2021
Miralles, Beatriz; Sanchón, J.; Sánchez-Rivera, L.; Martínez-Maqueda, D.; Gouar, Y. Le; Dupont, D.; Amigo, L.; Recio, Isidra
Peptidomic data in porcine duodenal effluents after oral administration of micellar casein Artículo de revista
En: Data in Brief, vol. 38, pp. 107326, 2021, ISSN: 2352-3409.
Resumen | Enlaces | BibTeX | Etiquetas: Digestion, Micellar casein, Peptidomic analysis, Pig duodenum
@article{MIRALLES2021107326,
title = {Peptidomic data in porcine duodenal effluents after oral administration of micellar casein},
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/S2352340921006107},
doi = {https://doi.org/10.1016/j.dib.2021.107326},
issn = {2352-3409},
year = {2021},
date = {2021-01-01},
urldate = {2021-01-01},
journal = {Data in Brief},
volume = {38},
pages = {107326},
abstract = {The data in this article are related to the research publication “Digestion of micellar casein in duodenum cannulated pigs. Correlation between in vitro simulated gastric digestion and in vivo data” (Miralles et al., Food Chemistry, 2021, 343, 128428). Pig duodenum effluents were collected with a T-shaped cannula 15 min before and during digestion over 150 min after casein intake. The casein degradation profile of individual pigs during digestion is presented. All identified peptide sequences at different digestion times for six subjects are provided. The peptide profile of digests in the form of heat maps is shown for αs1-, αs2-, β- and κ-casein. The sum of amino acids belonging to peptides released from β- and αs1-casein has been used to determine correlation coefficients and range the inter-individual variability. Finally, the global amino acid composition, isoelectric point and sequence length of all released peptides has been determined.},
keywords = {Digestion, Micellar casein, Peptidomic analysis, Pig duodenum},
pubstate = {published},
tppubtype = {article}
}
The data in this article are related to the research publication “Digestion of micellar casein in duodenum cannulated pigs. Correlation between in vitro simulated gastric digestion and in vivo data” (Miralles et al., Food Chemistry, 2021, 343, 128428). Pig duodenum effluents were collected with a T-shaped cannula 15 min before and during digestion over 150 min after casein intake. The casein degradation profile of individual pigs during digestion is presented. All identified peptide sequences at different digestion times for six subjects are provided. The peptide profile of digests in the form of heat maps is shown for αs1-, αs2-, β- and κ-casein. The sum of amino acids belonging to peptides released from β- and αs1-casein has been used to determine correlation coefficients and range the inter-individual variability. Finally, the global amino acid composition, isoelectric point and sequence length of all released peptides has been determined.
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
Sousa, Raquel; Portmann, Reto; Dubois, Sébastien; Recio, Isidra; Egger, Lotti
Protein digestion of different protein sources using the INFOGEST static digestion model Artículo de revista
En: Food Research International, vol. 130, pp. 108996, 2020, ISSN: 0963-9969.
Resumen | Enlaces | BibTeX | Etiquetas: Amino acid, Digestion, Liquid chromatography-mass spectrometry peptides, Protein hydrolysis, proteins
@article{SOUSA2020108996,
title = {Protein digestion of different protein sources using the INFOGEST static digestion model},
author = {Raquel Sousa and Reto Portmann and Sébastien Dubois and Isidra Recio and Lotti Egger},
url = {https://www.sciencedirect.com/science/article/pii/S0963996920300211},
doi = {https://doi.org/10.1016/j.foodres.2020.108996},
issn = {0963-9969},
year = {2020},
date = {2020-01-01},
journal = {Food Research International},
volume = {130},
pages = {108996},
abstract = {In vitro digestion systems are valuable tools for understanding and monitoring the complex behavior of food degradation during digestion, thus proving to be good candidates for replacing in vivo assays. The aim of the present work was to study protein hydrolysis in a selection of different protein sources using the harmonized INFOGEST static protocol: three isolated proteins (collagen, zein, and whey protein) and five foods (sorghum flour, wheat bran cereals, peanuts, black beans, and pigeon peas). The proteins of all the substrates were analyzed by SDS-PAGE and HPLC-MS/MS. Individual amino acid composition was analyzed by high-performance liquid chromatography (HPLC). EAA/NEAA (essential amino acids/ nonessential amino acids) ratios in the substrates from low to high were as follows: wheat bran cereals, peanuts, collagen, zein, whey protein, sorghum, pigeon peas, and black beans. The results revealed sorghum, whey protein, and zein as good sources of BCAA. In all substrates, no intact protein from the substrates was visually detected by SDS-PAGE after the intestinal phase of in vitro digestion with the INFOGEST protocol. However, digestion-resistant peptides were detected in all substrates after the intestinal digestion phase. Protein hydrolysis was high in whey protein isolate and pigeon pea and low for wheat bran cereals and bovine collagen.},
