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Whey is an abundantand sustainable source of bioactive peptides obtained from cheese making process. Whey proteins such as α-lactalbumin can be biologically active when the bioactive peptides encrypted in the amino acid sequence of the native protein are released by enzymatic hydrolysis. In the present work, the identification, sequence analysis, and antioxidant activity of bioaccessible peptides from α-lactalbumin alcalase-hydrolysate was assessed. Antioxidant activity (ABTS, ORAC, and HORAC) of α-lactalbumin showed a significant increase (p < 0.05) after the enzymatic treatment with alcalase and this capacity increased even more after the simulation of the gastrointestinal digestion process. Peptides contained in the gastrointestinal digest of α-lactalbumin hydrolysate were separated by preparative RP-HPLC (55 fractions), and three peptides were identified by LC-MS/MS analysis from selected fractions: IWCKDDQNPH (MW: 1254.54 Da) f(59-68), KFLDDDLTDDIM (MW: 1439.64 Da) f(79-90), DKFLDDDLTDDIM (MW: 1554.67 Da) f(78-90). Among the chemically synthesized peptides, IWCKDDQNPH showed the highest antioxidant capacity determined by ORAC, ABTS, and HORAC assays (IC50 0.015 ± 0.002, 0.45 ± 0.02, and 1.30 ± 0.05 mg/ml, respectively) and this activity may be related to the amino acid sequence. This is the first report where these bioaccessible peptides from α-lactalbumin hydrolysate were identified. The α-lactalbumin hydrolysate could be employed as a functional antioxidant ingredient. PRACTICAL APPLICATION: The present work studied the bioaccessibility of antioxidant peptides from an α-lactalbumin alcalase-hydrolysate by identifying three novel bioaccessible peptides responsible for the antioxidant capacity, providing evidence of the hydrolysate potential as an antioxidant ingredient in the formulations of functional foods and/or food supplements.

Bacterial, nutritional, and bioactive compositions of fermented sweet potato leaves (SPL) were investigated. Three samples were utilized: control (C), natural fermentation (NF), and probiotic fermentation (PF). Bacterial composition was assessed by high-throughput sequencing. Lactobacillus plantarum and Enterococcus durans were identified in NF. Lactobacillus plantarum was also found in PF, showing a relative abundance of 90.2%. Polyphenol composition determined by HPLC changed considerably during NF decreasing its concentration to a value of 6.69 mg/g dw compared to the value found in C (42.77 mg/g dw). PF maintained the polyphenol concentration (38.64 mg/g dw) but some interconversion between polyphenols seems to occur. ABTS radical scavenging capacity value was similar in C and PF, demonstrating no changes in antioxidant activity. During PF antioxidant activity was maintained, and angiotensin-converting enzyme inhibitory activity was even improved. Fermentation was a good process for SPL. According to the parameters assessed, PF was better than NF. Novelty impact statement: The effect of natural and probiotic fermentations on the bacterial composition, nutritional, and bioactive composition of sweet potato leaves was compared. Results showed that fermentation was a good process for sweet potato leaves. According to the parameters assessed, probiotic fermentation was better than natural fermentation., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

The objective of this study was to formulate a beverage based on amaranth proteins, stable and nutritious. The process of obtaining the beverage was based on the existing knowledge about starch separation techniques and techno-functional properties of the amaranth proteins. Gums, gellan and xanthan were added to the protein extract and it was heat-treated at 80 °C during 20 min. A beverage with a composition similar to skim cow’s milk was obtained (3.42 ± 0.08; 0.60 ± 0.06; 1.9 ± 0.4; 0.43 ± 0.01; 3 and 90.58 ± 0.01% for proteins, lipids, fiber, ashes, carbohydrates and water, respectively). Thermal treatment caused the denaturation and aggregation of the proteins, while the addition of gums induced a decrease in the sensitivity to heat treatment of the proteins. Formation of protein aggregates and gum-protein complexes was characterized by electrophoresis, differential scanning calorimetry, and particle size distribution. Heat treatment and addition of gums generated macrocomplexes with enhanced absolute value of ζ-potential, which contributed to the high colloidal stability of amaranth-based beverage. This beverage is suitable for vegans, celiac patients, and lactose intolerants., Facultad de Ciencias Exactas, Centro de Investigación y Desarrollo en Criotecnología de Alimentos

This paper investigated the effects of heat treatment (75 °C × 18 s and 100 °C × 18 s) and wet-mix total solids level (TS: 50 and 60%, w/w) on the physicochemical and techno-functional properties of model infant milk formula (IMF) powders. IMF produced from wet-mixes with 50% TS preheated at 75 °C (50%-75°C) exhibited the longest wettability time (55 ± 2 s) and the poorest flowability, explained by the small particle size (D [4;3]= 16.5 ± 2.29 μm) and low poured bulk density (0.27 ± 0.02 g/cm3). Larger particles were obtained by increasing both pasteurization temperature and TS. Further, powders from 60% TS wet-mixes showed less particle size uniformity, leading to better packing and higher bulk densities. 50%-75°C powders also showed the lowest onset glass transition temperature, which may affect its storage stability. Wettability time was reduced by increasing TS from 50 to 60% or by increasing pre-heating temperature from 75 to 100 °C. However, as observed by low-field nuclear magnetic resonance, the increase in the pasteurization temperature slowed down the global rehydration process. The flowing properties of the powders improved by increasing TS level of the wet-mix. In conclusion, the pre-spray drying wet-mix processing variables, pasteurization temperature and TS level, had a major effect on the physicochemical and functional properties of the IMF powders. It is crucial to understand how variations in the process parameters affect these powder characteristics, due to their functional, technological and economic importance.

