Publicaciones

@article{FONTESCANDIA2022107505,

title = {Development of polysaccharide-casein gel-like structures resistant to in vitro gastric digestion},

author = {Cynthia Fontes-Candia and Pablo Jiménez-Barrios and Beatriz Miralles and Isidra Recio and Amparo López-Rubio and Marta Martínez-Sanz},

url = {https://www.sciencedirect.com/science/article/pii/S0268005X2200025X},

doi = {https://doi.org/10.1016/j.foodhyd.2022.107505},

issn = {0268-005X},

year  = {2022},

date = {2022-01-01},

urldate = {2022-01-01},

journal = {Food Hydrocolloids},

volume = {127},

pages = {107505},

abstract = {Controlling protein digestion is a promising strategy to modulate hormonal responses involved in satiety and appetite regulation. In this context, polysaccharide-casein gel-like structures have been developed and subjected to in-vitro gastrointestinal digestions to evaluate their potential for delaying casein hydrolysis. The effect of the polysaccharide type (agar vs. κ-carrageenan), the polysaccharide:casein ratio and the physical state of the structures (hydrogels vs. aerogels) on the protection ability was investigated. The microstructure evolution of the materials upon the digestions was studied and the molecular weight distribution and peptidomic profile of the digestion products were also determined. During the gastric phase most of the developed structures exerted a protective effect and intact casein clusters were even detected in some of the formulations. In contrast, during the intestinal phase most of the casein was released and hydrolysed to a certain extent. In general, the hydrogels showed a greater protective effect than the aerogels, due to a limited diffusion of the protein towards the liquid medium. Moreover, a higher polysaccharide:protein ratio produced stronger gel networks which provided greater protection. In particular, agar-based and κ-carrageenan hydrogels with 25% polysaccharide and agar-based aerogels with 75% polysaccharide would be the most optimum for delaying casein digestion, since they were able to preserve intact casein after the gastric phase while promoting the release of peptides during the intestinal phase.},

keywords = {Aerogels, bioactive proteins, body mass index, Controlled digestibility, Human milk, Hydrogels, in vitro infant digestion, MALDI mass spectrometry, Simulated gastrointestinal digestion, Sulphated polysaccharides},

pubstate = {published},

tppubtype = {article}

}

@article{GALLO2022112713,

title = {Physicochemical properties, structure and digestibility in simulated gastrointestinal environment of bread added with green lentil flour},

author = {Veronica Gallo and Annalisa Romano and Beatriz Miralles and Pasquale Ferranti and Paolo Masi and Marta Santos-Hernández and Isidra Recio},

url = {https://www.sciencedirect.com/science/article/pii/S0023643821018661},

doi = {https://doi.org/10.1016/j.lwt.2021.112713},

issn = {0023-6438},

year  = {2022},

date = {2022-01-01},

journal = {LWT},

volume = {154},

pages = {112713},

abstract = {Aim of this work was to evaluate the impact of bread enrichment with different concentrations of lentil flour (LF) (0 g/100g, 10 g/100g and 20 g/100g) on some physico-chemical, structural, and nutritional features of bread. The addition of LF in formulation affected its properties, leading to a darker appearance and to a more compact structure (e.g., higher density and lower gas bubble area fraction). Besides, it led to a significant rise in the protein, free glucose, and rapidly digestible starch content as well as in the expected glycemic index. Concerning the investigation of nutritional properties, starch and protein digestibility has been evaluated by the combination of different digestion models. Each type of bread was subjected to an in vivo oral phase followed by a semi-dynamic in vitro gastrointestinal digestion. During the oral and the gastric phases of digestion, bread with the greatest LF content (20 g/100g) exhibited an extensive starch digestibility and a partial protein digestibility compared to the other samples, due to its higher protein content. In contrast, during the intestinal phase, control (0 g/100g) showed a stronger starch digestibility compared with the LF samples, while no differences could be observed in terms of protein digestibility investigated by SDS-PAGE.},

