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
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/68268
Ver los metadatos del registro completo
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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 Técnicas2025-10-22T11:53:03Zoai: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:34982025-10-22 11:53:04.151CONICET 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 |
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2012-07 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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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 |
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http://hdl.handle.net/11336/68268 |
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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 |
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eng |
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eng |
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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 |
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openAccess |
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American Oil Chemists' Society |
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American Oil Chemists' Society |
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