This study investigated the effects of total solids (TS) in the wet-mix and pasteurisation temperature on the whey protein (WP) denaturation, rheological behaviour, emulsifying properties and available lysine content of a model infant milk formula (IMF). IMF with 50% or 60% (w/w) TS were produced by wet-mix process and pasteurised at 75 °C or 100 °C for 18 s. Measurements were taken after dispersion, pasteurisation, homogenisation and spray-drying of wet-mix. Pasteurisation at 100 °C caused extensive WP denaturation (above 80%) and increased the viscosity. Available lysine content was 52% higher in powdered IMF obtained from wet-mixes pasteurised at 75 °C compared to 100 °C. A significant reduction in energy consumption could be achieved by producing IMF from 60% TS wet-mixes pasteurised at 75 °C, while obtaining powders with less than 7% WP denaturation, no loss of available lysine during processing and post-reconstitution stability for 2 h.

A number of functional foods containing seaweed-derived peptides are currently commercialized. Some seaweed derived peptide-containing products include Wakame peptide® and Nori peptide S®. To develop functional foods with the addition of Ulva spp. peptides, the isolation and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from hydrolysates of this seaweed was performed. Ulva spp. peptides were fractionated and purified sequentially by anion exchange, ultrafiltration, and reversed phase high performance liquid chromatography. The fractions obtained from each analytical step were collected and the in vitro enzyme inhibitory activity was evaluated. The applied purification process increased the in vitro DPP-IV inhibitory activity. The inhibition mechanism of DPP-IV of the most active fraction was evaluated and it was analyzed by MALDI-TOF. A peptide SLAVSVH was identified. It has 57% of hydrophobic residues in their sequence (including Ala and branched chain amino acids), which could be a common feature among inhibitory peptides of DPP-IV. Molecular docking analysis showed that SLAVSVH/DPP-IV complex was stabilized by CH–π interactions between the side chains of Val6 with the indol of Trp629, and between rings of His7 with Trp563. The energy values obtained for the peptide under study indicate that it is a good candidate to inhibit DPP-IV.

In the present work the effect of the presence of soluble and insoluble protein on the stability of oil-water emulsions prepared with amaranth protein isolates (API) was analyzed. For this purpose, four types of emulsions were prepared: API-pH2 and API-pH6.3 dispersions and solutions. At pH 2.0 the amaranth proteins present higher solubility, are denatured and partially hydrolyzed; while at pH 6.3 its solubility is lower and its structure is more similar to the native protein. The soluble proteins present in API-pH2 and API-pH6.3 reduce with equal intensity the interfacial tension. However, the proteins present in API-pH2 are adsorbed twice as fast as those present in API-pH6.3, with equal rearrangement rate at the oil/water interface. Both, solutions and dispersions of API-pH2 and API-pH6.3 allow the formation of oil-in-water emulsions. Flocculation phenomena are evident, particularly in the case of API-pH6.3 dispersions. The calculated creaming-flocculation constant demonstrates that stability of emulsions increase with protein concentration and with the decrease of pH. The behaviour of API-pH2 and API-pH6.3 solutions was similar to that corresponding to the dispersions discarding a negative effect of the insoluble protein on the emulsifying properties of amaranth proteins., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

Among the factors affecting the development of cardiovascular diseases, hypertension is one of the most important. Research done on amaranth proteins has demonstrated their hypotensive capacity in vivo and in vitro; nevertheless, the mechanism underlying this effect remains unclear. The aim of this study was to analyze in vitro the inhibition of peptides derived from an amaranth hydrolysate (AHH) on other RAS enzymes other than ACE. The chymase and renin activities were studied. AHH was not able to inhibit chymase activity, although a dose-response effect was found on renin activity (IC50 0.6 mg/mL). To provide an approach to the renin inhibition mechanism, we analyzed AHH renin inhibition kinetics and performed a structural characterization of the peptides involved in the effect in terms of molecular size and hydrophobicity. Results suggest that amaranth peptides exhibit renin competitive inhibition behavior. Renin inhibition potency was directly related to peptide hydrophobicity. RP-HPLC separation of AHH and subsequent analysis of the peptide sequences showed 6 peptides belonging to 11S globulin (that can be grouped into 3 families) that would be responsible for renin inhibition. These results demonstrate that Amaranthus hypochondriacus seeds are an adequate source of peptides with renin inhibitory properties that could be used in functional food formulations. Fil: Quiroga, Alejandra Viviana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Aphalo, Paula. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Nardo, Agustina Estefania. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina

The objective of this work was to develop a new protocol to predict with greater confidence peptides as potential inhibitors of the renin enzyme. For this, free, friendly and rigorous servers developed specifically for peptides as ligands were used. Six peptides (SFNLPILR; FNLPILR; SFNLPIL; QAFEDGFEWVSFK; AFEDGFEWVSFK and VNVDDPSKA) identified in an amaranth hydrolysate obtained with alcalase (hydrolysis degree 21%±4) were used. Two positive (angiotensinogen and IRLIIVLMPILMA) and one negative (a tridecapeptide of alanine) controls were included in the analysis. A protocol was designed to include two consecutive stages was performed using CABS-dock server (http://biocomp.chem.uw.edu.pl/CABSdock) and FlexPepDock server (http:// flexpepdock.furmanlab.cs.huji.ac.il/). Peptides SFNLPILR, FNLPILR and AFEDGFEWVSFK inhibited the enzyme in vitro. The heptapeptide FNLPILR was the most potent inhibitor, with an IC50 of 0.41 mM., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

