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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/10226
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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 Técnicas2025-09-29T09:32:45Zoai: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:34982025-09-29 09:32:45.995CONICET 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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1844613001112453120 |
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13.070432 |