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dc.contributor.author
Echeverría, Ignacio
dc.contributor.author
Eisenberg, Patricia
dc.contributor.author
Mauri, Adriana Noemi
dc.date.available
2016-12-26T20:59:41Z
dc.date.issued
2014-01
dc.identifier.citation
Echeverría, Ignacio; Eisenberg, Patricia; Mauri, Adriana Noemi; Nanocomposites films based on soy proteins and montmorillonite processed by casting; Elsevier Science; Journal of Membrane Science; 449; 1-2014; 15-26
dc.identifier.issn
0376-7388
dc.identifier.uri
http://hdl.handle.net/11336/10246
dc.description.abstract
In this work the effect of montmorillonite (MMT) addition to soy-protein-based films on the physicochemical properties of the resulting nanocomposites was studied and the structure–function relationship of these materials and the changes in phase structures, due to different interactions among the material components were analyzed. Flexible nanocomposite films consisting in a soy-protein (SP) matrix supplemented with different concentrations of montmorillonite (MMT) up to 10 g/100 g of SP were prepared by the casting technique. The resulting films were homogeneous, yellowish, and transparent and indistinguishable visually from films of pure protein. The process used for film formation—involving mechanical agitation and ultrasonication, in combination with the intrinsic affinity of MMT for the SPs—favors the dispersion of the clay so as to reach a high degree of intercalation into the protein matrix with consequent exfoliation of the layers of MMT among the proteins (verified by both transmission electron microscopy and X-ray diffraction). The efficient dispersion and distribution of the MMT laminas within the films generated a significant strengthening of the nanolayer that was evident in the observed resistance to breakage; modulation of elasticity; and decrease in extension, moisture content, solubility, and permeability to water vapor. In the presence of MMT, the disulfide bridges in the SPs play a critical role in the stabilization of the protein matrix, whereas in the films composed of proteins alone the residues capable of participating in hydrogen bonding would be involved in other types of highly stabilizing interactions.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
BIODEGRADABLE FILMS
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BIONANOCOMPOSITES
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CASTING
dc.subject
MONTMORILLONITE
dc.subject
SOY PROTEINS
dc.subject.classification
Recubrimientos y Películas
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Ingeniería de los Materiales
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Nanocomposites films based on soy proteins and montmorillonite processed by casting
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-12-12T14:08:40Z
dc.journal.volume
449
dc.journal.pagination
15-26
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Echeverría, Ignacio. 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
dc.description.fil
Fil: Eisenberg, Patricia. Instituto Nacional de Tecnologia Industrial; Argentina
dc.description.fil
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
dc.journal.title
Journal of Membrane Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.memsci.2013.08.006
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0376738813006492
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