Las proteínas del suero son sometidas a calor durante la producción de fórmulas infantiles. Su desnaturalización y agregación puede reducir la solubilidad, lo que tiene connotaciones funcionales, tecnológicas y nutricionales en el producto final. En el presente trabajo se estudió el efecto del tratamiento térmico y la presencia de caseína, lactosa e inulina, en las proporciones utilizadas en fórmulas infantiles, en la solubilidad proteica. Se prepararon dispersiones acuosas de WPI, con o sin caseinato de calcio (CAS), inulina (INUL) y lactosa (LAC). Las dispersiones se analizaron antes (STT) y luego del tratamiento térmico (TT) a 66ºC, 75ºC y 85ºC durante 30 o 60 min. Los sistemas STT con mayor solubilidad fueron WP (89,3±2,0 %) y WP-INUL (89,6±1,8 %). La solubilidad de WP disminuyó paulatinamente con el TT a partir de 75ºC-30 min, alcanzando una solubilidad mínima de 41,7±1,2 % luego de 85ºC-60 min. WP-INUL mostró la misma tendencia. WP-LAC redujo su solubilidad con el TT, aunque la caída en la solubilidad luego del TT 75ºC-60 min fue menor que en el sistema sin lactosa. La presencia de CAS impidió la pérdida de solubilidad proteica, que aumentó con el TT hasta 75ºC-60 min (alcanzando 100 % en el sistema WP-CAS). Whey proteins are heated during production of infant formulae. The denaturation and aggregation of whey proteins can reduce their solubility, with functional, technological and nutritional implications. In the current work, the effect of heat treatment and presence of casein, lactose and inulin, at the proportions used during production of infant formula, on the protein solubility was studied. Aqueous whey protein isolate (WPI) dispersions with or without calcium caseinate (CAS), inulin (INUL) and lactose (LAC) were prepared. Unheated (UH) and heated (HT) dispersions at 66, 75 and 85 ℃ for 30 and 60 min were analyzed. The UH systems with the highest solubility were WP (89.3 ± 2.0% w/w) and WP - INUL (89,6 ± 1,8% w/w). Solubility of WP decreased with HT from 75 ℃ - 30 min, reaching the minimum solubility (41,7 ± 1.2 % w/w) after 85 ℃ - 60 min. WP - INUL showed the same trend. Solubility of WP - LAC decreased with HT, although the solubility loss after HT 75 ℃ - 60 min was lower than in the system without lactose. CAS presence prevented the loss of protein solubility, which increased with HT until 75 ℃ - 60 min (reaching 100% w/w in the WP - CAS system). This study provides relevant information on the role of the main non - fatty ingredients of infant formulae in the loss of solubility of whey proteins. As proteínas do soro de leite são submetidas ao calor durante a produção de fórmulas para bebês. Sua desnaturação e agregação podem reduzir a solubilidade, que possui conotações funcionais, tecnológicas e nutricionais no produto final. Neste trabalho estudamos o efeito do tratamento térmico e a presença de caseína, lactose e inulina, nas proporções utilizadas nas fórmulas infantis, na solubilidade das proteínas. Dispersões aquosas de isolado de proteínas do soro de leite (WPI) foram preparadas, com ou sem caseinato de cálcio (CAS), inulina (INUL) e lactose (LAC). As dispersões foram analisadas antes (STT) e após tratamento térmico (TT) a 66 ℃, 75 ℃ e 85 ℃ por 30 ou 60 min. Os sistemas STT com maior solubilidade foram WP (89,3 ± 2,0% m/m) e WP - INUL (89,6 ± 1,8 % m/m). A solubilidade do WP diminuiu gradualmente com o TT de 75 ℃ - 30 min, atingindo uma solubilidade mínima de 41,7 ± 1,2 % m/m após 85 ℃ - 60 min. WP - INUL mostrou a mesma tendência. O WP - LAC reduziu sua solubilidade com TT, embora a queda na solubilidade após TT 75 ℃ - 60 min foi menor do que no sistema sem lactose. A presença de CAS impediu a perda de solubilidade da proteína, que aumentou com o TT até 75 ℃ - 60 min (atingindo 100% m/m no sistema WP - CAS). Este estudo fornece informações relevantes sobre o papel dos principais ingredientes não gordurosos das fórmulas infantis na perda de solubilidade das proteínas do soro de leite Fil: Rodríguez Arzuaga, M.. Laboratorio Tecnológico del Uruguay; Uruguay Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Abraham, Analia Graciela. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina

The aim of this work was to evaluate the ability of broken rice, an underutilized industrial by-product, as a potential functional and health promoting ingredient. With this purpose, the ability to inhibit the angiotensin converting enzyme and renin of a rice protein hydrolyzate (RPH) obtained from a high-protein variety of broken rice (var. Nutriar FCAyF) was analyzed (IC₅₀ = 0.87 and 2.7 mg/mL, respectively). RPH was separated by gel permeation chromatography and in a second purification step by RP-HPLC. The sequence of antihypertensive peptides presented in two RP-HPLC fractions was analyzed. Peptides capable of interacting with the active sites of both enzymes were identified. In this study, we demonstrate that the hydrolysis treatment improves functional and biological properties of rice proteins. Protein preparations obtained from a by-product of rice industry, such as broken rice, are a promising ingredient with potentially good biological properties., Facultad de Ciencias Agrarias y Forestales, Facultad de Ciencias Exactas, Centro de Investigación y Desarrollo en Criotecnología de Alimentos

A rapid method of screening for lactic acid bacteria with high inhibitory power was developed. The methodology employed was the agar-diffusion assay, which was standardized for the indicator strain, medium composition, and incubation conditions. The assay was performed in nutrient agar at 30°C with 10 8 spores of Bacillus subtilis per plate as indicator strain. The inhibition produced by supernatants of lactic acid bacteria cultures harvested at stationary phase was determined. The inhibitory powers of different strains were compared with a standard curve obtained with racemic lactic acid. Results obtained with lactic acid and supernatants of bacterial cultures demonstrate that the diameter of the inhibition zone (d) was related to the pH by the exponential relation d = a exp (- b pH). Results obtained with strains that produced inhibitory substances other than lactic acid could not be fitted into the standard linear curves obtained in the plot of ln d versus pH of lactic acid.

