Publicaciones

@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{https://doi.org/10.1002/jsfa.8668,

title = {Dynamic gastric digestion of a commercial whey protein concentrate†},

author = {Beatriz Miralles and Roberto Barrio and Carolina Cueva and Isidra Recio and Lourdes Amigo},

url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.8668},

doi = {https://doi.org/10.1002/jsfa.8668},

year  = {2018},

date = {2018-01-01},

journal = {Journal of the Science of Food and Agriculture},

volume = {98},

number = {5},

pages = {1873-1879},

abstract = {Abstract BACKGROUND A dynamic gastrointestinal simulator, simgi®, has been applied to assess the gastric digestion of a whey protein concentrate. Samples collected from the outlet of the stomach have been compared to those resulting from the static digestion protocol INFOGEST developed on the basis of physiologically inferred conditions. RESULTS Progress of digestion was followed by SDS-PAGE and LC–MS/MS. By SDS-PAGE, serum albumin and α-lactalbumin were no longer detectable at 30 and 60 min, respectively. On the contrary, β-lactoglobulin was visible up to 120 min, although in decreasing concentrations in the dynamic model due to the gastric emptying and the addition of gastric fluids. Moreover, β-lactoglobulin was partly hydrolysed by pepsin probably due to the presence of heat-denatured forms and the peptides released using both digestion models were similar. Under dynamic conditions, a stepwise increase in number of peptides over time was observed, while the static protocol generated a high number of peptides from the beginning of digestion. CONCLUSION Whey protein digestion products using a dynamic stomach are consistent with those generated with the static protocol but the kinetic behaviour of the peptide profile emphasises the effect of the sequential pepsin addition, peristaltic shaking, and gastric emptying on protein digestibility. © 2017 Society of Chemical Industry},

keywords = {dynamic gastric digestion model, INFOGEST static digestion protocol, peptides, simgi®, Tandem mass spectrometry, whey proteins},

pubstate = {published},

tppubtype = {article}

}

@article{Bounouala2017,

title = {Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity},

author = {Fatima Zohra Bounouala and Salima Roudj and Nour-Eddine Karam and Isidra Recio and Beatriz Miralles},

url = {https://doi.org/10.1021/acs.jafc.7b03203},

doi = {10.1021/acs.jafc.7b03203},

issn = {0021-8561},

year  = {2017},

date = {2017-10-25},

urldate = {2017-10-25},

journal = {Journal of Agricultural and Food Chemistry},

volume = {65},

number = {42},

pages = {9324-9332},

publisher = {American Chemical Society},

keywords = {bioactive peptides, casein hydrolysate, enzyme specificity, lactic acid bacteria, QSAR, sheep milk, Tandem mass spectrometry},

pubstate = {published},

tppubtype = {article}

}

@article{SILVA2017140,

title = {Identification of peptides released from flaxseed (Linum usitatissimum) protein by Alcalase® hydrolysis: Antioxidant activity},

author = {Fernanda Guimarães Drummond Silva and Blanca Hernández-Ledesma and Lourdes Amigo and Flavia Maria Netto and Beatriz Miralles},

url = {https://www.sciencedirect.com/science/article/pii/S002364381630651X},

doi = {https://doi.org/10.1016/j.lwt.2016.10.049},

issn = {0023-6438},

year  = {2017},

date = {2017-01-01},

journal = {LWT - Food Science and Technology},

volume = {76},

pages = {140-146},

abstract = {In this study, the hydrolysis of a flaxseed protein isolate with Alcalase® was performed as a strategy to generate antioxidant peptides. A chromatographic separation of the hydrolysate was conducted by RP-HPLC. Both hydrolysate and six collected fractions were subjected to ORAC and FRAP assays to evaluate their antioxidant capacity. The higher antioxidant values were shown by fractions containing predominantly low molecular weight peptides, as it was demonstrated by MALDI analysis. Four peptides were identified by LC-MS/MS and one by Edman degradation. The peptide with sequence GFPGRLDHWCASE was synthesised showing a notable ORAC activity, 3.20 μmol Trolox equivalents/μmol of peptide. This value was higher than that reported for butylated hydroxyanisole. Therefore, the contribution of this peptide to the activity of the fraction where it had been found was 61%. The identified sequences represent an advance in the molecular characterization of the flaxseed protein fraction.},

keywords = {Alcalase hydrolysis, Antioxidant capacity, Flaxseed, peptides, Tandem mass spectrometry},

pubstate = {published},

tppubtype = {article}

}

@article{SANCHEZRIVERA2016348,

title = {Peptide fragments from β-casein f(134–138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity},

author = {Laura Sánchez-Rivera and Pedro Ferreira Santos and Beatriz Miralles and Rosalía Carrón and M José Montero and Isidra Recio},

url = {https://www.sciencedirect.com/science/article/pii/S0963996915302775},

doi = {https://doi.org/10.1016/j.foodres.2015.12.007},

issn = {0963-9969},

year  = {2016},

date = {2016-01-01},

urldate = {2016-01-01},

journal = {Food Research International},

volume = {88},

pages = {348-353},

abstract = {The intact absorption of a β-casein peptide, HLPLP, into rat blood circulation after oral administration was recently demonstrated. In addition to the parent peptide, several derived fragments were detected in rat plasma. The aim of the present work is to elucidate whether these fragments retain antihypertensive activity and if their activity is mediated by angiotensin-converting-enzyme inhibition. The penta-peptide was incubated in rat plasma in order to identify and quantify the fragments generated by the action of plasmatic peptidases on HLPLP, using tandem mass spectrometry. Peptides HLPL, LPLP and HLP were generated within seconds of incubation. The parent peptide, HLPLP, and all possible derived peptides showed potent antihypertensive activity in spontaneously hypertensive rats and caused inhibition of vascular contraction elicited by angiotensin-I. It can be concluded that the antihypertensive effect of HLPLP can be produced by the concomitant action of the parent peptide and several novel derived fragments.},

note = {The 4th International Conference on Food Digestion},

keywords = {antihypertensive peptide, In vivo active form, Plasma peptidases, SHR, Tandem mass spectrometry},

pubstate = {published},

tppubtype = {article}

}

@article{CRUZHUERTA2015648,

title = {Caseinophosphopeptides released after tryptic hydrolysis versus simulated gastrointestinal digestion of a casein-derived by-product},

author = {E. Cruz-Huerta and M. J. García-Nebot and Beatriz Miralles and Isidra Recio and L. Amigo},

url = {https://www.sciencedirect.com/science/article/pii/S0308814614011388},

doi = {https://doi.org/10.1016/j.foodchem.2014.07.090},

issn = {0308-8146},

year  = {2015},

date = {2015-01-01},

urldate = {2015-01-01},

journal = {Food Chemistry},

volume = {168},

pages = {648-655},

abstract = {The production of caseinophosphopeptides from a casein-derived by-product generated during the manufacture of a functional ingredient based on antihypertensive peptides was attempted. The casein by-product was submitted to tryptic hydrolysis for 30, 60 and 120min and further precipitated with calcium chloride and ethanol at pH 4.0, 6.0 and 8.0. Identification and semi quantification of the derived products by tandem mass spectrometry revealed some qualitative and quantitative changes in the released caseinophosphopeptides over time at the different precipitation pHs. The by-product was also subjected to simulated gastrointestinal digestion. Comparison of the resulting peptides showed large sequence homology in the phosphopeptides released by tryptic hydrolysis and simulated gastrointestinal digestion. Some regions, specifically αS1-CN 43-59, αS1-CN 60-74, β-CN 1-25 and β-CN 30-50 showed resistance to both tryptic hydrolysis and simulated digestion. The results of the present study suggest that this casein-derived by-product can be used as a source of CPPs.},

keywords = {Casein by-product, Caseinophosphopeptides, Simulated gastrointestinal digestion, Tandem mass spectrometry, Tryptic hydrolysis},

pubstate = {published},

tppubtype = {article}

}