Publicaciones

@article{Carrillo2018-ku,

title = {Antiulcerative Activity of Milk Proteins Hydrolysates},

author = {Wilman Carrillo and Karin Maia Monteiro and Daniel Mart'inez-Maqueda and Mercedes Ramos and Isidra Recio and Jo ao Ernesto de Carvalho},

url = {https://www.liebertpub.com/doi/10.1089/jmf.2017.0087},

doi = {https://doi.org/10.1089/jmf.2017.0087},

year  = {2018},

date = {2018-04-01},

urldate = {2018-04-01},

journal = {Journal of Medicinal Food},

volume = {21},

number = {4},

pages = {408--415},

publisher = {Mary Ann Liebert, Inc., publishers},

abstract = {Abstract Several studies have shown the protective effect of 

 dairy products, especially $alpha$-lactalbumin and derived 

 hydrolysates, against induced gastric ulcerative lesions. The 

 mucus strengthening represents an important mechanism in the 

 defense of gastrointestinal mucosa. Previously, a hydrolysate 

 from casein (CNH) and a hydrolysate from whey protein 

 concentrate rich in ?-lactoglobulin (WPH) demonstrated a 

 stimulatory activity on mucus production in intestinal goblet 

 cells. The aim of this work was to evaluate the possible 

 antiulcerative activity of these two hydrolysates in an 

 ethanol-induced ulcer model in rats. All tested samples 

 significantly reduced the ulcerative lesions index (ULI), 

 compared with the saline solution, using doses of 300 and 

 1000?mg kg?1 body weight with decreases up to 66.3% ULI. A 

 dose?response relationship was found for both hydrolysates. The 

 involvement of endogenous sulfhydryl (SH) groups and 

 prostaglandins (PGs) in the antiulcerative activity was 

 evaluated using their blockage. The antiulcerative activity of 

 WPH showed a drastic decrease in presence of N-ethylmaleimide 

 (from 41.4% to 9.2% ULI). However, the CNH antiulcerative 

 properties were not significantly affected. The cytoprotective 

 effect of WPH appears to depend on a PG-mediated mechanism. In 

 conclusion, CNH and WPH demonstrated in vivo antiulcerative 

 properties and represent a promising alternative as protectors 

 of the gastric mucosa.},

keywords = {antiulcerative activity, casein hydrolysate, peptides, rat model, whey protein hydrolysate},

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{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{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}

}