The aim of this work was to analyse the hypotensive effect of amaranth protein/peptides on spontaneously hypertensive rats (SHR). The mechanism of action of these peptides was studied in vivo and ex vivo. We also tested the effect of protection against gastrointestinal digestion (GID) exerted by an O:W emulsion on the integrity of the antihypertensive peptides. All samples tested produced a decrease in blood pressure (SBP). The animals treated with emulsion (GE) and emulsion + peptide (GE+VIKP) showed the most significant reduction in the SBP (42 ± 2 mmHg and 35 ± 2 mmHg, respectively). The results presented suggest that after GID, a variety of peptides with biological activities were released or were resistant to this process. These peptides play a role in the regulation of the SBP by acting on plasma ACE, plasma renin and the vascular system. These results support the use of amaranth protein/peptides in the elaboration of functional foods for hypertensive individuals., Centro de Investigación y Desarrollo en Criotecnología de Alimentos, Facultad de Ciencias Médicas

We analyze the possibility of using the emulsifying properties of amaranth proteins and the bioactivity shown by peptide sequences encrypted in these proteins to formulate functional emulsions with angiotensin I-converting enzyme (ACE) inhibitory activity. For this we formulate O:W emulsions, 20:80, from a mixture in equal parts (50:50) of amaranth protein isolates (API), and hydrolysates (AH) at 1 and 2% protein w/v. Results obtained showed that these emulsions, API50-AH50-1% and API50-AH50-2%, are highly flocculated (Flocculation index: 8.2 and 5.9) and stable at least for 8 days, without evident creaming or coalescence. The components present in the emulsions were capable of inhibiting ACE, in in vitro assays (IC₅₀ of 0.14 ± 0.02 mg/mL). API and API50-AH50 emulsions were subjected to a simulated gastrointestinal digestion in vitro. The emulsions were susceptible to aggregation and coalescence phenomena during this process, which could be a consequence of the chaotropic action of the bile salt on the interface and the proteolytic and lipolytic action of pancreatin and lipase, respectively (D₄.₃ of original emulsion: 1.22 ± 0.01 μm and D₄.₃ of digested emulsion 79.5 ± 17.1 μm). We also found that amaranth proteins were more resistant to gastric than duodenal digestion. After the process of simulated gastrointestinal digestion, the inhibition of ACE (IC₅₀ of 0.13 ± 0.07 mg/mL) was maintained. This fact evidences the protective effect of the emulsion on the bioavailability of the ACE inhibitory peptides, by either their participation in the formation of the interfacial film and/or their participation in the network of formed flocs., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

In this study, amaranth flour was used as an ingredient to prepare gluten-free cookies. The production process and attributes of amaranth cookies were characterised, and the potential use of amaranth flour as a functional ingredient was analysed. Cookies exhibited a non-uniform reddish brown colour and a cookie factor ratio of 4.5 ± 0.6. Storage studies indicated that after 3 weeks at room temperature cookies presented slight variations in the texture. Simulated gastrointestinal digestion of this product was able to release peptides capable of exerting potential antithrombotic and antihypertensive activities, IC₅₀ values of 0.22 ± 0.04 and 0.23 ± 0.03 mg mL⁻¹ protein, respectively. This work demonstrates for the first time that food made with amaranth flour exerts potential antithrombotic and antihypertensive activity. In conclusion, these amaranth cookies could be an alternative way of incorporating potentially health beneficial products for people who choose a conscious diet, including coeliac or vegan consumers., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

The in vivo immunomodulatory effect of a bioactive peptide from Amaranthus hypochondriacus grains in an IgE-mediated food allergy mouse model was examined. The synthetic SSEDIKE peptide was orally administered to prevent food allergy. Upon oral challenge with milk allergens we observed an alleviation of hypersensitivity symptoms with negativization of skin test, a significant inhibition of specific IgE and IgG1 secretion, a substantial reduction in the secretion of IL-5 and IL-13 by antigen-stimulated spleen cells and mucosal reduction of transcripts coding for ccl20, gata-3 and nf-kb. In addition tgf-β and foxp3 mRNA levels were up-regulated in jejunum. The charged SSEDIKE peptide from Amaranth inhibited the allergy reaction in a mouse model of food allergy, with suppression of IgE secretion and control of the intestinal inflammation preventing the activation of NF-κB, which might be attributed to the induction of local tolerance. Fil: Moronta, Julián. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Smaldini, Paola Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina Fil: Fossati, Carlos Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Docena, Guillermo H.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina

The objective of this work was to assess the possibility of obtaining calcium-added soymilk with acceptable characteristics regarding protein solubility and physical stability, and inactivation of trypsin inhibitors and lipoxygenase, through a combined thermal-high hydrostatic pressure treatment. A Doehlert design was applied to study the effect of combining pressure levels (500–700 MPa), initial temperatures (45–65 °C) and CaCl2 concentrations (5–15 mmol L− 1). Results showed that protein solubility was a function of CaCl2 concentration (p < 0.005), and that inactivation of trypsin inhibitors was a function of pressure level and temperature (p < 0.005). Lipoxygenase activity was fully inactivated in most of the conditions tested. Physical stability was improved by the combined treatments: depending on calcium concentration, either no settling was detected in a 5-day period or a less conspicuous phase separation was observed. Our results indicate that some combined thermal-high hydrostatic pressure treatments allow the preparation of calcium-enriched soymilks with improved physical stability without additives such as chelating agents, and acceptable in terms of full inactivation of trypsin inhibitors and lipoxygenase. Fil: Manassero, Carlos Alberto. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Vaudagna, Sergio Ramon. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina Fil: Sancho, Ana Maria. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Speroni Aguirre, Francisco José. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina

The effect of casein (CAS) and inulin (INUL), at ratios commonly found during infant formula processing, on the conformational changes of whey proteins (WP) was investigated. Model systems were prepared as aqueous dispersions of WP isolate alone or with calcium caseinate and/or INUL, and heated for 30 min at66, 70 or 75 C. Heat treatment of WP induced denaturation and aggregation. Solubility of WP system decreased by 25% when heated at 75 C. Upon heating, the presence of CAS did not prevent WP denaturation, but increased protein solubility up to 100% in WPeCAS system and prevented aggregation. INULaffected the secondary structure of WP and increased the denaturation temperature, although it did not prevent aggregation nor solubility loss at 75 C. In conclusion, presence of CAS prevented aggregationand solubility loss of WP during heating while INUL induced WP conformational changes impacting the denaturation stage. Fil: Rodríguez Arzuaga, Mariana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Laboratorio Tecnológico del Uruguay; Uruguay Fil: Bosch, María Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Abraham, Analia Graciela. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina

Antiproliferative effect of Amaranthus mantegazzianus proteins and peptides released after simulated gastrointestinal digestion (DH% 37.8 ± 3.8) was investigated on human colon cancer cell line (HT-29). Inhibition of proliferation of HT-29 cells was exhibited after a 24 h treatment with different concentrations of amaranth protein isolate (API) and the peptides released after digestion (DGS), presenting IC50 values of 1.35 ± 0.12 and 0.30 ± 0.07 mg soluble protein/mL, respectively. Lactate dehydrogenase assay indicated that both samples caused the loss of membrane integrity and cell lysis over HT-29 cells, and DAPI fluorescence microscopies evidenced typical apoptotic features. Moreover, Annexin V-FITC flow cytometry showed a significant increase of early apoptotic and late apoptotic/necrotic HT-29 cells compared to untreated ones, and caspase-3 assay confirmed the apoptosis induction with a 43.0 ± 10.3% and 65.8 ± 12.7% increase of caspase-3 activity produced by a 2 mg/mL treatment of API and DGS, respectively. In conclusion, amaranth peptides successfully released after simulated gastrointestinal digestion would exert a potential antiproliferative activity over HT-29 tumor cells. This effect was linked to the induction of cell necrosis and apoptosis, supporting the idea of using amaranth proteins as a potential food alternative ingredient for functional foods. Fil: Sabbione, Ana Clara. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Ogutu, Fredrick Oñandu. Chinese Academy Of Agricultural Sciences; China Fil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Zhang, Miao. Chinese Academy Of Agricultural Sciences; China Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Mu, Tai-Hua. Chinese Academy Of Agricultural Sciences; China

The hypocholesterolemic effect of amaranth was studied in male Wistar rats fed a high-fat diet that was supplemented with amaranth flour, AF, or isolated protein, AI. Likewise, an in vitro test was carried out, in which the capacity of the AI, AF, the digested isolate, DAI, and the digested amaranth flour, DAF, to displace the cholesterol of the model micelles was evaluated. The in vivo results showed an increase in the excretion of cholesterol through feces (77% for AF7; 23% and 108% for AI30 and AF30, respect control) and a decrease in the content of hepatic cholesterol (98% for AF7; 96% and 53% for AI30 and AF30 respect control); whereas in vitro it was shown that both AF and DAF have greater power to displace cholesterol than the AI and DAI (IC50 0.1, 0.71, 0.2, and 2.1 for AF, DAF, AI, and DAI, respectively). These evidences show that the proteins and fibers of amaranth have an effect on cholesterol metabolism., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

The effect of amaranth peptides on the activity and expression of tissue factor (TF) on THP-1 activated cells was evaluated in vitro. An active anticoagulant peptide fraction (AF) was found to inhibit TF expression (IC50 = 0.39 mg mL-1) and activity. Immunocytochemical fluorescence confocal microscopy analysis showed that treated monocytes decreased TF membrane translocation by 49.0% and increased two-fold in nuclei compared to a positive control, indicating a decrease of active TF to initiate the coagulation cascade. Moreover, a cytokine array suggested that the AF mechanism of action implied the inhibition of the NF-κB pathway. Expression of MIP-3α, interleukin-1β, interleukin-1α, TARC, pentaxin 3, and PDGF-AA cytokines was highly suppressed by AF peptides, producing reductions of 78.8%, 61.8%, 54.1%, 42.6%, 37.9% and 37.8%, respectively, compared to a positive control. The results suggest a potential mechanism for the antithrombotic and anti-inflammatory effect of AF, by showing that amaranth peptides play a negative feedback regulatory role over the NF-κB pathway. In this research, we link for the first time the immunomodulatory activity of amaranth peptides with the inhibition of TF expression and therefore their antithrombotic potential. Fil: Sabbione, Ana Clara. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Luna Vital, Diego Armando. University of Illinois at Urbana; Estados Unidos Fil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: González de Mejía, María Elvira. University of Illinois at Urbana; Estados Unidos

Amaranth protein isolate was obtained and subjected to simulated gastrointestinal digestion to evaluate its potential antithrombotic activity. The protein isolate did not present fibrin clotting inhibition at the concentrations studied, whereas the hydrolysate (DH% = 51.1 ± 3.8%) exhibited inhibition of fibrin coagulation, showing a dose–response behaviour (IC50 = 0.23 ± 0.02 mg/mL), confirming that the enzymatic treatment was able to release bioactive peptides from amaranth proteins. A fraction with high antithrombotic activity was obtained from this hydrolysate, and resulted to be three times more potent than its original sample (IC50 = 0.07 ± 0.01 mg/mL). The absorption of this active fraction was studied with an in vitro peptides transport assay through intestinal epithelium and it was observed that some peptides are able to cross the Caco2-TC7 cell monolayer. Potentially bioactive peptides were found after sequencing them, and informatics tools allowed us to select and locate in their native molecules those peptides prone to inhibit thrombin activity., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

The use of amaranth starch granules and nanocrystals as possible reinforcement of amaranth 17 proteins films was analyzed. Starch granules and protein isolates were extracted of amaranth 18 grain, and nanocrystals were prepared by acidic hydrolysis from starch. Films were prepared 19 by casting aqueous dispersions containing amaranth protein isolate (API, 5% w/v), glycerol 20 (1.25 % w/v) and different concentrations of starch granules (0 to 30 wt% relative to API) 21 and nanocrystals (0 to 12 wt% relative to API). All films were homogeneous, translucent 22 and slightly brownish, with a general visual appearance similar to the control amaranth 23 protein film. While it was possible to prepare films in which the starch granules retain their 24 native structure after being processed, the presence of these particles did not improve the film 25 properties. Only the addition of starch nanocrystals improved their tensile strength and 26 water vapour permeability as well as their water susceptibility, probably due to their 27 nanosize, uniform distribution and the strong interactions that developed with protein matrix. Fil: Condes, María Cecilia. Facultad de Ciencias Exactas. Universidad Nacional de La Plata; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Dufresne, Alain. Centre National de la Recherche Scientifique; Francia. Universite Grenoble Alpes; Argentina Fil: Mauri, Adriana Noemi. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina

The ability of freeze-dried high pressure-treated soybean proteins to form cold-set gels and their aptitude to act as a protective matrix to Lactobacillus delbrueckii subsp lactis strain CIDCA 133 were evaluated. Gels were obtained by dispersing denatured soybean protein isolates (SPI) in water or in a lactobacilli suspensions, and further incorporation of calcium. When SPI were dispersed in water, ordered, adhesive, and with high water holding capacity gels were obtained at a calcium concentration of 0.015 mol L 1 . Increase in calcium concentration to 0.020 mol L 1 increased elastic modulus (small deformation rheology) and maximum force (texture profile) and made gels become opaque. When protein concentration was 90 g L 1 , and denaturation of SPI was carried out at 600 MPa gels with higher values of elastic modulus were obtained as compared with those from gels denatured at 400 MPa. After dispersing denatured SPI in lactobacillus suspensions the gels were turbid and with a pink-like color. Elastic modulus and tan d of gels prepared in lactobacilli suspensions were higher than those dispersed in water, revealing that matrix was modified by lactobacilli presence. The lactobacilli included in these cold-set gels survived better than in coagulated milk to a modeled gastric challenge. Moreover, bacteria remained viable without damaging the matrix during a 28-days storage at 4 C. The high soybean protein concentration would be responsible for lactobacilli protection. Our results suggest that SPI cold-set gels may be used as carriers for lactobacilli protecting them from the effect of simulated gastric juice and enabling their incorporation in functional foods. Fil: Hugo, Ayelen Amelia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina Fil: Perez, Pablo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina Fil: Speroni, Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina

Physical and chemical techniques were applied to characterize the type of interaction between hydrocolloids and the gluten network in wheat dough, with and without NaCl. Modified celluloses (microcrystalline cellulose, MCC; carboxymethylcellulose, CMC, hydroxypropylmethylcelluloses, HPMC) and pectins of low (LMP) and high (HMP) degree of methylation were utilized as hydrocolloids to interact with gluten proteins. Modified celluloses were employed at 1.5% (flour basis) and pectins at 2.0% (flour basis). By microscopy (SEM and CLSM), it could be observed that NaCl induced a more marked crosslinking and orientation of gluten network. On the other hand, the addition of hydrocolloids led to more open matrices. Molecular mobility was evaluated by 1H-NMR assays and significant effects of NaCl addition and hydrocolloid type were found on relaxation times (T2). In presence of salt, significantly higher relaxation times were observed when modified celluloses were added. Hydrocolloid addition strongly affected the secondary conformation of proteins as studied by FT-Raman. In absence of NaCl, control and MCC samples exhibited the higher α-helix conformation percentage (indicating a more ordered and compact structure), followed by dough with HMP, HPMCs, LMP and CMC. In general, doughs with modified celluloses and NaCl showed a decrease of α-helix conformation. CMC dough showed the smallest percentage of α-helix conformation, and the highest contributions of more unfolded structures. Doughs with pectins and NaCl showed similar percentages of α-helix to control one but an increase of random coil structure was observed. Electrophoresis assays confirmed that the presence of certain hydrocolloids (CMC) during gluten formation could affect protein interaction promoting subunits lability from the matrix. Fil: Correa, María Jimena. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina; Argentina Fil: Evelina Ferrer. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina Fil: Maria Cristina Añón. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina; Argentina Fil: Ferrero, Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina; Argentina

The ability of soybean proteins to form cold-set gels, using high pressure (HP) processing as denaturing agent and calcium incorporation was evaluated. Different protein preparations were assayed: soybean protein isolate (SPI), a b-conglycinin enriched fraction (7SEF) and a glycinin enriched fraction (11SEF). 7SEF formed aggregated gels with low water holding capacity whereas 11SEF did not form self-standing gels. SPI formed the better gels: ordered and with high water holding capacity. SPI gels were relatively soft and their visual aspect, rheological and texture properties, and water holding capacity depended on HP level (400e600 MPa), CaCl2 concentration (0.015e0.020 mol L 1) and protein concentration (85e95 g L 1), thus gels with different characteristics may be obtained. The gels comprised a three dimensional network stabilized by non-covalent interactions with spaces filled of proteins in aqueous solution. The results indicate that it is possible to use HP and subsequent calcium incorporation to form self-standing cold-set gels from soybean proteins. These gels may be of interest to incorporate heat-labile compounds or probiotics during the gelation step. Fil: Speroni Aguirre, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones En Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata; Argentina Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones En Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata; Argentina

The technological and sensory quality of pasta made from bread wheat flour substituted with wholemeal amaranth flour (Amaranthus mantegazzianus) at four levels, 15, 30, 40 and 50% w/w was investigated. The quality of the resulted pasta was compared to that of control pasta made from bread wheat flour. The flours were analyzed for chemical composition and pasting properties. Cooking behavior, color, raw and cooked pasta texture, scanning electron microscopy and sensory evaluation were determined on samples. The pasta obtained from amaranth flour showed some detriment of the technological and sensory quality. So, a maximum substitution level of 30% w/w was defined. This is an equilibrium point between an acceptable pasta quality and the improved nutritional and functional properties from the incorporation of amaranth flour. Fil: Martinez, Cristina S.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina Fil: Ribotta, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Córdoba; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Leon, Alberto Edel. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Ciencia y Tecnología de Alimentos Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Ciencia y Tecnología de Alimentos Córdoba; Argentina

In the Northeast of Argentina, cowpeas are frequently produced by small- and medium-sized farmers for either personal consumption or trade. The objective of this work was to study, using a principal component analysis (PCA), the effect of thermal and non-thermal treatments on the nutritional and anti-nutritional properties of the four different varieties of Vigna unguiculata . Anti-nutrients contents allowed treatment differentiation for each variety because they contributed mainly in the PC1 axis construction (PCA). In contrast, nutrient (proteins and carbohydrates) contribution to treatment differentiation was not significant. Colorado variety presented the highest mineral in vitro availability, with the exception of iron. Thermal treatment increased the protein digestibility of all flours. The typical thermograms of native flours presented a two overlapping endotherm with denaturing temperatures (Td) of 83–84 °C and 91–93 °C respectively and a total enthalpy (Δ H ) 7–9 J/g. Heat treatments produced a shift of Td (67–73 °C) with increasing treatment time. Cowpea seeds varieties, especially Colorado and Cuarenton, because of their nutritional and antinutritional components under thermal treatments, could be used as an alternative low cost protein source for food formulas.

