Amaranth protein films from thermally treated proteins

Autores
Condes, María Cecilia; Añon, Maria Cristina; Mauri, Adriana Noemi
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The usefulness of amaranth protein isolates, native and thermally treated, in edible films preparation was studied. Protein films were prepared by casting using glycerol as plasticizer. Films from amaranth native protein isolates showed low water vapor permeability (WVP) but poor mechanical properties. In order to improve this functionality, proteins were treated at 70 and 90 C which corresponds to the denaturation temperature of the protein fractions present in the isolates. The unfolded conformation of these thermally treated proteins, when partially or totally denatured, favors the interactions between polypeptide chains during the film formation. These interactions lead to a greater cross-linking degree, which was reflected in the lower amount of water-soluble free peptides that were linked to the matrix. In these thermally treated protein films, a greatest contribution of disulfide and hydrogen bonds to the films stabilization was observed. These changes in the films structural properties would confer them a greater tensile strength and lower water solubility but higher thickness and WVP.
Fil: Condes, María Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Mauri, Adriana Noemi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Materia
Protein Films
Amaranth Proteins
Thermal Treatment
Protein Cross-Linking
Mechanical Properties
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10342
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/10342
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Amaranth protein films from thermally treated proteinsCondes, María CeciliaAñon, Maria CristinaMauri, Adriana NoemiProtein FilmsAmaranth ProteinsThermal TreatmentProtein Cross-LinkingMechanical Propertieshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The usefulness of amaranth protein isolates, native and thermally treated, in edible films preparation was studied. Protein films were prepared by casting using glycerol as plasticizer. Films from amaranth native protein isolates showed low water vapor permeability (WVP) but poor mechanical properties. In order to improve this functionality, proteins were treated at 70 and 90 C which corresponds to the denaturation temperature of the protein fractions present in the isolates. The unfolded conformation of these thermally treated proteins, when partially or totally denatured, favors the interactions between polypeptide chains during the film formation. These interactions lead to a greater cross-linking degree, which was reflected in the lower amount of water-soluble free peptides that were linked to the matrix. In these thermally treated protein films, a greatest contribution of disulfide and hydrogen bonds to the films stabilization was observed. These changes in the films structural properties would confer them a greater tensile strength and lower water solubility but higher thickness and WVP.Fil: Condes, María Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaFil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaFil: Mauri, Adriana Noemi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaElsevier2013-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10342Condes, María Cecilia; Añon, Maria Cristina; Mauri, Adriana Noemi; Amaranth protein films from thermally treated proteins; Elsevier; Journal Of Food Engineering; 119; 3; 12-2013; 573-5790260-8774enginfo:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1016/j.jfoodeng.2013.06.006info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0260877413002963info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:13:44Zoai:ri.conicet.gov.ar:11336/10342instacron: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 10:13:44.511CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Amaranth protein films from thermally treated proteins
title Amaranth protein films from thermally treated proteins
spellingShingle Amaranth protein films from thermally treated proteins
Condes, María Cecilia
Protein Films
Amaranth Proteins
Thermal Treatment
Protein Cross-Linking
Mechanical Properties
title_short Amaranth protein films from thermally treated proteins
title_full Amaranth protein films from thermally treated proteins
title_fullStr Amaranth protein films from thermally treated proteins
title_full_unstemmed Amaranth protein films from thermally treated proteins
title_sort Amaranth protein films from thermally treated proteins
dc.creator.none.fl_str_mv Condes, María Cecilia
Añon, Maria Cristina
Mauri, Adriana Noemi
author Condes, María Cecilia
author_facet Condes, María Cecilia
Añon, Maria Cristina
Mauri, Adriana Noemi
author_role author
author2 Añon, Maria Cristina
Mauri, Adriana Noemi
author2_role author
author
dc.subject.none.fl_str_mv Protein Films
Amaranth Proteins
Thermal Treatment
Protein Cross-Linking
Mechanical Properties
topic Protein Films
Amaranth Proteins
Thermal Treatment
Protein Cross-Linking
Mechanical Properties
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 usefulness of amaranth protein isolates, native and thermally treated, in edible films preparation was studied. Protein films were prepared by casting using glycerol as plasticizer. Films from amaranth native protein isolates showed low water vapor permeability (WVP) but poor mechanical properties. In order to improve this functionality, proteins were treated at 70 and 90 C which corresponds to the denaturation temperature of the protein fractions present in the isolates. The unfolded conformation of these thermally treated proteins, when partially or totally denatured, favors the interactions between polypeptide chains during the film formation. These interactions lead to a greater cross-linking degree, which was reflected in the lower amount of water-soluble free peptides that were linked to the matrix. In these thermally treated protein films, a greatest contribution of disulfide and hydrogen bonds to the films stabilization was observed. These changes in the films structural properties would confer them a greater tensile strength and lower water solubility but higher thickness and WVP.
Fil: Condes, María Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Mauri, Adriana Noemi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
description The usefulness of amaranth protein isolates, native and thermally treated, in edible films preparation was studied. Protein films were prepared by casting using glycerol as plasticizer. Films from amaranth native protein isolates showed low water vapor permeability (WVP) but poor mechanical properties. In order to improve this functionality, proteins were treated at 70 and 90 C which corresponds to the denaturation temperature of the protein fractions present in the isolates. The unfolded conformation of these thermally treated proteins, when partially or totally denatured, favors the interactions between polypeptide chains during the film formation. These interactions lead to a greater cross-linking degree, which was reflected in the lower amount of water-soluble free peptides that were linked to the matrix. In these thermally treated protein films, a greatest contribution of disulfide and hydrogen bonds to the films stabilization was observed. These changes in the films structural properties would confer them a greater tensile strength and lower water solubility but higher thickness and WVP.
publishDate 2013
dc.date.none.fl_str_mv 2013-12
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/11336/10342
Condes, María Cecilia; Añon, Maria Cristina; Mauri, Adriana Noemi; Amaranth protein films from thermally treated proteins; Elsevier; Journal Of Food Engineering; 119; 3; 12-2013; 573-579
0260-8774
url http://hdl.handle.net/11336/10342
identifier_str_mv Condes, María Cecilia; Añon, Maria Cristina; Mauri, Adriana Noemi; Amaranth protein films from thermally treated proteins; Elsevier; Journal Of Food Engineering; 119; 3; 12-2013; 573-579
0260-8774
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1016/j.jfoodeng.2013.06.006
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0260877413002963
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
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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score 13.070432

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