A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions

Autores
Víctor, M.; Pizones Ruiz Henestrosa, Víctor Manuel; Martinez, María Julia; Patino, Juan M. R.; Pilosof, Ana Maria Renata
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this work, the complex assembly of one of the major storage proteins in soybean, glycinin, was analyzed using dynamic light scattering, from the hydrodynamic diameter of assembled forms in solution. The protein concentration and temperature were maintained constant at 10-1% w/w and 20 °C, respectively, and the pH was 7.6, 7.0 and 3.0. By analyzing the intensity and volume size distributions, a complex equilibrium between self-assembled forms could be determined. At pH 7.6 and an ionic strength of 0.5 M, where the self-assembly of glycinin has been widely reported in the literature, the DLS technique revealed an equilibrium between different assembled forms, that shifted towards the 11S form. At a lower ionic strength for pH 3.0 or 7.0, the 7S form predominated. The hydrodynamic diameter evolved differently upon heating, depending on pH and ionic strength. For pH 7 (I = 0.05) and 7.6 (I = 0.5) a significant increase in d H was observed at a temperatures of 55 and 70 °C, respectively, which were significantly lower than the denaturation onset temperatures as determined by DSC. No changes in dH nor a transition endotherm were observed at pH 3.
Fil: Víctor, M.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Fil: Pizones Ruiz Henestrosa, Víctor Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Universidad de Sevilla; España
Fil: Martinez, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Fil: Patino, Juan M. R.. Universidad de Sevilla; España
Fil: Pilosof, Ana Maria Renata. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Materia
Dynamic Light Scattering
Globulin
Soy
Structure
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:11336/68268

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network_name_str CONICET Digital (CONICET)
spelling A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutionsVíctor, M.Pizones Ruiz Henestrosa, Víctor ManuelMartinez, María JuliaPatino, Juan M. R.Pilosof, Ana Maria RenataDynamic Light ScatteringGlobulinSoyStructurehttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2In this work, the complex assembly of one of the major storage proteins in soybean, glycinin, was analyzed using dynamic light scattering, from the hydrodynamic diameter of assembled forms in solution. The protein concentration and temperature were maintained constant at 10-1% w/w and 20 °C, respectively, and the pH was 7.6, 7.0 and 3.0. By analyzing the intensity and volume size distributions, a complex equilibrium between self-assembled forms could be determined. At pH 7.6 and an ionic strength of 0.5 M, where the self-assembly of glycinin has been widely reported in the literature, the DLS technique revealed an equilibrium between different assembled forms, that shifted towards the 11S form. At a lower ionic strength for pH 3.0 or 7.0, the 7S form predominated. The hydrodynamic diameter evolved differently upon heating, depending on pH and ionic strength. For pH 7 (I = 0.05) and 7.6 (I = 0.5) a significant increase in d H was observed at a temperatures of 55 and 70 °C, respectively, which were significantly lower than the denaturation onset temperatures as determined by DSC. No changes in dH nor a transition endotherm were observed at pH 3.Fil: Víctor, M.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; ArgentinaFil: Pizones Ruiz Henestrosa, Víctor Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Universidad de Sevilla; EspañaFil: Martinez, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; ArgentinaFil: Patino, Juan M. R.. Universidad de Sevilla; EspañaFil: Pilosof, Ana Maria Renata. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; ArgentinaAmerican Oil Chemists' Society2012-07info: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/11336/68268Víctor, M.; Pizones Ruiz Henestrosa, Víctor Manuel; Martinez, María Julia; Patino, Juan M. R.; Pilosof, Ana Maria Renata; A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions; American Oil Chemists' Society; Journal of the American Oil Chemists Society; 89; 7; 7-2012; 1183-11910003-021XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s11746-012-2029-7info:eu-repo/semantics/altIdentifier/url/https://aocs.onlinelibrary.wiley.com/doi/abs/10.1007/s11746-012-2029-7info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:20:24Zoai:ri.conicet.gov.ar:11336/68268instacron: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 10:20:25.238CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
title A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
spellingShingle A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
Víctor, M.
Dynamic Light Scattering
Globulin
Soy
Structure
title_short A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
title_full A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
title_fullStr A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
title_full_unstemmed A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
title_sort A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions
dc.creator.none.fl_str_mv Víctor, M.