Changes in the secondary structure of gluten proteins due to emulsifiers were analyzed by Raman Spectroscopy. The protein folding induced by 0.25% SSL (Sodium Stearoyl Lactylate) (GS0.25, Gluten + 0.25% SSL) included an increase in alfa-helix conformation and a decrease in beta-sheet, turns and random coil. The same behavior, although in a less degree, was observed for 0.5% gluten?DATEM (Diacetyl Tartaric Acid Esters of Monoglycerides) system. The low burial of Tryptophan residues to a more hydrophobic environment and the low percentage area of the C?H stretching band for GS0.25 (Gluten + 0.25% SSL), could be related to the increased in a-helix conformation. This behavior was also confirmed by changes in stretching vibrational modes of disulfide bridges (S?S) and the low exposure of Tyrosine residues. High levels of SSL (0.5% and 1.0%) and DATEM (1.0%) led to more disordered protein structures, with different gluten networks. SSL (1.0%) formed a more disordered and opened gluten matrix than DATEM, the last one being laminar and homogeneous. Fil: Gómez, Analía Verónica. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Agrarias y Forestales; Argentina Fil: Ferrer, Evelina Gloria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Puppo, Maria Cecilia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Agrarias y Forestales; Argentina

For several years, plant proteins have been the interest of both researchers and industrialists. The diversity, differences in physicochemical and nutritional properties, contributions to the health of consumers, low cost, and advances in production and processing technologies have made the storage proteins of grains and seeds an extremely attractive potential from the commercial point of view (Moure et al., 2006).

Los alimentos ejercen una influencia importante en el desarrollo de diversas enfermedades no transmisibles, entre las que es posible incluir el cáncer. Por otra parte, existe información que da cuenta de que algunos alimentos o algún componente alimentario pueden proteger contra el desarrollo de esta enfermedad. El objetivo de este trabajo fue purificar, caracterizar y analizar la potencial actividad antiproliferativa de una lectina proveniente de Amaranthus hypochondriacus (AH). Para ello se purificó parcialmente la lectina a partir de harina desgrasada de AH (LPP). Se encontró una proteína con una masa molecular aproximada de 65-70 kDa, compuesta por dos subunidades de aproximadamente 35 kDa unidas por interacciones no covalentes, con actividad hemaglutinante característica de las lectinas. Se estudió la inhibición de la proliferación celular utilizando la línea celular tumoral CaCo2/TC7 mediante el ensayo del cristal violeta. Además de la lectina parcialmente purificada, se estudió el efecto antiproliferativo de los aislados de Amaranhus hypochondriacus y mantegazzianus, y una lectina comercial de Amaranthus caudatus. Todas las muestras ensayadas mostraron efectos citotóxicos en forma de dosis respuesta., Food exerts an important influence on the development of several chronic diseases, including cancer. On the other hand there is evidence indicating that some food components can protect against the development of this disease. The aim of this work was to purify, characterize and analyze the potential antiproliferative activity of a lectin from Amaranthus hypochondriacus. Lectin was partially purified from defatted Amaranthus hipochondriacus flour. A protein with an approximate molecular mass of 65-70 kDa, composed of two subunits of about 35 kDa held together by noncovalent interactions with hemagglutinating activity characteristic of lectins was found. Inhibition of cell proliferation was studied using the tumor cell line CaCo2/TC7 by the crystal violet assay. In addition to the partially purified lectin, the antiproliferative effect of Amaranhus hypochondriacus and mantegazzianus isolates, and a commercial lectin from Amaranthus caudatus was studied. All samples tested showed cytotoxic effects in a dose dependent way., Centro de Investigación y Desarrollo en Criotecnología de Alimentos

Ingestion of diets with antithrombotic and antioxidant components offer a convenient and effective way to prevent and reduce the incidence of cardiovascular diseases. The aim of the present work was to obtain an amaranth hydrolysate by the activation of an endogenous aspartic protease, to establish adequate experimental conditions, and to evaluate its antithrombotic and antioxidant activity in order to assess its potential application as an ingredient in functional foods. The results obtained not only confirmed the presence of an endogenous protease in the amaranth isolate, but also allowed us to select an adequate incubation conditions (pH 2, 40 °C, 16 h). The hydrolysate obtained (degree of hydrolysis 5.3 ± 0.4 %) showed potential antithrombotic activity (IC₅₀ = 5.9 ± 0.1 mg soluble protein/mL) and had more antioxidant activity than the isolate, indicating that the activation of the protease released bioactive peptides from amaranth proteins. Decreasing the pH is a simple and cheap process and is another way to obtain potential functional ingredients with bioactive compounds., Facultad de Ciencias Exactas, Centro de Investigación y Desarrollo en Criotecnología de Alimentos

The goal of this work was to analyze the effect of different treatments on functional properties (Color parameters, water holding capacity, oil holding capacity, water imbibition capacity, protein solubility and apparent viscosity) and microstructure of three cowpea varieties. Proteins present in flours obtained from heat-treated seeds exhibited a significant increase in water and oil absorption values, water imbibition capacity, and apparent viscosity, whereas solubility decreased. Color determinations on flours showed a reduction in L * and H *, and an increment in C * with treatment intensity. Structural changes in seeds would explain the variations in the functionality of flours. This study shows that cooking and autoclaving affect significantly the functional properties of flours, while soaking had a lower impact. The knowledge about these changes will be very useful for developing and obtaining new preparations based on cowpea flour.

