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Dive into the research topics where Víctor M. Pizones Ruiz-Henestrosa is active.

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Featured researches published by Víctor M. Pizones Ruiz-Henestrosa.


Ultrasonics Sonochemistry | 2015

Modification of foaming properties of soy protein isolate by high ultrasound intensity: Particle size effect

Rocío Morales; Karina D. Martínez; Víctor M. Pizones Ruiz-Henestrosa; Ana M.R. Pilosof

The effect of high intensity ultrasound (HIUS) may produce structural modifications on proteins through a friendly environmental process. Thus, it can be possible to obtain aggregates with a determined particle size, and altering a defined functional property at the same time. The objective of this work was to explore the impact of HIUS on the functionality of a denatured soy protein isolate (SPI) on foaming and interfacial properties. SPI solutions at pH 6.9 were treated with HIUS for 20 min, in an ultrasonic processor at room temperature, at 75, 80 and 85°C. The operating conditions were: 20 kHz, 4.27 ± 0.71 W and 20% of amplitude. It was determined the size of the protein particles, before and after the HIUS treatment, by dynamic light scattering. It was also analyzed the interfacial behavior of the different systems as well as their foaming properties, by applying the whipping method. The HIUS treatment and HIUS with temperature improved the foaming capacity by alteration of particle size whereas stability was not modified significantly. The temperature of HIUS treatment (80 and 85°C) showed a synergistic effect on foaming capacity. It was found that the reduction of particle size was related to the increase of foaming capacity of SPI. On the other hand, the invariable elasticity of the interfacial films could explain the stability of foams over time.


Journal of Agricultural and Food Chemistry | 2008

Effect of sucrose on functional properties of soy globulins: adsorption and foam characteristics.

Víctor M. Pizones Ruiz-Henestrosa; Cecilio Carrera Sánchez; Juan M. Rodríguez Patino

In this contribution, we have analyzed the effect of sucrose on dynamic interfacial (dynamic surface pressure and surface dilatational properties) and foaming (foam capacity and foam stability) characteristics of soy globulins (7S and 11S). The protein (at 1 x 10(-3), 1 x 10(-2), 0.1, and 1 wt %) and sucrose (at 0, 0.25, 0.5, and 1.0 M) concentrations in aqueous solution and the pH (at 5 and 7), and ionic strength (at 0.05 and 0.5 M) were analyzed as variables. The temperature was maintained constant at 20 degrees C. We have observed the following. (i) The dynamics of adsorption (presence of a lag period, diffusion, and penetration at the air-water interface) of soy globulins depend on the peculiar molecular features of proteins (7S or 11S soy globulin) and the level of association/dissociation of these proteins by varying the pH and ionic strength, as well as the effect of sucrose in the aqueous phase on the unfolding of the protein. The rate of adsorption increases with the protein concentration in solution, at pH 7 compared to pH 5, at high ionic strength, and in the absence of sucrose. (ii) The surface dilatational properties reflect the fact that soy globulin adsorbed films exhibit viscoelastic behavior. The surface dilatational modulus increases at pH 7 compared to pH 5, but decreases with the addition of sucrose into the aqueous phase. (iii) The rate of adsorption and surface dilatational properties (surface dilatational modulus and phase angle) during adsorption at the air-water interface play an important role in the formation of foams generated from aqueous solutions of soy globulins. (iv) The increased interfacial adsorption (at high surface pressures) and the combined effects of interfacial adsorption and interfacial interactions between adsorbed soy globulin molecules (at high surface dilatational modulus) can explain the higher stability of the foam, with few exceptions.


Colloids and Surfaces B: Biointerfaces | 2012

Interfacial and foaming interactions between casein glycomacropeptide (CMP) and propylene glycol alginate

María J. Martinez; Víctor M. Pizones Ruiz-Henestrosa; Cecilio Carrera Sánchez; Juan M. Rodríguez Patino; Ana M.R. Pilosof

Proteins and polysaccharides are widely used in food formulation. While most of the proteins are surface active, only few polysaccharides can adsorb at the air-water interface; this is the case of propylene glycol alginates (PGA). It is known that casein glycomacropeptide (CMP), a bioactive polypeptide derived from κ-casein by the action of chymosin, presents a great foaming capacity but provides unstable foams. So, the objective of this work was to analyze the impact of mixing CMP and a commercial variety of PGA, Kelcoloid O (KO), on the interfacial and foaming properties at pH 7.0. It was determined the surface pressure isotherm, the dynamics of adsorption and the foaming properties for CMP, KO and the mixed system CMP-KO. CMP dominated the surface pressure of CMP-KO mixed system. The presence of KO synergistically improved the viscoelastic properties of surface film. The foaming capacity of CMP was altered by KO. KO foam presented a higher stability than CMP foam and it controlled the stability against drainage and the initial collapse in the mixed foam.


