Structural and functional properties of soy protein isolate and cod gelatin blend films
- Autores
- Denavi, Gabriela Alejandra; Pérez Mateos, Miriam; Añon, Maria Cristina; Montero, Pilar; Mauri, Adriana Noemi; Gomez Guillén, M. Carmen
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The structure-function relationship of composite films obtained from soybean-protein isolate (SPI) and cod gelatin was studied. Films with different ratios of SPI:gelatin (0, 25, 50, 75, 100% [w/w]) and plasticized by a mixture of glycerol and sorbitol were prepared by casting. Regardless of the soybean-protein concentration, the thickness and water-vapor permeability of the composite films diminished significantly as compared to pure-gelatin films. The formulation containing 25% SPI: 75% cod-skin gelatin had the maximum force at the breaking point, which was 1.8-fold and 2.8-fold greater than those of 100% gelatin and 100% SPI films, respectively. Moreover, this formulation offered high percent-deformation values lower than those of gelatin but higher than all other films containing SPI-, and the same relatively low water-vapor permeability as the 100% SPI film. While all the films exhibited high water solubility, a slight reduction in film solubility and soluble protein was observed with increasing SPI concentration. Differential-scanning calorimetry analyses revealed that gelatin was completely denatured in all films, while soy proteins largely maintained their native conformation. Analysis by fourier-transform–infrared spectroscopy revealed that the presence of 25% SPI produced gelatin conformational changes, self-aggregation of gelatin chains, and intermolecular associations via Cdouble bondO bonds between gelatin and SPI proteins. All films were translucent in appearance, but the yellowish color increased with increasing proportions of the soybean proteins.
Fil: Denavi, Gabriela Alejandra. 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: Pérez Mateos, Miriam. Consejo Superior de Investigaciones Científicas; España
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
Fil: Montero, Pilar. Consejo Superior de Investigaciones Científicas; España
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
Fil: Gomez Guillén, M. Carmen. Consejo Superior de Investigaciones Científicas; España - Materia
-
COD GELATINE
EDIBLE FILMS
FTIR
MECHANICAL PROPERTIES
SOY PROTEINS
STRUCTURAL PROPERTIES
WATER VAPOR PERMEABILITY - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/136301
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oai:ri.conicet.gov.ar:11336/136301 |
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CONICET Digital (CONICET) |
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Structural and functional properties of soy protein isolate and cod gelatin blend filmsDenavi, Gabriela AlejandraPérez Mateos, MiriamAñon, Maria CristinaMontero, PilarMauri, Adriana NoemiGomez Guillén, M. CarmenCOD GELATINEEDIBLE FILMSFTIRMECHANICAL PROPERTIESSOY PROTEINSSTRUCTURAL PROPERTIESWATER VAPOR PERMEABILITYhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The structure-function relationship of composite films obtained from soybean-protein isolate (SPI) and cod gelatin was studied. Films with different ratios of SPI:gelatin (0, 25, 50, 75, 100% [w/w]) and plasticized by a mixture of glycerol and sorbitol were prepared by casting. Regardless of the soybean-protein concentration, the thickness and water-vapor permeability of the composite films diminished significantly as compared to pure-gelatin films. The formulation containing 25% SPI: 75% cod-skin gelatin had the maximum force at the breaking point, which was 1.8-fold and 2.8-fold greater than those of 100% gelatin and 100% SPI films, respectively. Moreover, this formulation offered high percent-deformation values lower than those of gelatin but higher than all other films containing SPI-, and the same relatively low water-vapor permeability as the 100% SPI film. While all the films exhibited high water solubility, a slight reduction in film solubility and soluble protein was observed with increasing SPI concentration. Differential-scanning calorimetry analyses revealed that gelatin was completely denatured in all films, while soy proteins largely maintained their native conformation. Analysis by fourier-transform–infrared spectroscopy revealed that the presence of 25% SPI produced gelatin conformational changes, self-aggregation of gelatin chains, and intermolecular associations via Cdouble bondO bonds between gelatin and SPI proteins. All films were translucent in appearance, but the yellowish color increased with increasing proportions of the soybean proteins.Fil: Denavi, Gabriela Alejandra. 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; ArgentinaFil: Pérez Mateos, Miriam. Consejo Superior de Investigaciones Científicas; EspañaFil: 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; ArgentinaFil: Montero, Pilar. Consejo Superior de Investigaciones Científicas; EspañaFil: 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; ArgentinaFil: Gomez Guillén, M. Carmen. Consejo Superior de Investigaciones Científicas; EspañaElsevier2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/136301Denavi, Gabriela Alejandra; Pérez Mateos, Miriam; Añon, Maria Cristina; Montero, Pilar; Mauri, Adriana Noemi; et al.; Structural and functional properties of soy protein isolate and cod gelatin blend films; Elsevier; Food Hydrocolloids; 23; 8; 12-2009; 2094-21010268-005X1873-7137CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2009.03.007info:eu-repo/semantics/altIdentifier/url/https://bit.ly/3ich18sinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:02:03Zoai:ri.conicet.gov.ar:11336/136301instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:02:03.863CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
title |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
spellingShingle |