The effects of High Pressure (HP) on the solubility, aggregation and sedimentation of calcium-supplemented soybean proteins present in soybean protein isolate (SPI), and protein fractions enriched in β-conglycinin and glycinin were analyzed in this work. Calcium addition (up to 0.0075 mol/L) to soybean protein dispersions (1% w/v - pH 8.0) provoked the formation of insoluble aggregates with a very large size. HP treatments split those particles. The size of the HP-formed aggregates was a function of HP intensity, of calcium concentration and of protein composition of samples. 400 and 600 MPa improved the solubility of calcium-added soybean proteins in the three protein samples assayed. At certain calcium concentrations and HP levels, these soluble proteins were involved in the formation of macroaggregates. The velocity of sedimentation of insoluble proteins in calcium-enriched SPI dispersions decreased markedly after HP treatment. This work provides information that may be useful for the handling of complexes formed from soybean proteins and calcium, in order to obtain species with different characteristics regarding solubility and molecular weight. Industrial relevance: The knowledge provided by this work may promote the use of high pressure in the food industry. Indeed high pressure increases the solubility of calcium-added soybean proteins and, in the case of the insoluble ones, slows down their settling. These features may allow the incorporation of calcium-added soybean proteins to different kinds of enriched drinks. © 2012 Elsevier Ltd. Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: De Lamballerie, M.. Centre National de la Recherche Scientifique; Francia Fil: Speroni Aguirre, Francisco José. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina

A comparative study on the behavior in the air–water interface of b-lactoglobulin, a-lactoalbumin, glycinin and b-conglycinin was performed. The behavior at the interface was evaluated by equilibrium surface tension and surface rheological properties of adsorbed films. There were significant differences (a 0.05) in the values of the constants of adsorption to the interface of the four proteins. The glycinin had the slowest rate of adsorption, due to its low average hydrophobicity, low molecular flexibility and large molecular size. Smaller proteins like b-lactoglobulin and a-lactoalbumin tended to greater equilibrium pressure values than the larger proteins because of its higher rate of adsorption to the interface. The foam capacity of proteins showed a positive correlation with the average hydrophobicity; the maximal retained liquid volume or the initial rate of passage of liquid to foam were significantly lower (a 0.05) when protein was glycinin. The dilatational modulus of glycinin was the lowest, which implies lowest resistance to disruption of the film. Glycinin protein has lower proportion of gravitational drainage and higher disproportionation having perhaps a less resistant film. In conclusion, b-conglycinin and whey proteins showed a similar behavior, so b-conglycinin might be the best soybean protein to replace milk proteins in food formulations. Fil: Medrano, A.. Universidad de la Republica; Uruguay Fil: Abirached, C.. Universidad de la Republica; Uruguay Fil: Araujo, A. C.. Universidad de la Republica; Uruguay Fil: Panizzolo, L. A.. Universidad de la Republica; Uruguay Fil: Moyna, P.. Universidad de la Republica; Uruguay Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata; Argentina

BACKGROUND: Amaranth 7S globulin is a minor globulin component and its impact on the properties of an amaranth protein ingredient depends on its proportion in the variety of amaranth being considered. Some physicochemical, functional and angiotesin I-converting enzyme (ACE) inhibitory properties of amaranth vicilin were studied in this work and compared with the 11S globulin. RESULTS: Fluorescence spectroscopy results indicated that 7S globulin tryptophans were more exposed to the solvent and, by calorimetry, the 7S globulin denaturation temperature (Td) was found lower than the 11S globulin Td, suggesting a more flexible structure. The 7S globulin surface hydrophobicity was higher than that of the 11S globulin, which is in agreement with the better emulsifying properties of the 7S globulin. The solubility in neutral buffer of the 7S globulin (851 ± 25 g kg−1) was also higher than that of the 11S globulin (195 ± 6 g kg−1). Bioinformatic analyses showed the presence of ACE inhibitory peptides encrypted in 7S tryptic sequences and peptides released after in vitro gastrointestinal digestion showed a high ACE-inhibitory capacity (IC50 = 0.17 g L−1), similar to that of 11S globulin peptides. CONCLUSION: Compared with the 11S globulin, the 7S globulin presents similar ACE inhibitory activity and some functional advantages, better solubility and emulsifying activity, which suits some food requirements. The functional behavior has been related with the structural properties. Copyright © 2011 Society of Chemical Industry

Food protein product, gluten protein, was chemically modified by varying levels of sodium stearoyl lactylate (SSL); and the extent of modifications (secondary and tertiary structures) of this protein was analyzed by using Raman spectroscopy. Analysis of the Amide I band showed an increase in its intensity mainly after the addition of the 0.25% of SSL to wheat flour to produced modified gluten protein, pointing the formation of a more ordered structure. Side chain vibrations also confirmed the observed changes.

Most studies on functionality of soybean proteins have been made with total protein isolates, with the drawback to limit the knowledge of phenomena due to the important complexity of protein composition. In this study we have tried to better understand the behavior of soy emulsions by using their two partially purified fractions: β-conglycinin (7S) and glycinin (11S). Furthermore, we have assessed the combined effect of temperature (20-60 ºC) and high pressure (0.1-600 MPa) on physicochemical, microstructural and rheological properties of oil-in-water emulsions prepared with 7S or 11S proteins at 7% (w/v). Our results show that 7S and 11S emulsions behaved differently under the combined treatments and that 7S protein was responsible for the global properties of soybean emulsions, whereas 11S proteins exerted a negligible effect. From 400 MPa and at 60 ºC, we have noticed for 7S emulsions an increase of flocculation and gelation, largely confirmed by confocal microscopy due to aggregation between adsorbed and aqueous 7S proteins. Globally we have evidenced that temperature reinforces the effect of high pressure and that the threshold to obtain some changes is 400 MPa. The very different behavior of 7S and 11S proteins in emulsions under treatments could help to orientate their commercial use as function of planed treatments Fil: Puppo, Maria Cecilia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Beaumal, Valérie. Instituto National de Recherches Agronomiques. Biopolymères Interactions Assemblages; Francia Fil: Speroni Aguirre, Francisco José. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: De Lamballerie, M.. Genie Des Procedes - Environnement - Agro-alimentaire. Genie Des Procedes - Environnement - Agro-alimentaire Sede Oniris; Francia. Centre National de la Recherche Scientifique; Francia Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Anton, Marc. Instituto National de Recherches Agronomiques. Biopolymères Interactions Assemblages; Francia