Colloids and Surfaces B: Biointerfaces | 2017

Synergistic performance of lecithin and glycerol monostearate in oil/water emulsions

María I. Moran-Valero; Víctor M. Pizones Ruiz-Henestrosa; Ana M.R. Pilosof

The effects of the combination of two low-molecular weight emulsifiers (lecithin and glycerol-monostearate (GMS)) on the stability, the dynamic interfacial properties and rheology of emulsions have been studied. Different lecithin/GMS ratios were tested in order to assess their impact in the formation and stabilization of oil in water emulsions. The combination of the two surfactants showed a synergistic behaviour, mainly when combined at the same ratio. The dynamic film properties and ζ-potential showed that lecithin dominated the surface of oil droplets, providing stability to the emulsions against flocculation and coalescence, while allowing the formation of small oil droplets. At long times of adsorption, all of the mixtures showed similar interfacial activity. However, higher values of interfacial pressure at the initial times were reached when lecithin and GMS were at the same ratio. Interfacial viscoelasticity and viscosity of mixed films were also similar to that of lecithin alone. On the other hand, emulsions viscosity was dominated by GMS. The synergistic performance of lecithin-GMS blends as stabilizers of oil/water emulsions is attributed to their interaction both in the bulk and at the interface.


Carbohydrate Polymers | 2015

Behaviour of cyanidin-3-glucoside, β-lactoglobulin and polysaccharides nanoparticles in bulk and oil-in-water interfaces

Ana Emília Figueiredo de Oliveira; Víctor M. Pizones Ruiz-Henestrosa; Mariana von Staszewski; Ana M.R. Pilosof; Manuela Pintado

Particle size distributions as well the interfacial and rheological properties of the films at the oil/water interface were used to study the effect of the interacting system between β-lactoglobulin, cyanidin-3-glucoside and pectin or chitosan in buffer solutions. The particles obtained were smaller with cy-3-gluc-β-lg-pectin and had reduced polydispersity with cy-3-gluc-β-lg-chitosan. Based on time dependent surface pressure results, β-lg-pectin mixtures showed a slower increase at the beginning of the measurement, while β-lg-chitosan mixtures showed no differences with β-lg alone. Contrarily, dilatational properties increased for ternary chitosan mixtures, but they remained similar to the pure protein in ternary pectin mixtures. Cy-3-gluc interfacial properties were reduced by the presence of pectin and chitosan. The interactions between cy-3-gluc and the biopolymers that have been selected in the present work resulted in a lower content of free polyphenol, reduced antioxidant properties as well as free β-lg. The impact of this effect was more relevant when pectin was used.


Colloids and Surfaces A: Physicochemical and Engineering Aspects | 2007

Interfacial and foaming characteristics of soy globulins as a function of pH and ionic strength

Víctor M. Pizones Ruiz-Henestrosa; Cecilio Carrera Sánchez; María del Mar Yust Escobar; Justo J. Pedroche Jiménez; Francisco Rodríguez; Juan M. Rodríguez Patino


Food Hydrocolloids | 2005

Milk and soy protein films at the air–water interface

M. Rosario Rodríguez Niño; Cecilio Carrera Sánchez; Víctor M. Pizones Ruiz-Henestrosa; Juan M. Rodríguez Patino


Food Hydrocolloids | 2007

Soy protein–polysaccharides interactions at the air–water interface

Karina D. Martínez; Cecilio Carrera Sánchez; Víctor M. Pizones Ruiz-Henestrosa; Juan M. Rodríguez Patino; Ana M.R. Pilosof


Food Hydrocolloids | 2014

Green tea polyphenols-β-lactoglobulin nanocomplexes: Interfacial behavior, emulsification and oxidation stability of fish oil

Mariana von Staszewski; Víctor M. Pizones Ruiz-Henestrosa; Ana M.R. Pilosof


Food Hydrocolloids | 2007

Effect of limited hydrolysis of soy protein on the interactions with polysaccharides at the air–water interface

Karina D. Martínez; Cecilio Carrera Sánchez; Víctor M. Pizones Ruiz-Henestrosa; Juan M. Rodríguez Patino; Ana M.R. Pilosof

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Ana M.R. Pilosof

Facultad de Ciencias Exactas y Naturales

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Karina D. Martínez

Facultad de Ciencias Exactas y Naturales

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Mariana von Staszewski

Facultad de Ciencias Exactas y Naturales

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María J. Martinez

Facultad de Ciencias Exactas y Naturales

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Fernando A. Bellesi

Facultad de Ciencias Exactas y Naturales

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Manuela Pintado

The Catholic University of America

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Francisco Millán

Spanish National Research Council

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Justo Pedroche

Spanish National Research Council

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