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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/111368

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network_name_str CONICET Digital (CONICET)
spelling 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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