Dilatational properties of soy globulin adsorbed films at the air–water interface from acidic solutions

• Autores: Rodríguez Patino, Juan M.; Rodríguez Niño, María Rosario; Carrera Sánchez, Cecilio; Molina Ortiz, Sara Eugenia; Añon, Maria Cristina
• Año de publicación: 2005
• Idioma: inglés
• Tipo de recurso: artículo
• Materia: Air–water interface; Food emulsifier; β-Conglycinin; Glycinin; Soy proteins; Adsorbed films; Surface rheology
• Institución: Consejo Nacional de Investigaciones Científicas y Técnicas

In this paper we present surface dilatational properties of soy globulins (b-conglycinin,glycinin, and reduced glycinin with 10 mM of dithiothreitol (DTT)) adsorbed on the air–water interface,as a function of adsorption time. The surface rheological parameters (surface dilatational modulus, E,its elastic and viscous components,and phase angle) were measured as a function of protein concentration (ranging from 1 to 1 · 103%,wt/wt) at pH 2.0 and 5.0. We found that the surface dilatational modulus, E,increases with time, h. This phenomenon has been related to protein adsorption,unfolding, and/or protein–protein interactions (at long-term adsorption). The dilatational properties of the adsorbed films depend on the molecular structure of the protein,the pH,and on the protein concentration in the aqueous phase. Soy globulins are adsorbed at the air–water interface with different degrees of association at different concentrations in the bulk phase and at different aqueous phase pH.b-conglycinin,glycinin, and reduced glycinin with 10 mM of dithiothreitol (DTT)) adsorbed on the air–water interface,as a function of adsorption time. The surface rheological parameters (surface dilatational modulus, E,its elastic and viscous components,and phase angle) were measured as a function of protein concentration (ranging from 1 to 1 · 103%,wt/wt) at pH 2.0 and 5.0. We found that the surface dilatational modulus, E,increases with time, h. This phenomenon has been related to protein adsorption,unfolding, and/or protein–protein interactions (at long-term adsorption). The dilatational properties of the adsorbed films depend on the molecular structure of the protein,the pH,and on the protein concentration in the aqueous phase. Soy globulins are adsorbed at the air–water interface with different degrees of association at different concentrations in the bulk phase and at different aqueous phase pH.E,its elastic and viscous components,and phase angle) were measured as a function of protein concentration (ranging from 1 to 1 · 103%,wt/wt) at pH 2.0 and 5.0. We found that the surface dilatational modulus, E,increases with time, h. This phenomenon has been related to protein adsorption,unfolding, and/or protein–protein interactions (at long-term adsorption). The dilatational properties of the adsorbed films depend on the molecular structure of the protein,the pH,and on the protein concentration in the aqueous phase. Soy globulins are adsorbed at the air–water interface with different degrees of association at different concentrations in the bulk phase and at different aqueous phase pH.· 103%,wt/wt) at pH 2.0 and 5.0. We found that the surface dilatational modulus, E,increases with time, h. This phenomenon has been related to protein adsorption,unfolding, and/or protein–protein interactions (at long-term adsorption). The dilatational properties of the adsorbed films depend on the molecular structure of the protein,the pH,and on the protein concentration in the aqueous phase. Soy globulins are adsorbed at the air–water interface with different degrees of association at different concentrations in the bulk phase and at different aqueous phase pH.h. This phenomenon has been related to protein adsorption,unfolding, and/or protein–protein interactions (at long-term adsorption). The dilatational properties of the adsorbed films depend on the molecular structure of the protein,the pH,and on the protein concentration in the aqueous phase. Soy globulins are adsorbed at the air–water interface with different degrees of association at different concentrations in the bulk phase and at different aqueous phase pH.
Fil: Rodríguez Patino, Juan M.. Universidad de Sevilla; España
Fil: Rodríguez Niño, María Rosario. Universidad de Sevilla; España
Fil: Carrera Sánchez, Cecilio. Universidad de Sevilla; España
Fil: Molina Ortiz, Sara Eugenia. 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