Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH

Autores
Ventureira, Jorge Luis; Bolontrade, Agustín Juan; Speroni Aguirre, Francisco; David Briand, Elisabeth; Scilingo, Adriana Alicia; Ropers, Marie-Hélène; Boury, Frank; Añón, María Cristina; Anton, Marc
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Amaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties. Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/105696
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/105696
network_acronym_str SEDICI
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network_name_str SEDICI (UNLP)
spelling Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pHVentureira, Jorge LuisBolontrade, Agustín JuanSperoni Aguirre, FranciscoDavid Briand, ElisabethScilingo, Adriana AliciaRopers, Marie-HélèneBoury, FrankAñón, María CristinaAnton, MarcQuímicaAmaranthInterfacial propertiesDilatational interfacial rheologyLangmuir isothermEmulsifying propertiesAmaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties. Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1-7http://sedici.unlp.edu.ar/handle/10915/105696enginfo:eu-repo/semantics/altIdentifier/issn/0023-6438info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2011.07.024info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:55:42Zoai:sedici.unlp.edu.ar:10915/105696Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:55:42.394SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
spellingShingle Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
Ventureira, Jorge Luis
Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
title_short Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_full Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_fullStr Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_full_unstemmed Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_sort Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
dc.creator.none.fl_str_mv Ventureira, Jorge Luis
Bolontrade, Agustín Juan
Speroni Aguirre, Francisco
David Briand, Elisabeth
Scilingo, Adriana Alicia
Ropers, Marie-Hélène
Boury, Frank
Añón, María Cristina
Anton, Marc
author Ventureira, Jorge Luis
author_facet Ventureira, Jorge Luis
Bolontrade, Agustín Juan
Speroni Aguirre, Francisco
David Briand, Elisabeth
Scilingo, Adriana Alicia
Ropers, Marie-Hélène
Boury, Frank
Añón, María Cristina
Anton, Marc
author_role author
author2 Bolontrade, Agustín Juan
Speroni Aguirre, Francisco
David Briand, Elisabeth
Scilingo, Adriana Alicia
Ropers, Marie-Hélène
Boury, Frank
Añón, María Cristina
Anton, Marc
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
topic Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
dc.description.none.fl_txt_mv Amaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties. Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description Amaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties. Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/105696
url http://sedici.unlp.edu.ar/handle/10915/105696
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0023-6438
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2011.07.024
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
1-7
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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