keywords = {Amino acid, Digestion, Liquid chromatography-mass spectrometry peptides, Protein hydrolysis, proteins},
pubstate = {published},
tppubtype = {article}
}
In vitro digestion systems are valuable tools for understanding and monitoring the complex behavior of food degradation during digestion, thus proving to be good candidates for replacing in vivo assays. The aim of the present work was to study protein hydrolysis in a selection of different protein sources using the harmonized INFOGEST static protocol: three isolated proteins (collagen, zein, and whey protein) and five foods (sorghum flour, wheat bran cereals, peanuts, black beans, and pigeon peas). The proteins of all the substrates were analyzed by SDS-PAGE and HPLC-MS/MS. Individual amino acid composition was analyzed by high-performance liquid chromatography (HPLC). EAA/NEAA (essential amino acids/ nonessential amino acids) ratios in the substrates from low to high were as follows: wheat bran cereals, peanuts, collagen, zein, whey protein, sorghum, pigeon peas, and black beans. The results revealed sorghum, whey protein, and zein as good sources of BCAA. In all substrates, no intact protein from the substrates was visually detected by SDS-PAGE after the intestinal phase of in vitro digestion with the INFOGEST protocol. However, digestion-resistant peptides were detected in all substrates after the intestinal digestion phase. Protein hydrolysis was high in whey protein isolate and pigeon pea and low for wheat bran cereals and bovine collagen.
2019
Gil-Sánchez, Irene; Monge, Miguel; Miralles, Beatriz; Armentia, Gloria; Cueva, Carolina; Crespo, Julian; Luzuriaga, Jose M. López; Olmos, M. Elena; Bartolomé, Begoña; Llano, Dolores González; Moreno-Arribas, M Victoria
Some new findings on the potential use of biocompatible silver nanoparticles in winemaking Artículo de revista
En: Innovative Food Science & Emerging Technologies, vol. 51, pp. 64-72, 2019, ISSN: 1466-8564, (Innovations in Food Science and Technology at the Spanish National Research Council (CSIC)).
Resumen | Enlaces | BibTeX | Etiquetas: Caco-2 cell, Digestion, Silver nanoparticles, Sulphur dioxide alternatives, Wine bacteria
@article{GILSANCHEZ201964,
title = {Some new findings on the potential use of biocompatible silver nanoparticles in winemaking},
author = {Irene Gil-Sánchez and Miguel Monge and Beatriz Miralles and Gloria Armentia and Carolina Cueva and Julian Crespo and Jose M. López Luzuriaga and M. Elena Olmos and Begoña Bartolomé and Dolores González Llano and M Victoria Moreno-Arribas},
url = {https://www.sciencedirect.com/science/article/pii/S1466856418300195},
doi = {https://doi.org/10.1016/j.ifset.2018.04.017},
issn = {1466-8564},
year = {2019},
date = {2019-01-01},
urldate = {2019-01-01},
journal = {Innovative Food Science & Emerging Technologies},
volume = {51},
pages = {64-72},
abstract = {There is currently an increasing commercial demand for silver nanoparticles (Ag NPs) due to their wide applicability in various markets. Because of their powerful antimicrobial properties, these nanoparticles are frequently used for food-associated consumer products. In this paper, the effect of two Ag NPs coated with biocompatible materials – PEG-Ag NPs 20 (polyethylene glycol) and GSH-Ag NPs (reduced glutathione) – to control microbial growth in wines was assessed. Both Ag NPs were subjected to an in vitro three-step digestion, and changes in their morphology and an assessment of their cytotoxicity against Caco-2 cells were determined. Both Ag NPs were effective against the different microbial population present in tested wines. Regarding their in vitro digestion, the size and shape of the nanoparticles were almost unaltered in the case of GSH-Ag NPs, while in PEG-Ag NPs 20 some particle agglomeration was observed. Overall, these results suggest that Ag NPs may reach the intestine in a nano-scaled form. Finally, Caco-2 cell experiments seemed to exclude toxicity of Ag NPs at the intestinal epithelium.
