On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics

Autores
Martinez, María Julia; Pilosof, Ana Maria Renata
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
There are a lot of works in literature about the size particle of β-lactoglobulin (β-lg) at different conditions and also about its rheological properties; however, there are not works which connect both results. The aim of this work was precisely to relate the state of association of β-lg in solution with the heat-induced aggregation and the dynamics of gelation upon heating in a wide range of pH. The state of association and the heat-induced aggregation of β-lg were evaluated by the determination of its size particle at room temperature and upon heating by dynamic light scattering, while the dynamics of gelation was studied by rheological measurements in a controlled stress rheometer. The state of association of β-lg was highly dependent on pH at room temperature increasing near to its isoelectric point. The rate of heat aggregation, the size of aggregates and the dynamic of gelation of β-lg were also highly dependent on pH. Finally, a mechanism involved in β-lg gelation at different pH values is proposed. The dynamic light scattering technique proved to be a useful tool to characterize the state of association and the onset of β-lg aggregation upon heating for understanding the behaviour of these proteins, for example, under the effect of heating on the gelling properties.
Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
Materia
BETA-LACTOGLOBULIN
HEAT-INDUCED AGGREGATION
GELATION
PH
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:11336/92479
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamicsMartinez, María JuliaPilosof, Ana Maria RenataBETA-LACTOGLOBULINHEAT-INDUCED AGGREGATIONGELATIONPHhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1There are a lot of works in literature about the size particle of β-lactoglobulin (β-lg) at different conditions and also about its rheological properties; however, there are not works which connect both results. The aim of this work was precisely to relate the state of association of β-lg in solution with the heat-induced aggregation and the dynamics of gelation upon heating in a wide range of pH. The state of association and the heat-induced aggregation of β-lg were evaluated by the determination of its size particle at room temperature and upon heating by dynamic light scattering, while the dynamics of gelation was studied by rheological measurements in a controlled stress rheometer. The state of association of β-lg was highly dependent on pH at room temperature increasing near to its isoelectric point. The rate of heat aggregation, the size of aggregates and the dynamic of gelation of β-lg were also highly dependent on pH. Finally, a mechanism involved in β-lg gelation at different pH values is proposed. The dynamic light scattering technique proved to be a useful tool to characterize the state of association and the onset of β-lg aggregation upon heating for understanding the behaviour of these proteins, for example, under the effect of heating on the gelling properties.Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; ArgentinaUniversiti Putra Malaysia. Faculty of Food Science & Technology2018-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/92479Martinez, María Julia; Pilosof, Ana Maria Renata; On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics; Universiti Putra Malaysia. Faculty of Food Science & Technology; International Food Research Journal; 25; 2; 4-2018; 676-6832231-7546CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.ifrj.upm.edu.my/ifrj-2018-25-issue-2.htmlinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:06:26Zoai:ri.conicet.gov.ar:11336/92479instacron: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:34982025-09-10 13:06:26.684CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
title On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
spellingShingle On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
Martinez, María Julia
BETA-LACTOGLOBULIN
HEAT-INDUCED AGGREGATION
GELATION
PH
title_short On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
title_full On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
title_fullStr On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
title_full_unstemmed On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
title_sort On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics
dc.creator.none.fl_str_mv Martinez, María Julia
Pilosof, Ana Maria Renata
author Martinez, María Julia
author_facet Martinez, María Julia
Pilosof, Ana Maria Renata
author_role author
author2 Pilosof, Ana Maria Renata
author2_role author
dc.subject.none.fl_str_mv BETA-LACTOGLOBULIN
HEAT-INDUCED AGGREGATION
GELATION
PH
topic BETA-LACTOGLOBULIN
HEAT-INDUCED AGGREGATION
GELATION
PH
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv There are a lot of works in literature about the size particle of β-lactoglobulin (β-lg) at different conditions and also about its rheological properties; however, there are not works which connect both results. The aim of this work was precisely to relate the state of association of β-lg in solution with the heat-induced aggregation and the dynamics of gelation upon heating in a wide range of pH. The state of association and the heat-induced aggregation of β-lg were evaluated by the determination of its size particle at room temperature and upon heating by dynamic light scattering, while the dynamics of gelation was studied by rheological measurements in a controlled stress rheometer. The state of association of β-lg was highly dependent on pH at room temperature increasing near to its isoelectric point. The rate of heat aggregation, the size of aggregates and the dynamic of gelation of β-lg were also highly dependent on pH. Finally, a mechanism involved in β-lg gelation at different pH values is proposed. The dynamic light scattering technique proved to be a useful tool to characterize the state of association and the onset of β-lg aggregation upon heating for understanding the behaviour of these proteins, for example, under the effect of heating on the gelling properties.
Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
description There are a lot of works in literature about the size particle of β-lactoglobulin (β-lg) at different conditions and also about its rheological properties; however, there are not works which connect both results. The aim of this work was precisely to relate the state of association of β-lg in solution with the heat-induced aggregation and the dynamics of gelation upon heating in a wide range of pH. The state of association and the heat-induced aggregation of β-lg were evaluated by the determination of its size particle at room temperature and upon heating by dynamic light scattering, while the dynamics of gelation was studied by rheological measurements in a controlled stress rheometer. The state of association of β-lg was highly dependent on pH at room temperature increasing near to its isoelectric point. The rate of heat aggregation, the size of aggregates and the dynamic of gelation of β-lg were also highly dependent on pH. Finally, a mechanism involved in β-lg gelation at different pH values is proposed. The dynamic light scattering technique proved to be a useful tool to characterize the state of association and the onset of β-lg aggregation upon heating for understanding the behaviour of these proteins, for example, under the effect of heating on the gelling properties.
publishDate 2018
dc.date.none.fl_str_mv 2018-04
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/11336/92479
Martinez, María Julia; Pilosof, Ana Maria Renata; On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics; Universiti Putra Malaysia. Faculty of Food Science & Technology; International Food Research Journal; 25; 2; 4-2018; 676-683
2231-7546
CONICET Digital
CONICET
url http://hdl.handle.net/11336/92479
identifier_str_mv Martinez, María Julia; Pilosof, Ana Maria Renata; On the relationship between pH-dependent β-lactoglobulin self assembly and gelation dynamics; Universiti Putra Malaysia. Faculty of Food Science & Technology; International Food Research Journal; 25; 2; 4-2018; 676-683
2231-7546
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.ifrj.upm.edu.my/ifrj-2018-25-issue-2.html
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
dc.publisher.none.fl_str_mv Universiti Putra Malaysia. Faculty of Food Science & Technology
publisher.none.fl_str_mv Universiti Putra Malaysia. Faculty of Food Science & Technology
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 12.993085

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