keywords = {Bread, Green lentil flour, INFOGEST, Simulated gastrointestinal digestion, Wheat flour},

pubstate = {published},

tppubtype = {article}

}

@article{https://doi.org/10.1002/jsfa.9294,

title = {Release of multifunctional peptides from kiwicha (Amaranthus caudatus) protein under in vitro gastrointestinal digestion},

author = {Rubén Vilcacundo and Cristina Martínez-Villaluenga and Beatriz Miralles and Blanca Hernández-Ledesma},

url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.9294},

doi = {https://doi.org/10.1002/jsfa.9294},

year  = {2019},

date = {2019-01-01},

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

volume = {99},

number = {3},

pages = {1225-1232},

abstract = {Abstract BACKGROUND The multifactorial origin of many chronic diseases provides a new framework for the development of multifunctional foods. In this study, the effect of in vitro simulated gastrointestinal digestion of kiwicha (Amaranthus caudatus) proteins on the release of multifunctional peptides was evaluated. RESULTS Gastric digest showed higher angiotensin I converting enzyme (ACE) inhibitory activity while 60 min gastroduodenal digest showed the highest antioxidant, dipeptidyl peptidase IV (DPP-IV), α-amylase and Caco-2 cell viability inhibitory activities. Peptides >5 kDa were more effective in inhibiting colon cancer cell viability, whereas peptides <5 kDa were mainly responsible for the antioxidant, ACE, DPP-IV and α-amylase inhibitory activities. Thirteen peptides from amaranth sequenced proteins were identified. Structure–activity relationship analysis of the identified sequences pointed to three amaranth fragments, namely FLISCLL, SVFDEELS and DFIILE, as potential peptides able to concurrently exert antioxidant capacity and ability to inhibit both ACE and α-amylase. CONCLUSIONS Five of thirteen peptides identified in kiwicha protein digests show high potential to exert multifunctional properties. Thus kiwicha proteins might start to gain importance as ingredients for functional foods for the prevention and/or management of chronic diseases related to oxidative stress, hypertension and/or diabetes. © 2018 Society of Chemical Industry},

keywords = {bioactive peptides, kiwicha, multifunctional activity, Simulated gastrointestinal digestion},

pubstate = {published},

tppubtype = {article}

}

@article{VILCACUNDO2018403,

title = {In vitro chemopreventive properties of peptides released from quinoa (Chenopodium quinoa Willd.) protein under simulated gastrointestinal digestion},

author = {Rubén Vilcacundo and Beatriz Miralles and Wilman Carrillo and Blanca Hernández-Ledesma},

url = {https://www.sciencedirect.com/science/article/pii/S0963996917308062},

doi = {https://doi.org/10.1016/j.foodres.2017.11.036},

issn = {0963-9969},

year  = {2018},

date = {2018-01-01},

journal = {Food Research International},

volume = {105},

pages = {403-411},

abstract = {Because of the continuous and direct interaction between the digestive tract and foods, dietary compounds represent an interesting source of chemopreventive agents for gastrointestinal health. In this study, the influence of a standardized static in vitro gastrointestinal digestion model on the release of peptides with chemopreventive potential from quinoa protein was investigated. Gastroduodenal digests and fractions collected by ultrafiltration were evaluated for their in plate oxygen radical absorbance capacity and in vitro colon cancer cell viability inhibitory activity. Highest effects were observed in the digests obtained during the intestinal phase, with fraction containing peptides <5kDa as the main responsible for the antioxidant activity and peptides >5kDa showing the greatest anti-cancer effects. Seventeen potential bioactive peptides derived from quinoa proteins have been identified. These proteins might be utilized as new ingredients in the development of functional foods or nutraceuticals with the aim of reducing oxidative stress-associated diseases, including cancer.},

keywords = {Antioxidant, bioactive peptides, colon cancer cell viability, Quinoa protein, Simulated gastrointestinal digestion},

pubstate = {published},

tppubtype = {article}

}

@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}

}

@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}

}