Industrial relevance
Traditionally, sulphur dioxide (SO2) has been used by oenologists to control the microbial population in wine. As a result of increasing evidence of possible health risks associated with this additive in wine, there has been growing interest in finding new alternatives to replace it. Silver nanoparticles display a broad spectrum of antimicrobial activity, so they could constitute a very promising approach to reducing SO2 in winemaking.},
note = {Innovations in Food Science and Technology at the Spanish National Research Council (CSIC)},
keywords = {Caco-2 cell, Digestion, Silver nanoparticles, Sulphur dioxide alternatives, Wine bacteria},
pubstate = {published},
tppubtype = {article}
}
There is currently an increasing commercial demand for silver nanoparticles (Ag NPs) due to their wide applicability in various markets. Because of their powerful antimicrobial properties, these nanoparticles are frequently used for food-associated consumer products. In this paper, the effect of two Ag NPs coated with biocompatible materials – PEG-Ag NPs 20 (polyethylene glycol) and GSH-Ag NPs (reduced glutathione) – to control microbial growth in wines was assessed. Both Ag NPs were subjected to an in vitro three-step digestion, and changes in their morphology and an assessment of their cytotoxicity against Caco-2 cells were determined. Both Ag NPs were effective against the different microbial population present in tested wines. Regarding their in vitro digestion, the size and shape of the nanoparticles were almost unaltered in the case of GSH-Ag NPs, while in PEG-Ag NPs 20 some particle agglomeration was observed. Overall, these results suggest that Ag NPs may reach the intestine in a nano-scaled form. Finally, Caco-2 cell experiments seemed to exclude toxicity of Ag NPs at the intestinal epithelium.
Industrial relevance
Traditionally, sulphur dioxide (SO2) has been used by oenologists to control the microbial population in wine. As a result of increasing evidence of possible health risks associated with this additive in wine, there has been growing interest in finding new alternatives to replace it. Silver nanoparticles display a broad spectrum of antimicrobial activity, so they could constitute a very promising approach to reducing SO2 in winemaking.
Industrial relevance
Traditionally, sulphur dioxide (SO2) has been used by oenologists to control the microbial population in wine. As a result of increasing evidence of possible health risks associated with this additive in wine, there has been growing interest in finding new alternatives to replace it. Silver nanoparticles display a broad spectrum of antimicrobial activity, so they could constitute a very promising approach to reducing SO2 in winemaking.
2018
Bohn, T.; Carriere, F.; Day, L.; Deglaire, A.; Egger, L.; Freitas, D.; Golding, M.; Feunteun, S. Le; Macierzanka, A.; Menard, O.; Miralles, Beatriz; Moscovici, A.; Portmann, R.; Recio, Isidra; Rémond, D.; Santé-Lhoutelier, V.; Wooster, T. J.; Lesmes, U.; Mackie, A. R.; Dupont, D.
Correlation between in vitro and in vivo data on food digestion. What can we predict with static in vitro digestion models? Artículo de revista
En: Critical Reviews in Food Science and Nutrition, vol. 58, no 13, pp. 2239-2261, 2018, ISSN: 1040-8398.
Enlaces | BibTeX | Etiquetas: bioaccessibility, bioactive, bioavailability, Digestion, in vitro, in vivo, liquid, micronutrient, proteins
@article{Bohn2018,
title = {Correlation between in vitro and in vivo data on food digestion. What can we predict with static in vitro digestion models?},
author = {T. Bohn and F. Carriere and L. Day and A. Deglaire and L. Egger and D. Freitas and M. Golding and S. Le Feunteun and A. Macierzanka and O. Menard and Beatriz Miralles and A. Moscovici and R. Portmann and Isidra Recio and D. Rémond and V. Santé-Lhoutelier and T. J. Wooster and U. Lesmes and A. R. Mackie and D. Dupont},
url = {https://doi.org/10.1080/10408398.2017.1315362},
doi = {10.1080/10408398.2017.1315362},
issn = {1040-8398},
year = {2018},
date = {2018-09-02},
urldate = {2018-09-02},
journal = {Critical Reviews in Food Science and Nutrition},
volume = {58},
number = {13},
pages = {2239-2261},
publisher = {Taylor & Francis},
keywords = {bioaccessibility, bioactive, bioavailability, Digestion, in vitro, in vivo, liquid, micronutrient, proteins},
pubstate = {published},
tppubtype = {article}
}
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.
2016
Egger, Lotti; Ménard, Olivia; Delgado-Andrade, Cristina; Alvito, Paula; Assunção, Ricardo; Balance, Simon; Barberá, Reyes; Brodkorb, Andre; Cattenoz, Thomas; Clemente, Alfonso; Comi, Irene; Dupont, Didier; Garcia-Llatas, Guadalupe; Lagarda, María Jesús; Feunteun, Steven Le; JanssenDuijghuijsen, Lonneke; Karakaya, Sibel; Lesmes, Uri; Mackie, Alan R.; Martins, Carla; Meynier, Anne; Miralles, Beatriz; Murray, Brent S.; Pihlanto, Anne; Picariello, Gianluca; Santos, Claudia N.; Simsek, Sebnem; Recio, Isidra; Rigby, Neil; Rioux, Laurie-Eve; Stoffers, Helena; Tavares, Ana; Tavares, Lucelia; Turgeon, Sylvie; Ulleberg, Ellen K.; Vegarud, Gerd E.; Vergères, Guy; Portmann, Reto
The harmonized INFOGEST in vitro digestion method: From knowledge to action Artículo de revista
En: Food Research International, vol. 88, pp. 217-225, 2016, ISSN: 0963-9969, (The 4th International Conference on Food Digestion).
