Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1

Autores
Bolontrade, Agustín Juan; Scilingo, Adriana Alicia; Añon, Maria Cristina
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This work has focused on the study of the relationships between the structural changes in proteins of amaranth under different conditions of pH and ionic strength and the ability to form foam, also taking into consideration the kinetics of adsorption of proteins at the interface. Results showed that treatment at pH 2.0 significantly improves the foaming properties of amaranth proteins. The structural studies performed indicate that amaranth proteins at acidic pH are denatured, dissociated and undergo partial hydrolysis due to the existence of an endoprotease. They also present a lower content of -sheet and random coil secondary structures. Diffusion–adsorption studies of proteins at the air:water interface allowed to determine that the acidic pH favors adsorption thereof (higher values of kdiff and ka) and reduces the need for a rearrangement (higher values of r). The interfacial behavior of amaranth proteins is a direct consequence of the structural changes they undergo at acidic pH, changes that also were reflected on the increased foaming capacity (higher vo) thus forming more dense and homogeneous foams. The behavior of the soluble proteins as surfactants was not altered by the presence of protein aggregates and insoluble proteins.
Fil: Bolontrade, Agustín Juan. 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: Scilingo, Adriana Alicia. 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
Materia
Amaranth Proteins
Interface Air/Water
Foam Formation
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:11336/10226
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1Bolontrade, Agustín JuanScilingo, Adriana AliciaAñon, Maria CristinaAmaranth ProteinsInterface Air/WaterFoam Formationhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2This work has focused on the study of the relationships between the structural changes in proteins of amaranth under different conditions of pH and ionic strength and the ability to form foam, also taking into consideration the kinetics of adsorption of proteins at the interface. Results showed that treatment at pH 2.0 significantly improves the foaming properties of amaranth proteins. The structural studies performed indicate that amaranth proteins at acidic pH are denatured, dissociated and undergo partial hydrolysis due to the existence of an endoprotease. They also present a lower content of -sheet and random coil secondary structures. Diffusion–adsorption studies of proteins at the air:water interface allowed to determine that the acidic pH favors adsorption thereof (higher values of kdiff and ka) and reduces the need for a rearrangement (higher values of r). The interfacial behavior of amaranth proteins is a direct consequence of the structural changes they undergo at acidic pH, changes that also were reflected on the increased foaming capacity (higher vo) thus forming more dense and homogeneous foams. The behavior of the soluble proteins as surfactants was not altered by the presence of protein aggregates and insoluble proteins.Fil: Bolontrade, Agustín Juan. 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: Scilingo, Adriana Alicia. 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; ArgentinaElsevier Science2013-05info: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/11336/10226Bolontrade, Agustín Juan; Scilingo, Adriana Alicia; Añon, Maria Cristina; Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1; Elsevier Science; Colloids And Surfaces B: Biointerfaces; 105; 5-2013; 319-3270927-7765enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2012.12.039info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/23384694info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:00:44Zoai:ri.conicet.gov.ar:11336/10226instacron: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:34982025-10-22 11:00:44.979CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
title Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
spellingShingle Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
Bolontrade, Agustín Juan
Amaranth Proteins
Interface Air/Water
Foam Formation
title_short Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
title_full Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
title_fullStr Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
title_full_unstemmed Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
title_sort Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1
dc.creator.none.fl_str_mv Bolontrade, Agustín Juan
Scilingo, Adriana Alicia
Añon, Maria Cristina
author Bolontrade, Agustín Juan
author_facet Bolontrade, Agustín Juan
Scilingo, Adriana Alicia
Añon, Maria Cristina
author_role author
author2 Scilingo, Adriana Alicia
Añon, Maria Cristina
author2_role author
author
dc.subject.none.fl_str_mv Amaranth Proteins
Interface Air/Water
Foam Formation
topic Amaranth Proteins
Interface Air/Water
Foam Formation
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv This work has focused on the study of the relationships between the structural changes in proteins of amaranth under different conditions of pH and ionic strength and the ability to form foam, also taking into consideration the kinetics of adsorption of proteins at the interface. Results showed that treatment at pH 2.0 significantly improves the foaming properties of amaranth proteins. The structural studies performed indicate that amaranth proteins at acidic pH are denatured, dissociated and undergo partial hydrolysis due to the existence of an endoprotease. They also present a lower content of -sheet and random coil secondary structures. Diffusion–adsorption studies of proteins at the air:water interface allowed to determine that the acidic pH favors adsorption thereof (higher values of kdiff and ka) and reduces the need for a rearrangement (higher values of r). The interfacial behavior of amaranth proteins is a direct consequence of the structural changes they undergo at acidic pH, changes that also were reflected on the increased foaming capacity (higher vo) thus forming more dense and homogeneous foams. The behavior of the soluble proteins as surfactants was not altered by the presence of protein aggregates and insoluble proteins.
Fil: Bolontrade, Agustín Juan. 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: Scilingo, Adriana Alicia. 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
description This work has focused on the study of the relationships between the structural changes in proteins of amaranth under different conditions of pH and ionic strength and the ability to form foam, also taking into consideration the kinetics of adsorption of proteins at the interface. Results showed that treatment at pH 2.0 significantly improves the foaming properties of amaranth proteins. The structural studies performed indicate that amaranth proteins at acidic pH are denatured, dissociated and undergo partial hydrolysis due to the existence of an endoprotease. They also present a lower content of -sheet and random coil secondary structures. Diffusion–adsorption studies of proteins at the air:water interface allowed to determine that the acidic pH favors adsorption thereof (higher values of kdiff and ka) and reduces the need for a rearrangement (higher values of r). The interfacial behavior of amaranth proteins is a direct consequence of the structural changes they undergo at acidic pH, changes that also were reflected on the increased foaming capacity (higher vo) thus forming more dense and homogeneous foams. The behavior of the soluble proteins as surfactants was not altered by the presence of protein aggregates and insoluble proteins.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/10226
Bolontrade, Agustín Juan; Scilingo, Adriana Alicia; Añon, Maria Cristina; Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1; Elsevier Science; Colloids And Surfaces B: Biointerfaces; 105; 5-2013; 319-327
0927-7765
url http://hdl.handle.net/11336/10226
identifier_str_mv Bolontrade, Agustín Juan; Scilingo, Adriana Alicia; Añon, Maria Cristina; Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1; Elsevier Science; Colloids And Surfaces B: Biointerfaces; 105; 5-2013; 319-327
0927-7765
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2012.12.039
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/23384694
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 Science
publisher.none.fl_str_mv Elsevier Science
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 12.982451

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