Structural and functional properties of soy protein isolate and cod gelatin blend films Denavi, Gabriela Alejandra COD GELATINE EDIBLE FILMS FTIR MECHANICAL PROPERTIES SOY PROTEINS STRUCTURAL PROPERTIES WATER VAPOR PERMEABILITY |
title_short |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
title_full |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
title_fullStr |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
title_full_unstemmed |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
title_sort |
Structural and functional properties of soy protein isolate and cod gelatin blend films |
dc.creator.none.fl_str_mv |
Denavi, Gabriela Alejandra Pérez Mateos, Miriam Añon, Maria Cristina Montero, Pilar Mauri, Adriana Noemi Gomez Guillén, M. Carmen |
author |
Denavi, Gabriela Alejandra |
author_facet |
Denavi, Gabriela Alejandra Pérez Mateos, Miriam Añon, Maria Cristina Montero, Pilar Mauri, Adriana Noemi Gomez Guillén, M. Carmen |
author_role |
author |
author2 |
Pérez Mateos, Miriam Añon, Maria Cristina Montero, Pilar Mauri, Adriana Noemi Gomez Guillén, M. Carmen |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
COD GELATINE EDIBLE FILMS FTIR MECHANICAL PROPERTIES SOY PROTEINS STRUCTURAL PROPERTIES WATER VAPOR PERMEABILITY |
topic |
COD GELATINE EDIBLE FILMS FTIR MECHANICAL PROPERTIES SOY PROTEINS STRUCTURAL PROPERTIES WATER VAPOR PERMEABILITY |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
The structure-function relationship of composite films obtained from soybean-protein isolate (SPI) and cod gelatin was studied. Films with different ratios of SPI:gelatin (0, 25, 50, 75, 100% [w/w]) and plasticized by a mixture of glycerol and sorbitol were prepared by casting. Regardless of the soybean-protein concentration, the thickness and water-vapor permeability of the composite films diminished significantly as compared to pure-gelatin films. The formulation containing 25% SPI: 75% cod-skin gelatin had the maximum force at the breaking point, which was 1.8-fold and 2.8-fold greater than those of 100% gelatin and 100% SPI films, respectively. Moreover, this formulation offered high percent-deformation values lower than those of gelatin but higher than all other films containing SPI-, and the same relatively low water-vapor permeability as the 100% SPI film. While all the films exhibited high water solubility, a slight reduction in film solubility and soluble protein was observed with increasing SPI concentration. Differential-scanning calorimetry analyses revealed that gelatin was completely denatured in all films, while soy proteins largely maintained their native conformation. Analysis by fourier-transform–infrared spectroscopy revealed that the presence of 25% SPI produced gelatin conformational changes, self-aggregation of gelatin chains, and intermolecular associations via Cdouble bondO bonds between gelatin and SPI proteins. All films were translucent in appearance, but the yellowish color increased with increasing proportions of the soybean proteins. Fil: Denavi, Gabriela Alejandra. 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: Pérez Mateos, Miriam. Consejo Superior de Investigaciones Científicas; España 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 Fil: Montero, Pilar. Consejo Superior de Investigaciones Científicas; España 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 Fil: Gomez Guillén, M. Carmen. Consejo Superior de Investigaciones Científicas; España |
description |
The structure-function relationship of composite films obtained from soybean-protein isolate (SPI) and cod gelatin was studied. Films with different ratios of SPI:gelatin (0, 25, 50, 75, 100% [w/w]) and plasticized by a mixture of glycerol and sorbitol were prepared by casting. Regardless of the soybean-protein concentration, the thickness and water-vapor permeability of the composite films diminished significantly as compared to pure-gelatin films. The formulation containing 25% SPI: 75% cod-skin gelatin had the maximum force at the breaking point, which was 1.8-fold and 2.8-fold greater than those of 100% gelatin and 100% SPI films, respectively. Moreover, this formulation offered high percent-deformation values lower than those of gelatin but higher than all other films containing SPI-, and the same relatively low water-vapor permeability as the 100% SPI film. While all the films exhibited high water solubility, a slight reduction in film solubility and soluble protein was observed with increasing SPI concentration. Differential-scanning calorimetry analyses revealed that gelatin was completely denatured in all films, while soy proteins largely maintained their native conformation. Analysis by fourier-transform–infrared spectroscopy revealed that the presence of 25% SPI produced gelatin conformational changes, self-aggregation of gelatin chains, and intermolecular associations via Cdouble bondO bonds between gelatin and SPI proteins. All films were translucent in appearance, but the yellowish color increased with increasing proportions of the soybean proteins. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-12 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/136301 Denavi, Gabriela Alejandra; Pérez Mateos, Miriam; Añon, Maria Cristina; Montero, Pilar; Mauri, Adriana Noemi; et al.; Structural and functional properties of soy protein isolate and cod gelatin blend films; Elsevier; Food Hydrocolloids; 23; 8; 12-2009; 2094-2101 0268-005X 1873-7137 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/136301 |
identifier_str_mv |
Denavi, Gabriela Alejandra; Pérez Mateos, Miriam; Añon, Maria Cristina; Montero, Pilar; Mauri, Adriana Noemi; et al.; Structural and functional properties of soy protein isolate and cod gelatin blend films; Elsevier; Food Hydrocolloids; 23; 8; 12-2009; 2094-2101 0268-005X 1873-7137 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2009.03.007 info:eu-repo/semantics/altIdentifier/url/https://bit.ly/3ich18s |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844613820736077824 |
score |
13.070432 |