Resumen | Enlaces | BibTeX | Etiquetas: Dairy proteins, Digestion, Harmonized IVD protocol, Inter-laboratory trial, Mass spectrometry, peptides
@article{EGGER2016217,
title = {The harmonized INFOGEST in vitro digestion method: From knowledge to action},
author = {Lotti Egger and Olivia Ménard and Cristina Delgado-Andrade and Paula Alvito and Ricardo Assunção and Simon Balance and Reyes Barberá and Andre Brodkorb and Thomas Cattenoz and Alfonso Clemente and Irene Comi and Didier Dupont and Guadalupe Garcia-Llatas and María Jesús Lagarda and Steven Le Feunteun and Lonneke JanssenDuijghuijsen and Sibel Karakaya and Uri Lesmes and Alan R. Mackie and Carla Martins and Anne Meynier and Beatriz Miralles and Brent S. Murray and Anne Pihlanto and Gianluca Picariello and Claudia N. Santos and Sebnem Simsek and Isidra Recio and Neil Rigby and Laurie-Eve Rioux and Helena Stoffers and Ana Tavares and Lucelia Tavares and Sylvie Turgeon and Ellen K. Ulleberg and Gerd E. Vegarud and Guy Vergères and Reto Portmann},
url = {https://www.sciencedirect.com/science/article/pii/S0963996915302751},
doi = {https://doi.org/10.1016/j.foodres.2015.12.006},
issn = {0963-9969},
year = {2016},
date = {2016-01-01},
journal = {Food Research International},
volume = {88},
pages = {217-225},
abstract = {Within the active field of in vitro digestion in food research, the COST Action INFOGEST aimed to harmonize in vitro protocols simulating human digestion on the basis of physiologically inferred conditions. A harmonized static in vitro digestion (IVD) method was recently published as a primary output from this network. To validate this protocol, inter-laboratory trials were conducted within the INFOGEST network. A first study was performed using skim milk powder (SMP) as a model food and served to compare the different in-house digestion protocols used among the INFOGEST members. In a second inter-laboratory study applying the harmonized protocol, the degree of consistency in protein hydrolysis was investigated. Analysis of the hydrolyzed proteins, after the gastric and intestinal phases, showed that caseins were mainly hydrolyzed during the gastric phase, whereas β-lactoglobulin was, as previously shown, resistant to pepsin. Moreover, generation of free amino acids occurred mainly during the intestinal phase. The study also showed that a few critical steps were responsible for the remaining inter-laboratory variability. The largest deviations arose from the determination of pepsin activity. Therefore, this step was further clarified, harmonized, and implemented in a third inter-laboratory study. The present work gives an overview of all three inter-laboratory studies, showing that the IVD INFOGEST method has led to an increased consistency that enables a better comparability of in vitro digestion studies in the future.},
note = {The 4th International Conference on Food Digestion},
keywords = {Dairy proteins, Digestion, Harmonized IVD protocol, Inter-laboratory trial, Mass spectrometry, peptides},
pubstate = {published},
tppubtype = {article}
}
Within the active field of in vitro digestion in food research, the COST Action INFOGEST aimed to harmonize in vitro protocols simulating human digestion on the basis of physiologically inferred conditions. A harmonized static in vitro digestion (IVD) method was recently published as a primary output from this network. To validate this protocol, inter-laboratory trials were conducted within the INFOGEST network. A first study was performed using skim milk powder (SMP) as a model food and served to compare the different in-house digestion protocols used among the INFOGEST members. In a second inter-laboratory study applying the harmonized protocol, the degree of consistency in protein hydrolysis was investigated. Analysis of the hydrolyzed proteins, after the gastric and intestinal phases, showed that caseins were mainly hydrolyzed during the gastric phase, whereas β-lactoglobulin was, as previously shown, resistant to pepsin. Moreover, generation of free amino acids occurred mainly during the intestinal phase. The study also showed that a few critical steps were responsible for the remaining inter-laboratory variability. The largest deviations arose from the determination of pepsin activity. Therefore, this step was further clarified, harmonized, and implemented in a third inter-laboratory study. The present work gives an overview of all three inter-laboratory studies, showing that the IVD INFOGEST method has led to an increased consistency that enables a better comparability of in vitro digestion studies in the future.
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