Publicaciones

@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}

}

@article{Moreno-Montoro2018,

title = {Bioaccessible peptides released by in vitro gastrointestinal digestion of fermented goat milks},

author = {Miriam Moreno-Montoro and Paula Jauregi and Miguel Navarro-Alarcón and Manuel Olalla-Herrera and Rafael Giménez-Martínez and Lourdes Amigo and Beatriz Miralles},

url = {https://doi.org/10.1007/s00216-018-0983-0},

doi = {10.1007/s00216-018-0983-0},

issn = {1618-2650},

year  = {2018},

date = {2018-06-01},

urldate = {2018-06-01},

journal = {Analytical and Bioanalytical Chemistry},

volume = {410},

number = {15},

pages = {3597-3606},

abstract = {In this study, ultrafiltered goat milks fermented with the classical starter bacteria Lactobacillus delbrueckii subsp. bulgaricus and Streptococcus salivarus subsp. thermophilus or with the classical starter plus the Lactobacillus plantarum C4 probiotic strain were analyzed using ultra-high performance liquid chromatography-quadrupole-time-of-flight tandem mass spectrometry (UPLC-Q-TOF-MS/MS) and/or high performance liquid chromatography-ion trap (HPLC-IT-MS/MS). Partial overlapping of the identified sequences with regard to fermentation culture was observed. Evaluation of the cleavage specificity suggested a lower proteolytic activity of the probiotic strain. Some of the potentially identified peptides had been previously reported as angiotensin-converting enzyme (ACE) inhibitory, antioxidant, and antibacterial and might account for the in vitro activity previously reported for these fermented milks. Simulated digestion of the products was conducted in the presence of a dialysis membrane to retrieve the bioaccessible peptide fraction. Some sequences with reported physiological activity resisted digestion but were found in the non-dialyzable fraction. However, new forms released by digestion, such as the antioxidant $alpha$s1-casein 144YFYPQL149, the antihypertensive $alpha$s2-casein 90YQKFPQY96, and the antibacterial $alpha$s2-casein 165LKKISQ170, were found in the dialyzable fraction of both fermented milks. Moreover, in the fermented milk including the probiotic strain, the k-casein dipeptidyl peptidase IV inhibitor (DPP-IV) 51INNQFLPYPY60 as well as additional ACE inhibitory or antioxidant sequences could be identified. With the aim of anticipating further biological outcomes, quantitative structure activity relationship (QSAR) analysis was applied to the bioaccessible fragments and led to potential ACE inhibitory sequences being proposed.},

keywords = {Bioaccessible peptides, Fermented goat’s milk, Gastrointestinal digestion, Peptidomics, Tandem mass spectrometry},

pubstate = {published},

tppubtype = {article}

}

@article{FERNANDEZTOME2018101,

title = {Transepithelial transport of lunasin and derived peptides: Inhibitory effects on the gastrointestinal cancer cells viability},

author = {Samuel Fernández-Tomé and Javier Sanchón and Isidra Recio and Blanca Hernández-Ledesma},

url = {https://www.sciencedirect.com/science/article/pii/S0889157517300285},

doi = {https://doi.org/10.1016/j.jfca.2017.01.011},

issn = {0889-1575},

year  = {2018},

date = {2018-01-01},

journal = {Journal of Food Composition and Analysis},

volume = {68},

pages = {101-110},

abstract = {Lunasin is a soybean peptide with demonstrated chemopreventive properties. Upon its oral intake, studies dealing with the effect of the digestive process on lunasin’s properties are crucial. The present study describes, for the first time, the behavior of lunasin and fragments derived from its digestion in the Caco-2 cell monolayer. The sequences SKWQHQQDSC and KIQGRGDDDDDDDDD showed a notable resistance against the epithelial brush-border peptidases, although some fragments were generated as cellular hydrolysis products. Lunasin and RKQLQGVN were absorbed intact across the intestinal epithelium. The tight junction disruptor cytochalasin D increased their transport, suggesting that the paracellular passive diffusion was the main mechanism involved. The study on the cancer cells viability showed that lunasin and SKWQHQQDSC exerted the highest effects on colorectal cancer HT-29 cells. The stability assay suggested that the cell line type was determinant in the behavior of lunasin added to the culture medium, and therefore in the anti-proliferative activity of released fragments.},

note = {Bioaccessibility and bioavailability of food components and contaminants},

keywords = {Caco-2 cells transport, Cancer cells, Cell viability, Food analysis, Food composition, Gastrointestinal digestion, Lunasin-fragments, Peptide lunasin},

pubstate = {published},

tppubtype = {article}

}

@article{Picariello2015,

title = {Role of intestinal brush border peptidases in the simulated digestion of milk proteins},

author = {Gianluca Picariello and Beatriz Miralles and Gianfranco Mamone and Laura Sánchez-Rivera and Isidra Recio and Francesco Addeo and Pasquale Ferranti},

url = {https://doi.org/10.1002/mnfr.201400856},

doi = {10.1002/mnfr.201400856},

issn = {1613-4125},

year  = {2015},

date = {2015-05-01},

urldate = {2015-05-01},

journal = {Molecular Nutrition & Food Research},

volume = {59},

number = {5},

pages = {948-956},

publisher = {John Wiley & Sons, Ltd},

abstract = {Scope This study aimed to assess the impact of the ?often neglected? intestinal brush border membranes (BBMs) hydrolases on dietary peptides, exploring the possibility that the disintegration of proteins progressed in the small intestine up to a ?core? of intrinsically stable oligopeptides, persisting independently on the up-stream breakdown. Methods and results Samples of sodium caseinate, skim milk powder, and whey protein isolate were submitted to in vitro simulated gastropancreatic digestion using two different procedures: (i) a simplified model involving the main compartmental specific proteases; (ii) a static digestion method based on a frameset of parameters inferred from in vivo. The gastroduodenal digesta were further hydrolyzed with peptidases from porcine jejunal BBM. The peptidomes arising from the two digestion models, characterized by combined HPLC and MS techniques, differed to some extent. However, only specific protein domains survived digestion, among which are potential bioactive or immunogenic (food allergy) peptides. The degree of hydrolysis (DH) after BBM digestion (70?77%) practically did not differ between the digestion models and significantly increased the DH after duodenal steps. Conclusion Any in vitro digestion model should be supplemented with a jejunal phase to realistically determine the bioaccessibility and bioavailability of dietary peptides.},

keywords = {brush border membrane hydrolases, degree of hydrolysis, Gastrointestinal digestion, in vitro digestion models, milk protreins},

pubstate = {published},

tppubtype = {article}

}