Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems

Autores
Gómez, Analía Verónica; Ferrer, Evelina Gloria; Añon, Maria Cristina; Puppo, Maria Cecilia
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
According to their amphiphilic nature, emulsifiers as Sodium Stearoyl Lactylate (SSL) and Diacetyl Tartaric Acid Esters of Monoglycerides (DATEM) favor interactions between dough components, although the mechanisms of action are not fully elucidated. There is quite information about the nature of emulsifier-gluten protein interaction and its consequence in breadmaking quality, but no reports were found about structural changes in gluten proteins produced by SSL and DATEM and their influence in aggregation-disaggregation gluten protein phenomena. For this reason the aim of this work was to investigate changes on gluten protein structure induced by SSL and DATEM; through the analysis of the nature of soluble aggregates by different SDS-PAGE techniques, and gliadins and glutenins extracted from gluten samples by RP-HPLC. At 1% level, SSL allowed the solubilization of a large proportion of high molecular mass aggregates, suggesting that at this high level, this emulsifier cause changes in native gluten protein network. Nevertheless, no significant differences in the protein quantity extracted of the distinct gliadins and glutenins were observed. On the other hand, the emulsifier SSL at 0.5% (w/w) level also allowed the extraction of a high percentage of γ-gliadins and low molecular weight glutenins in comparison with gluten and gluten-DATEM samples. In conclusion distinct quantity and quality of gliadins and glutenins were extracted from gluten samples, depending on the level and the chemical structure of each emulsifier.
Fil: Gómez, Analía Verónica. 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: Ferrer, Evelina Gloria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina
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
Fil: Puppo, Maria Cecilia. 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
Emulsifiers
Gliadins
Gluten Proteins
Glutenins
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:11336/82368
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systemsGómez, Analía VerónicaFerrer, Evelina GloriaAñon, Maria CristinaPuppo, Maria CeciliaEmulsifiersGliadinsGluten ProteinsGluteninshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1According to their amphiphilic nature, emulsifiers as Sodium Stearoyl Lactylate (SSL) and Diacetyl Tartaric Acid Esters of Monoglycerides (DATEM) favor interactions between dough components, although the mechanisms of action are not fully elucidated. There is quite information about the nature of emulsifier-gluten protein interaction and its consequence in breadmaking quality, but no reports were found about structural changes in gluten proteins produced by SSL and DATEM and their influence in aggregation-disaggregation gluten protein phenomena. For this reason the aim of this work was to investigate changes on gluten protein structure induced by SSL and DATEM; through the analysis of the nature of soluble aggregates by different SDS-PAGE techniques, and gliadins and glutenins extracted from gluten samples by RP-HPLC. At 1% level, SSL allowed the solubilization of a large proportion of high molecular mass aggregates, suggesting that at this high level, this emulsifier cause changes in native gluten protein network. Nevertheless, no significant differences in the protein quantity extracted of the distinct gliadins and glutenins were observed. On the other hand, the emulsifier SSL at 0.5% (w/w) level also allowed the extraction of a high percentage of γ-gliadins and low molecular weight glutenins in comparison with gluten and gluten-DATEM samples. In conclusion distinct quantity and quality of gliadins and glutenins were extracted from gluten samples, depending on the level and the chemical structure of each emulsifier.Fil: Gómez, Analía Verónica. 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: Ferrer, Evelina Gloria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; ArgentinaFil: 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; ArgentinaFil: Puppo, Maria Cecilia. 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 Science2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/82368Gómez, Analía Verónica; Ferrer, Evelina Gloria; Añon, Maria Cristina; Puppo, Maria Cecilia; Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems; Elsevier Science; Food Research International; 46; 1; 4-2012; 62-680963-9969CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0963996911006661info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2011.12.007info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:34Zoai:ri.conicet.gov.ar:11336/82368instacron: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 09:36:34.335CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
title Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
spellingShingle Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
Gómez, Analía Verónica
Emulsifiers
Gliadins
Gluten Proteins
Glutenins
title_short Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
