Physicochemical and mechanical properties of a new cold-set emulsion gel system and the effect of quinoa protein fortification

A new approach for soft and self-sustainable oil-in-water emulsion gel systems (EGs) preparation based on a formulation with olive oil, sodium alginate, citric acid, and calcium chloride, and the combination of high-speed homogenization and gelation induction by glucono-δ-lactone addition is presented. Also, the effect of EG protein fortification by the incorporation of quinoa concentrate (QC) and quinoa flour on the physicochemical and mechanical properties of these EGs upon storage at 4 °C was investigated. Despite soft and self-sustainable EGs (10 g/kg and 20 g/kg alginate, respectively) showed higher oil droplet size increment with total biopolymer concentration, these systems presented remarkable stability during 28 days. All fortified EGs showed higher fluid retention capacity (>99%), L*, a*, and lower b* values. After one day, EGs presented pHs ranging 4.1–4.3, and longer storage times promoted an increased acidity, to a less extent for QC-fortified-EGs. Lipid oxidation degree also increased during storage (from 30 to 150 μmol/L malonaldehyde), with no significant effects upon protein fortification. Protein fortification promoted higher gel strength in all self-sustainable EGs (from 3.5 N to almost 7 N), and especially after 14 days for soft-EGs. These EGs can be used in the food industry as fat replacers to formulate healthier products.Fil: Ingrassia, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería del Rosario. Departamento de Investigación Institucional; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentin

Sensory analysis of heated sodium alginate film flavored with chicken stock

The spread of non-communicable diseases (NCD) is considered one of the top health problems worldwide. A low intake of fruits and vegetables in conjunction with a high consumption of foods rich in saturated and trans fats, salt and sugar has been reported to be the main cause of a considerable proportion of deaths associated to NCDs (World Health Organization (WHO), 2009; WHO, 2011). NCD Global Action Plan 2013?2020 proposes, among other objectives, to reduce the impact of diabetes, giving priority to actions to prevent overweight and obesity (WHO, 2016). For this reason, interventions aiming at encouraging people to engage in healthier eating habits have been identified as one of the top priorities for reducing the burden of NCD (Beaglehole et al., 2011). To assist in the achievement of these objectives, an alternative for roasted chicken skin was proposed in the research carried out by Báez et al. (2017). In this work, a heat treated calcium alginate dry film prepared with chicken stock was developed. This film presented similar characteristics to roasted chicken skin when it was heated. Heat treatment of the dry film for 15 min at 130 °C produced the development of an opaque maroon color and an increased in their brittleness. This information can be used by product developers, culinary scientists and professional chefs in designing food products in which these kinds of films are employed to wrap or cover the top of chicken meat pieces that are then subjected to cooking. These studies suggest a potential use of heat treated-chicken stock films as a substitute of roasted chicken skin since the crisp texture and optical properties were alike. This is the basis for the preparation of healthier alternatives to the traditional roasted skin through reduction unhealthy components, such as fat (including cholesterol) and carcinogenic compounds, without loss of overall flavor intensity (Báez et al., 2017). However, sensory studies are needed before the product can be recommended.Fil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Busti, Pablo Andres. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Llopart, Emilce Elina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Báez, Germán David. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Verdini, Roxana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentin

Effects of extraction pH of chia protein isolates on functional properties

The aim of this work was to study the effect of the extraction pH on the functional properties of chia protein isolates (CPI). Samples were named as CPI10 or CPI12, according to their extraction pH, 10 or 12, respectively. Functional properties were significantly modified by the extraction pH. Color properties revealed that CPI12 presented a lower L* (47.8 ± 0.9 for CPI10 and 30 ± 1 for CPI12). Besides, a higher b* value was obtained for CPI12 (7.0 ± 0.3 for CPI12 and 5.6 ± 0.7 for CPI10), as a result of a higher ash content. CPI12 showed a higher WAC probably due to a higher exposure of polar amino acids (4.4 ± 0.1 g/g and 6.0 ± 0.2 g/g), whereas CPI10 showed a higher ability to bind oil (7.1 ± 0.2 g/g and 6.1 ± 0.2 g/g for CPI10 and CPI12, respectively). CPI10 proved more appropriate as an emulsion stabilizer than CPI12, which could be due to its higher surface hydrophobicity, protein solubility and negative net charge. The d4,3 (μm) was 29.5 ± 0.4 and 20.4 ± 0.3 in emulsions stabilized with CPI12 and CPI10, respectively. Although both isolates underwent heat gelation, they exhibited a weak gel behavior. Overall, CPI10 may be more suitable for the food industry as a meat replacer or extender.Fil: López, Débora Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Ingrassia, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario; ArgentinaFil: Wagner, Jorge Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Spelzini, Darío. Universidad Nacional de Rosario; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Boeris, Valeria. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario; Argentin

Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles

Interaction between vitamin D3 with beta-lactoglobulin (β-LG) was studied by turbidimetric measurements covering vitamin concentrations up to 500 μM, within a wide range of vitamin concentration and at high vitamin/protein ratios, both conditions that have not been assayed in previous studies. Turbidity of vitamin D3 in the absence and presence of β-LG (20, 40 and 100 μM) in 20 mM phosphate buffer at pH 7.0 proved the expected vitamin-protein interaction as well as the effect of protein concentration. In order to estimate the proportion of bound vitamin in the vitamin-protein complex, a binding parameter (BP) was defined and its dependence on protein concentration was analysed. Fluorescence quenching with acrylamide for 100 μM vitamin D3 and 20 μM β-LG in 20 mM phosphate buffer at pH 7.0, suggested vitamin D3 interact in the hydrophobic calix in the protein. Circular dichroism experiments showed the binding of the vitamin causes conformational changes in the secondary protein structure. Particle size and zeta potential determinations were also carried out in order to establish possible conformational models of interaction vitamin-protein. The higher the vitamin concentration, the greater the bound vitamin proportion was; which could be due to a cooperative phenomenon and/or a stacking process. These studies would be useful for a better understanding of the β-LG properties as a carrier of hydrophobic vitamins or other hydrophobic nutraceuticals in order to enrich non-fat foods.Fil: Berino, Romina Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Báez, Germán David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Instituto Nacional de Tecnología Agropecuaria; ArgentinaFil: Llopart, Emilce Elina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentin

Characterisation of beta‐lactoglobulin/sodium alginate dry films

Optimum beta-lactoglobulin/sodium alginate dry films (β-LG/SA(S)) formed from casting solutions containing β-LG 1.25% (w/v) and SA 1% (w/v) showed appropriate characteristics to be easily handled. SEM micrographs showed a less homogeneous microstructure of this films respect to sodium alginate dry films used as control (SA(F)). Tensile strength of 18 MPa and an elongation value of 5% were obtained for β-LG/SA(S). DSC thermograms did not demonstrate changes in thermal properties of SA in presence of β-LG. Studies based on fluorescence quenching by acrylamide did not show variations in the tertiary structure of β-LG when β-LG/SA(S) were dissolved in an aqueous environment. In addition, binding properties of the protein were similar to the native one when an alquilsulfonate compound was used as ligand. The maintenance of native binding properties of β-LG after the films’ dissolution would allow the development of new carriers for food bioactive compounds based on β-LG/SA(S) dry films.Fil: Báez, Germán David. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Llopart, Emilce Elina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas.; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Berino, Romina Paola. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Verdini, Roxana Andrea. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentin

Formación de nanocomplejos entre polifenoles de cáscaras de manzanas y beta-lactoglobulina para su potencial aplicación en alimentos funcionales = Nanocomplexes formation between polyphenols of apple peels and beta-lactoglobulin for their potential application in functional foods

Los polifenoles (PF) ejercen una importante in?uencia sobre la salud humana, principalmente por su capacidad antioxidante. Las manzanas poseen PF principalmente en su cáscara. La proteína mayoritaria del lactosuero, la beta-lactoglobulina (?-lg), puede unir compuestos anffílicos, como PF, protegiéndolos de agentes externos. Se estudió la posibilidad de vehiculizar PF de cáscara de manzanas rojas (Red Delicious), formando nanocomplejos (NC) con ?-lg. El contenido de PF de cáscara de manzana roja ensayada fue de 266 ± 2 mg AG/100 g. Por ultrafltración se determinó que el 57% formó NC con ?-lg. Por medidas de extinción de la ?uorescencia de los PF sobre ?-lg se confrmó la formación de un complejo estático entre PF y ?-lg. Las experiencias de extinción de la ?uorescencia con acrilamida no mostraron diferencia signifcativa ante la presencia de PF, indicando que los PF se unen a un sitio distinto al del bolsillo hidrofóbico de la proteína. El tamaño de partícula y el potencial ? de ?-lg no se modifcaron por agregado de PF. Se observó que la mayor parte de los PF forman NC con ?-lg. Son necesarios más estudios para caracterizar el complejo con la fnalidad de utilizarlo para enriquecer alimentos

