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.
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.
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.
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.
Gómez-Gallego, C.; Recio, Isidra; Gómez-Gómez, V.; Ortuño, I.; Bernal, M. J.; Ros, G.; Periago, M. J.
Effect of processing on polyamine content and bioactive peptides released after in vitro gastrointestinal digestion of infant formulas Artículo de revista
En: Journal of Dairy Science, vol. 99, no 2, pp. 924-932, 2016, ISSN: 0022-0302.
Resumen | Enlaces | BibTeX | Etiquetas: Infant formulas, Mass spectrometry, peptide, polyamine, Simulated gastrointestinal digestion
@article{GOMEZGALLEGO2016924,
title = {Effect of processing on polyamine content and bioactive peptides released after in vitro gastrointestinal digestion of infant formulas},
author = {C. Gómez-Gallego and Isidra Recio and V. Gómez-Gómez and I. Ortuño and M. J. Bernal and G. Ros and M. J. Periago},
url = {https://www.journalofdairyscience.org/article/S0022-0302(15)00890-5/fulltext},
doi = {https://doi.org/10.3168/jds.2015-10030},
issn = {0022-0302},
year = {2016},
date = {2016-01-01},
urldate = {2016-01-01},
journal = {Journal of Dairy Science},
volume = {99},
number = {2},
pages = {924-932},
abstract = {This study examined the influence of processing on polyamines and peptide release after the digestion of a commercial infant formula designed for children during the first months of life. Polyamine oxidase activity was not suppressed during the manufacturing process, which implicates that polyamine concentrations were reduced over time and during infant formula self-life. In gel electrophoresis, in vitro gastrointestinal digestion of samples with reduced amount of enzymes and time of digestion shows an increase in protein digestibility, reflected in the increase in nonprotein nitrogen after digestion and the disappearance of β-lactoglobulin and α-lactalbumin bands in gel electrophoresis. Depending on the sample, between 22 and 87 peptides were identified after gastrointestinal digestion. A peptide from β-casein f(98–105) with the sequence VKEAMAPK and antioxidant activity appeared in all of the samples. Other peptides with antioxidant, immunomodulatory, and antimicrobial activities were frequently found, which could have an effect on infant health. The present study confirms that the infant formula manufacturing process determines the polyamine content and peptidic profile after digestion of the infant formula. Because compositional dissimilarity between human milk and infant formula in polyamines and proteins could be responsible for some of the differences in health reported between breast-fed and formula-fed children, these changes must be taken into consideration because they may have a great effect on infant nutrition and development.},
keywords = {Infant formulas, Mass spectrometry, peptide, polyamine, Simulated gastrointestinal digestion},
pubstate = {published},
tppubtype = {article}
}
This study examined the influence of processing on polyamines and peptide release after the digestion of a commercial infant formula designed for children during the first months of life. Polyamine oxidase activity was not suppressed during the manufacturing process, which implicates that polyamine concentrations were reduced over time and during infant formula self-life. In gel electrophoresis, in vitro gastrointestinal digestion of samples with reduced amount of enzymes and time of digestion shows an increase in protein digestibility, reflected in the increase in nonprotein nitrogen after digestion and the disappearance of β-lactoglobulin and α-lactalbumin bands in gel electrophoresis. Depending on the sample, between 22 and 87 peptides were identified after gastrointestinal digestion. A peptide from β-casein f(98–105) with the sequence VKEAMAPK and antioxidant activity appeared in all of the samples. Other peptides with antioxidant, immunomodulatory, and antimicrobial activities were frequently found, which could have an effect on infant health. The present study confirms that the infant formula manufacturing process determines the polyamine content and peptidic profile after digestion of the infant formula. Because compositional dissimilarity between human milk and infant formula in polyamines and proteins could be responsible for some of the differences in health reported between breast-fed and formula-fed children, these changes must be taken into consideration because they may have a great effect on infant nutrition and development.
2015
Sánchez-Rivera, Laura; Ménard, Olivia; Recio, Isidra; Dupont, Didier
Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder Artículo de revista
En: Food Research International, vol. 77, pp. 132-139, 2015, ISSN: 0963-9969, (FOOD BIOACTIVE COMPOUNDS: QUALITY CONTROL AND BIOACTIVITY).
Resumen | Enlaces | BibTeX | Etiquetas: Dynamic digestion, Heat treatment, Mass spectrometry, Peptidomics
@article{SANCHEZRIVERA2015132,
title = {Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder},
author = {Laura Sánchez-Rivera and Olivia Ménard and Isidra Recio and Didier Dupont},
url = {https://www.sciencedirect.com/science/article/pii/S0963996915301381},
doi = {https://doi.org/10.1016/j.foodres.2015.08.001},
issn = {0963-9969},
year = {2015},
date = {2015-01-01},
urldate = {2015-01-01},
journal = {Food Research International},
volume = {77},
pages = {132-139},
abstract = {This study aims to evaluate the impact of heat treatment on the hydrolysis kinetics of cow milk proteins and on the peptide release during in vitro dynamic gastric digestion. SDS-PAGE and ELISA techniques were employed to assess the hydrolysis of proteins over time of digestion. The evolution of the peptidome generated through dynamic digestion of heated and non-heated milk was studied at different times, using MS-based techniques (ion trap and MALDI-TOF/TOF) coupled to liquid chromatography. The peptide homology value between both samples at the end of digestion (48%) confirmed the impact of heat treatment on the identity of peptides generated during digestion, despite their identical initial protein content and being the same matrix in both cases. Heat treatment produced an increased resistance to hydrolysis by pepsin in the casein fraction. However, β-lactoglobulin was found to be more susceptible to hydrolysis. Although differences on the pattern of peptide release were found between both samples, also some common traits after digestion were observed. The regions comprised between the residues 76–93 of β-casein, where several binding epitopes are included, as well as the β-casein domains 126–140 and 190–209 were found to be resistant to pepsin.},
note = {FOOD BIOACTIVE COMPOUNDS: QUALITY CONTROL AND BIOACTIVITY},
keywords = {Dynamic digestion, Heat treatment, Mass spectrometry, Peptidomics},
pubstate = {published},
tppubtype = {article}
}
This study aims to evaluate the impact of heat treatment on the hydrolysis kinetics of cow milk proteins and on the peptide release during in vitro dynamic gastric digestion. SDS-PAGE and ELISA techniques were employed to assess the hydrolysis of proteins over time of digestion. The evolution of the peptidome generated through dynamic digestion of heated and non-heated milk was studied at different times, using MS-based techniques (ion trap and MALDI-TOF/TOF) coupled to liquid chromatography. The peptide homology value between both samples at the end of digestion (48%) confirmed the impact of heat treatment on the identity of peptides generated during digestion, despite their identical initial protein content and being the same matrix in both cases. Heat treatment produced an increased resistance to hydrolysis by pepsin in the casein fraction. However, β-lactoglobulin was found to be more susceptible to hydrolysis. Although differences on the pattern of peptide release were found between both samples, also some common traits after digestion were observed. The regions comprised between the residues 76–93 of β-casein, where several binding epitopes are included, as well as the β-casein domains 126–140 and 190–209 were found to be resistant to pepsin.
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