title_full Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
title_fullStr Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
title_full_unstemmed Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
title_sort Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems
dc.creator.none.fl_str_mv Gómez, Analía Verónica
Ferrer, Evelina Gloria
Añon, Maria Cristina
Puppo, Maria Cecilia
author Gómez, Analía Verónica
author_facet Gómez, Analía Verónica
Ferrer, Evelina Gloria
Añon, Maria Cristina
Puppo, Maria Cecilia
author_role author
author2 Ferrer, Evelina Gloria
Añon, Maria Cristina
Puppo, Maria Cecilia
author2_role author
author
author
dc.subject.none.fl_str_mv Emulsifiers
Gliadins
Gluten Proteins
Glutenins
topic Emulsifiers
Gliadins
Gluten Proteins
Glutenins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv According to their amphiphilic nature, emulsifiers as Sodium Stearoyl Lactylate (SSL) and Diacetyl Tartaric Acid Esters of Monoglycerides (DATEM) favor interactions between dough components, although the mechanisms of action are not fully elucidated. There is quite information about the nature of emulsifier-gluten protein interaction and its consequence in breadmaking quality, but no reports were found about structural changes in gluten proteins produced by SSL and DATEM and their influence in aggregation-disaggregation gluten protein phenomena. For this reason the aim of this work was to investigate changes on gluten protein structure induced by SSL and DATEM; through the analysis of the nature of soluble aggregates by different SDS-PAGE techniques, and gliadins and glutenins extracted from gluten samples by RP-HPLC. At 1% level, SSL allowed the solubilization of a large proportion of high molecular mass aggregates, suggesting that at this high level, this emulsifier cause changes in native gluten protein network. Nevertheless, no significant differences in the protein quantity extracted of the distinct gliadins and glutenins were observed. On the other hand, the emulsifier SSL at 0.5% (w/w) level also allowed the extraction of a high percentage of γ-gliadins and low molecular weight glutenins in comparison with gluten and gluten-DATEM samples. In conclusion distinct quantity and quality of gliadins and glutenins were extracted from gluten samples, depending on the level and the chemical structure of each emulsifier.
Fil: Gómez, Analía Verónica. 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: Ferrer, Evelina Gloria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina
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
Fil: Puppo, Maria Cecilia. 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 According to their amphiphilic nature, emulsifiers as Sodium Stearoyl Lactylate (SSL) and Diacetyl Tartaric Acid Esters of Monoglycerides (DATEM) favor interactions between dough components, although the mechanisms of action are not fully elucidated. There is quite information about the nature of emulsifier-gluten protein interaction and its consequence in breadmaking quality, but no reports were found about structural changes in gluten proteins produced by SSL and DATEM and their influence in aggregation-disaggregation gluten protein phenomena. For this reason the aim of this work was to investigate changes on gluten protein structure induced by SSL and DATEM; through the analysis of the nature of soluble aggregates by different SDS-PAGE techniques, and gliadins and glutenins extracted from gluten samples by RP-HPLC. At 1% level, SSL allowed the solubilization of a large proportion of high molecular mass aggregates, suggesting that at this high level, this emulsifier cause changes in native gluten protein network. Nevertheless, no significant differences in the protein quantity extracted of the distinct gliadins and glutenins were observed. On the other hand, the emulsifier SSL at 0.5% (w/w) level also allowed the extraction of a high percentage of γ-gliadins and low molecular weight glutenins in comparison with gluten and gluten-DATEM samples. In conclusion distinct quantity and quality of gliadins and glutenins were extracted from gluten samples, depending on the level and the chemical structure of each emulsifier.
publishDate 2012
dc.date.none.fl_str_mv 2012-04
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/11336/82368
Gómez, Analía Verónica; Ferrer, Evelina Gloria; Añon, Maria Cristina; Puppo, Maria Cecilia; Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems; Elsevier Science; Food Research International; 46; 1; 4-2012; 62-68
0963-9969
CONICET Digital
CONICET
url http://hdl.handle.net/11336/82368
identifier_str_mv Gómez, Analía Verónica; Ferrer, Evelina Gloria; Añon, Maria Cristina; Puppo, Maria Cecilia; Analysis of soluble proteins/aggregates derived from gluten-emulsifiers systems; Elsevier Science; Food Research International; 46; 1; 4-2012; 62-68
0963-9969
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/S0963996911006661
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2011.12.007
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
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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score 13.070432

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