Acid-induced aggregation and gelation of heat-treated chia proteins

This work studied for the first time the acid-induced aggregation and gelation of heat-treated chia protein isolates obtained by extraction at pH 10 or 12 (CPI10 and CPI12, respectively). The aggregation state of proteins was modified during acidification. The size of the aggregates was reduced for both samples when the pH decreased but below pH 4.5 further protein aggregation took place for CPI12. Gelation of CPI12 was completed after about 30 min of acidification with glucone-δ-lactone. By contrast, this period was not enough to reach a constant value in G′ for CPI10. When gelation was ensured, confocal laser scanning micrographs from those gels revealed a coarse and irregular structure with large pores (median size of diameters: 30 μm). Instead, micrographs from CPI12 cold gels showed a more regular and interconnected network, with smaller pores (median size of diameters: 9 μm). These differences are consistent with a higher elastic behaviour ((Formula presented.) = 13.6 ± 0.1 Pa).Fil: López, Débora Natalia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Ingrassia, Romina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Wagner, Jorge Ricardo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Spelzini, Darío. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentin

Physicochemical and mechanical properties of a new cold-set emulsion gel system and the effect of quinoa protein fortification

A new approach for soft and self-sustainable oil-in-water emulsion gel systems (EGs) preparation based on a formulation with olive oil, sodium alginate, citric acid, and calcium chloride, and the combination of high-speed homogenization and gelation induction by glucono-δ-lactone addition is presented. Also, the effect of EG protein fortification by the incorporation of quinoa concentrate (QC) and quinoa flour on the physicochemical and mechanical properties of these EGs upon storage at 4 ◦C was investigated. Despite soft and self-sustainable EGs (10 g/kg and 20 g/kg alginate, respectively) showed higher oil droplet size increment with total biopolymer concentration, these systems presented remarkable stability during 28 days. All fortified EGs showed higher fluid retention capacity (>99%), L*, a*, and lower b* values. After one day, EGs presented pHs ranging 4.1–4.3, and longer storage times promoted an increased acidity, to a less extent for QC-fortified-EGs. Lipid oxidation degree also increased during storage (from 30 to 150 μmol/L malonaldehyde), with no significant effects upon protein fortification. Protein fortification promoted higher gel strength in all self-sustainable EGs (from 3.5 N to almost 7 N), and especially after 14 days for soft-EGs. These EGs can be used in the food industry as fat replacers to formulate healthier products.Fil: Ingrassia, Romina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Argentina.Fil: Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias. Argentina.Fil:Ingrassia, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Argentina.Fil: Busti, Pablo Andrés. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Argentina.Fil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Argentina.Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Argentina.Fil: Boeris, Valeria. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería Del Rosario. Argentina

Heat treatment of calcium alginate films obtained by ultrasonic atomizing: physicochemical characterization

Planar films of calcium alginate were obtained using an ultrasonic atomizing device. Sodium alginate solutions of 0.6% and 0.9% (w/v) were nebulized with calcium gluconolactate solutions (gelling agent) of 0, 1, 2 and 3% (w/v) at a flow rate of 0.3 mL min−1 for 20 min. After drying, thickness and mechanical properties were determined. In view of the results of mechanical properties, manageability and flexibility, calcium alginate films obtained using 0.9% sodium alginate and 2% calcium gluconolactate were selected as “optimum dry film” samples. These samples were cut into rectangular pieces and heated at 180 °C for 0, 4, 8, 12, 20 and 24 min. Thickness, mechanical and optical properties, differential scanning calorimetry (DSC) thermograms, Fourier transform infrared spectroscopy (FTIR) spectra, and scanning electron microscopy (SEM) micrographs were analyzed in order to characterize the physicochemical properties of heat-treated samples. The heat treatment produced thickness reduction, a yellow ochre color development and an increase in the brittleness of the films. DSC, FTIR and SEM studies suggested that heat treatment produced further dehydration of dry films and thermal dehydration–degradation of alginate macromolecules.Fil: Soazo, Marina del Valle. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario (IQUIR–CONICET); Argentina.Fil: Báez, Germán David. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario (IQUIR–CONICET); Argentina.Fil: Barboza, Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.Fil: Busti, Pablo Andrés. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.Fil: Rubiolo, Amelia Catalina. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química (UNL-CONICET); Argentina.Fil: Verdini, Roxana Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario (IQUIR–CONICET); Argentina.Fil: Delorenzi, Néstor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina