarities with specific overrepresented regions rich in proline and other hydrophobic residues. The statistical comparison of the in vivo and in vitro peptidome resulted in satisfactory correlation coefficients, up to 0.8. Therefore, the in vitro protocol used was a robust and simple model that provides a similar peptide profile than that found in porcine duodenum.
2020
Santos-Hernández, Marta; Alfieri, Fabio; Gallo, Veronica; Miralles, Beatriz; Masi, Paolo; Romano, Annalisa; Ferranti, Pasquale; Recio, Isidra
Compared digestibility of plant protein isolates by using the INFOGEST digestion protocol Artículo de revista
En: Food Research International, vol. 137, pp. 109708, 2020, ISSN: 0963-9969.
Resumen | Enlaces | BibTeX | Etiquetas: Casein, Epitopes, Garden pea, Gastrointestinal digestion, Grass pea, Lentil, Protein isolate, Soybean, Whey protein
@article{SANTOSHERNANDEZ2020109708,
title = {Compared digestibility of plant protein isolates by using the INFOGEST digestion protocol},
author = {Marta Santos-Hernández and Fabio Alfieri and Veronica Gallo and Beatriz Miralles and Paolo Masi and Annalisa Romano and Pasquale Ferranti and Isidra Recio},
url = {https://www.sciencedirect.com/science/article/pii/S096399692030733X},
doi = {https://doi.org/10.1016/j.foodres.2020.109708},
issn = {0963-9969},
year = {2020},
date = {2020-01-01},
urldate = {2020-01-01},
journal = {Food Research International},
volume = {137},
pages = {109708},
abstract = {The use of ingredients based on plant protein isolates is being promoted due to sustainability and health reasons. However, it is necessary to explore the behaviour of plant protein isolates during gastrointestinal digestion including the profile of released free amino acids and the characterization of resistant domains to gastrointestinal digestion. The aim of the present study was to monitor protein degradation of four legume protein isolates: garden pea, grass pea, soybean and lentil, using the harmonized Infogest in vitro digestion protocol. In vitro digests were characterized regarding protein, peptide and free amino acid content. Soybean was the protein isolate with the highest percentage of insoluble nitrogen at the end of the digestion (12%), being this fraction rich in hydrophobic amino acids. Free amino acids were mainly released during the intestinal digestion, comprising 21–24% of the total nitrogen content, while the percentage of nitrogen corresponding to peptides ranged from 66 to 76%. Legume globulins were resistant to gastric digestion whereas they were hydrolysed into peptides and amino acids during the intestinal phase. However, the molecular weight (MW) distribution demonstrated that all intestinal digests, except those from soybean, contained peptides with MW > 4 kDa at the end of gastrointestinal digestion. The profile of free amino acids released during digestion supports legume protein isolates as an excellent source of essential amino acids to be used in protein-rich food products. Peptides released during digestion matched with previously reported epitopes from the same plant species or others, explaining the ability to induce allergic reactions and cross-linked reactivity.},
keywords = {Casein, Epitopes, Garden pea, Gastrointestinal digestion, Grass pea, Lentil, Protein isolate, Soybean, Whey protein},
pubstate = {published},
tppubtype = {article}
}
The use of ingredients based on plant protein isolates is being promoted due to sustainability and health reasons. However, it is necessary to explore the behaviour of plant protein isolates during gastrointestinal digestion including the profile of released free amino acids and the characterization of resistant domains to gastrointestinal digestion. The aim of the present study was to monitor protein degradation of four legume protein isolates: garden pea, grass pea, soybean and lentil, using the harmonized Infogest in vitro digestion protocol. In vitro digests were characterized regarding protein, peptide and free amino acid content. Soybean was the protein isolate with the highest percentage of insoluble nitrogen at the end of the digestion (12%), being this fraction rich in hydrophobic amino acids. Free amino acids were mainly released during the intestinal digestion, comprising 21–24% of the total nitrogen content, while the percentage of nitrogen corresponding to peptides ranged from 66 to 76%. Legume globulins were resistant to gastric digestion whereas they were hydrolysed into peptides and amino acids during the intestinal phase. However, the molecular weight (MW) distribution demonstrated that all intestinal digests, except those from soybean, contained peptides with MW > 4 kDa at the end of gastrointestinal digestion. The profile of free amino acids released during digestion supports legume protein isolates as an excellent source of essential amino acids to be used in protein-rich food products. Peptides released during digestion matched with previously reported epitopes from the same plant species or others, explaining the ability to induce allergic reactions and cross-linked reactivity.
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