Pizones Ruiz Henestrosa, Víctor Manuel
Martinez, María Julia
Patino, Juan M. R.
Pilosof, Ana Maria Renata
author Víctor, M.
author_facet Víctor, M.
Pizones Ruiz Henestrosa, Víctor Manuel
Martinez, María Julia
Patino, Juan M. R.
Pilosof, Ana Maria Renata
author_role author
author2 Pizones Ruiz Henestrosa, Víctor Manuel
Martinez, María Julia
Patino, Juan M. R.
Pilosof, Ana Maria Renata
author2_role author
author
author
author
dc.subject.none.fl_str_mv Dynamic Light Scattering
Globulin
Soy
Structure
topic Dynamic Light Scattering
Globulin
Soy
Structure
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In this work, the complex assembly of one of the major storage proteins in soybean, glycinin, was analyzed using dynamic light scattering, from the hydrodynamic diameter of assembled forms in solution. The protein concentration and temperature were maintained constant at 10-1% w/w and 20 °C, respectively, and the pH was 7.6, 7.0 and 3.0. By analyzing the intensity and volume size distributions, a complex equilibrium between self-assembled forms could be determined. At pH 7.6 and an ionic strength of 0.5 M, where the self-assembly of glycinin has been widely reported in the literature, the DLS technique revealed an equilibrium between different assembled forms, that shifted towards the 11S form. At a lower ionic strength for pH 3.0 or 7.0, the 7S form predominated. The hydrodynamic diameter evolved differently upon heating, depending on pH and ionic strength. For pH 7 (I = 0.05) and 7.6 (I = 0.5) a significant increase in d H was observed at a temperatures of 55 and 70 °C, respectively, which were significantly lower than the denaturation onset temperatures as determined by DSC. No changes in dH nor a transition endotherm were observed at pH 3.
Fil: Víctor, M.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Fil: Pizones Ruiz Henestrosa, Víctor Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Universidad de Sevilla; España
Fil: Martinez, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
Fil: Patino, Juan M. R.. Universidad de Sevilla; España
Fil: Pilosof, Ana Maria Renata. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina
description In this work, the complex assembly of one of the major storage proteins in soybean, glycinin, was analyzed using dynamic light scattering, from the hydrodynamic diameter of assembled forms in solution. The protein concentration and temperature were maintained constant at 10-1% w/w and 20 °C, respectively, and the pH was 7.6, 7.0 and 3.0. By analyzing the intensity and volume size distributions, a complex equilibrium between self-assembled forms could be determined. At pH 7.6 and an ionic strength of 0.5 M, where the self-assembly of glycinin has been widely reported in the literature, the DLS technique revealed an equilibrium between different assembled forms, that shifted towards the 11S form. At a lower ionic strength for pH 3.0 or 7.0, the 7S form predominated. The hydrodynamic diameter evolved differently upon heating, depending on pH and ionic strength. For pH 7 (I = 0.05) and 7.6 (I = 0.5) a significant increase in d H was observed at a temperatures of 55 and 70 °C, respectively, which were significantly lower than the denaturation onset temperatures as determined by DSC. No changes in dH nor a transition endotherm were observed at pH 3.
publishDate 2012
dc.date.none.fl_str_mv 2012-07
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/11336/68268
Víctor, M.; Pizones Ruiz Henestrosa, Víctor Manuel; Martinez, María Julia; Patino, Juan M. R.; Pilosof, Ana Maria Renata; A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions; American Oil Chemists' Society; Journal of the American Oil Chemists Society; 89; 7; 7-2012; 1183-1191
0003-021X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/68268
identifier_str_mv Víctor, M.; Pizones Ruiz Henestrosa, Víctor Manuel; Martinez, María Julia; Patino, Juan M. R.; Pilosof, Ana Maria Renata; A Dynamic light scattering study on the complex assembly of glycinin soy globulin in aqueous solutions; American Oil Chemists' Society; Journal of the American Oil Chemists Society; 89; 7; 7-2012; 1183-1191
0003-021X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s11746-012-2029-7
info:eu-repo/semantics/altIdentifier/url/https://aocs.onlinelibrary.wiley.com/doi/abs/10.1007/s11746-012-2029-7
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 American Oil Chemists' Society
publisher.none.fl_str_mv American Oil Chemists' Society
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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