dc.creatorRodríguez Patino, Juan M.
dc.creatorRodríguez Niño, María Rosario
dc.creatorCarrera Sánchez, Cecilio
dc.creatorMolina Ortiz, Sara Eugenia
dc.creatorAñon, Maria Cristina
dc.date.accessioned2022-06-03T13:23:05Z
dc.date.accessioned2022-10-15T16:02:42Z
dc.date.available2022-06-03T13:23:05Z
dc.date.available2022-10-15T16:02:42Z
dc.date.created2022-06-03T13:23:05Z
dc.date.issued2005-06
dc.identifierRodríguez Patino, Juan M.; Rodríguez Niño, María Rosario; Carrera Sánchez, Cecilio; Molina Ortiz, Sara Eugenia; Añon, Maria Cristina; Dilatational properties of soy globulin adsorbed films at the air–water interface from acidic solutions; Elsevier; Journal of Food Engineering; 68; 4; 6-2005; 429-437
dc.identifier0260-8774
dc.identifierhttp://hdl.handle.net/11336/158845
dc.identifier1873-5770
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4406484
dc.description.abstractIn 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.
dc.languageeng
dc.publisherElsevier
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0260877404003024#!
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jfoodeng.2004.06.020
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAir–water interface
dc.subjectFood emulsifier
dc.subjectβ-Conglycinin
dc.subjectGlycinin
dc.subjectSoy proteins
dc.subjectAdsorbed films
dc.subjectSurface rheology
dc.titleDilatational properties of soy globulin adsorbed films at the air–water interface from acidic solutions
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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