Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins
- Autores
- Chel-Guerrero, Luis; Scilingo, Adriana Alicia; Gallegos Tintoré, Santiago; Dávila-Ortíz, G.; Añon, Maria Cristina
- Año de publicación
- 2007
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A globulin fraction from Phaseolus lunatus have been isolated and characterized. The fractionation scheme used allowed to obtain a Globulin partially purificated. Globulin purification by ultracentrifugation allowed to isolate three peaks with different sedimentation coefficient, while gel filtration chromatography yielded two species, I and II, which were later identified as 11S and 7S globulins, respectively. Species II, 7S globulin from P. lunatus, seems to have a molecular mass of 72 kDa and to be constituted by polypeptides of 34–36, 25–27 and 16–18 kDa without intermolecular disulfide bonds. These polypeptides would present certain heterogeneity, as suggested by the results of isoelectric focusing and electrophoresis analyses. This protein exhibited some particular features, including a lower molecular mass and higher thermal stability than typical vicilins. Species I, with a molecular mass of 336 kDa, would be constituted by subunits of 53–55 and 40–41 kDa formed by smaller polypeptides (around 30 and 20 kDa) linked by disulfide bonds. These features, together with the existence of basic and acid polypeptides in the molecule, would confirm that species I is a globulin of the legumins, 11S globulins or -conglutin family.
Fil: Chel-Guerrero, Luis. Universidad Autónoma de Yucatan. Facultad de Ingeniería Química; México
Fil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Gallegos Tintoré, Santiago. Universidad Autónoma de Yucatan. Facultad de Ingeniería Química; México
Fil: Dávila-Ortíz, G.. Instituto Politécnico Nacional. Escuela Nacional de Ciencias Biológicas; México
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina - Materia
-
Phaseolus lunatus
Globulins
Protein characterization - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/111368
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
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Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulinsChel-Guerrero, LuisScilingo, Adriana AliciaGallegos Tintoré, SantiagoDávila-Ortíz, G.Añon, Maria CristinaPhaseolus lunatusGlobulinsProtein characterizationhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2A globulin fraction from Phaseolus lunatus have been isolated and characterized. The fractionation scheme used allowed to obtain a Globulin partially purificated. Globulin purification by ultracentrifugation allowed to isolate three peaks with different sedimentation coefficient, while gel filtration chromatography yielded two species, I and II, which were later identified as 11S and 7S globulins, respectively. Species II, 7S globulin from P. lunatus, seems to have a molecular mass of 72 kDa and to be constituted by polypeptides of 34–36, 25–27 and 16–18 kDa without intermolecular disulfide bonds. These polypeptides would present certain heterogeneity, as suggested by the results of isoelectric focusing and electrophoresis analyses. This protein exhibited some particular features, including a lower molecular mass and higher thermal stability than typical vicilins. Species I, with a molecular mass of 336 kDa, would be constituted by subunits of 53–55 and 40–41 kDa formed by smaller polypeptides (around 30 and 20 kDa) linked by disulfide bonds. These features, together with the existence of basic and acid polypeptides in the molecule, would confirm that species I is a globulin of the legumins, 11S globulins or -conglutin family.Fil: Chel-Guerrero, Luis. Universidad Autónoma de Yucatan. Facultad de Ingeniería Química; MéxicoFil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Gallegos Tintoré, Santiago. Universidad Autónoma de Yucatan. Facultad de Ingeniería Química; MéxicoFil: Dávila-Ortíz, G.. Instituto Politécnico Nacional. Escuela Nacional de Ciencias Biológicas; MéxicoFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaElsevier Science2007-11info: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/11336/111368Chel-Guerrero, Luis; Scilingo, Adriana Alicia; Gallegos Tintoré, Santiago; Dávila-Ortíz, G.; Añon, Maria Cristina; Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins; Elsevier Science; LWT - Food Science and Technology; 40; 9; 11-2007; 1537-15440023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643806003124info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2006.11.014info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:37:50Zoai:ri.conicet.gov.ar:11336/111368instacron: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 09:37:50.363CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
title |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
spellingShingle |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins Chel-Guerrero, Luis Phaseolus lunatus Globulins Protein characterization |
title_short |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
title_full |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
title_fullStr |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
title_full_unstemmed |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
title_sort |
Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins |
dc.creator.none.fl_str_mv |
Chel-Guerrero, Luis Scilingo, Adriana Alicia Gallegos Tintoré, Santiago Dávila-Ortíz, G. Añon, Maria Cristina |
author |
Chel-Guerrero, Luis |
author_facet |
Chel-Guerrero, Luis Scilingo, Adriana Alicia Gallegos Tintoré, Santiago Dávila-Ortíz, G. Añon, Maria Cristina |
author_role |
author |
author2 |
Scilingo, Adriana Alicia Gallegos Tintoré, Santiago Dávila-Ortíz, G. Añon, Maria Cristina |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Phaseolus lunatus Globulins Protein characterization |
topic |
Phaseolus lunatus Globulins Protein characterization |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
A globulin fraction from Phaseolus lunatus have been isolated and characterized. The fractionation scheme used allowed to obtain a Globulin partially purificated. Globulin purification by ultracentrifugation allowed to isolate three peaks with different sedimentation coefficient, while gel filtration chromatography yielded two species, I and II, which were later identified as 11S and 7S globulins, respectively. Species II, 7S globulin from P. lunatus, seems to have a molecular mass of 72 kDa and to be constituted by polypeptides of 34–36, 25–27 and 16–18 kDa without intermolecular disulfide bonds. These polypeptides would present certain heterogeneity, as suggested by the results of isoelectric focusing and electrophoresis analyses. This protein exhibited some particular features, including a lower molecular mass and higher thermal stability than typical vicilins. Species I, with a molecular mass of 336 kDa, would be constituted by subunits of 53–55 and 40–41 kDa formed by smaller polypeptides (around 30 and 20 kDa) linked by disulfide bonds. These features, together with the existence of basic and acid polypeptides in the molecule, would confirm that species I is a globulin of the legumins, 11S globulins or -conglutin family. Fil: Chel-Guerrero, Luis. Universidad Autónoma de Yucatan. Facultad de Ingeniería Química; México Fil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina Fil: Gallegos Tintoré, Santiago. Universidad Autónoma de Yucatan. Facultad de Ingeniería Química; México Fil: Dávila-Ortíz, G.. Instituto Politécnico Nacional. Escuela Nacional de Ciencias Biológicas; México Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina |
description |
A globulin fraction from Phaseolus lunatus have been isolated and characterized. The fractionation scheme used allowed to obtain a Globulin partially purificated. Globulin purification by ultracentrifugation allowed to isolate three peaks with different sedimentation coefficient, while gel filtration chromatography yielded two species, I and II, which were later identified as 11S and 7S globulins, respectively. Species II, 7S globulin from P. lunatus, seems to have a molecular mass of 72 kDa and to be constituted by polypeptides of 34–36, 25–27 and 16–18 kDa without intermolecular disulfide bonds. These polypeptides would present certain heterogeneity, as suggested by the results of isoelectric focusing and electrophoresis analyses. This protein exhibited some particular features, including a lower molecular mass and higher thermal stability than typical vicilins. Species I, with a molecular mass of 336 kDa, would be constituted by subunits of 53–55 and 40–41 kDa formed by smaller polypeptides (around 30 and 20 kDa) linked by disulfide bonds. These features, together with the existence of basic and acid polypeptides in the molecule, would confirm that species I is a globulin of the legumins, 11S globulins or -conglutin family. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-11 |
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/11336/111368 Chel-Guerrero, Luis; Scilingo, Adriana Alicia; Gallegos Tintoré, Santiago; Dávila-Ortíz, G.; Añon, Maria Cristina; Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins; Elsevier Science; LWT - Food Science and Technology; 40; 9; 11-2007; 1537-1544 0023-6438 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/111368 |
identifier_str_mv |
Chel-Guerrero, Luis; Scilingo, Adriana Alicia; Gallegos Tintoré, Santiago; Dávila-Ortíz, G.; Añon, Maria Cristina; Physicochemical and structural characterization of Lima Bean (Phaseolus lunatus) globulins; Elsevier Science; LWT - Food Science and Technology; 40; 9; 11-2007; 1537-1544 0023-6438 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643806003124 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2006.11.014 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/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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1844613193658269696 |
score |
13.070432 |