Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment

Autores
Moro, Andrea; Báez, Germán David; Ballerini, Griselda A.; Busti, Pablo Andres; Delorenzi, Nestor Jorge
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effects of heat treatment on emulsifying properties of beta-lactoglobulin were studied in order to compare them with previous studies on foaming properties. Both of them are closely linked to the structural changes on the protein. Aliquots from 5.5% (w/v) beta-lactoglobulin solution in 20 mM phosphate buffer pH 6.8 were heated at 85 ºC for different time periods, from 1 to 15 min. Protein solubilities were measured for unheated and heated beta-lactoglobulin samples. Protein-stabilized O/W emulsions were prepared with these samples and corn oil. Droplet size distribution in the emulsions and emulsifying activity index were determined for each system, as parameters of the emulsifying ability of the protein. Emulsion stability was estimated from three different methods: backscattering, determination of the remaining protein concentration after creaming and monitoring the oiling off process. With the assayed methodology, heat treatment of beta-lactoglobulin led to different effects on foaming and emulsifying properties of the protein, depending on the time of heating. For shorter times of heating, both foamability and foam stability improved, while emulsifying properties diminished. After 10 min of heating at 85 °C, both foaming and emulsifying properties diminished. Formation time scales, as well as size of the sedimentable aggregates and their steric effect on the interfacial film, play an important role in explaining these differences between foaming and emulsifying properties.
Fil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Fil: Báez, Germán David. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Fil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina. Universidad Tecnológica Nacional. Facultad Regional Rosario; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Fil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Materia
Beta-Lactoglobulin
Heating Treatment
Protein Aggregates
Foaming Properties
Emulsifying Properties
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:11336/5986
Acceder
id CONICETDig_398fd17c9e97d45d4cb9ac3739b66d59
oai_identifier_str oai:ri.conicet.gov.ar:11336/5986
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatmentMoro, AndreaBáez, Germán DavidBallerini, Griselda A.Busti, Pablo AndresDelorenzi, Nestor JorgeBeta-LactoglobulinHeating TreatmentProtein AggregatesFoaming PropertiesEmulsifying Propertieshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The effects of heat treatment on emulsifying properties of beta-lactoglobulin were studied in order to compare them with previous studies on foaming properties. Both of them are closely linked to the structural changes on the protein. Aliquots from 5.5% (w/v) beta-lactoglobulin solution in 20 mM phosphate buffer pH 6.8 were heated at 85 ºC for different time periods, from 1 to 15 min. Protein solubilities were measured for unheated and heated beta-lactoglobulin samples. Protein-stabilized O/W emulsions were prepared with these samples and corn oil. Droplet size distribution in the emulsions and emulsifying activity index were determined for each system, as parameters of the emulsifying ability of the protein. Emulsion stability was estimated from three different methods: backscattering, determination of the remaining protein concentration after creaming and monitoring the oiling off process. With the assayed methodology, heat treatment of beta-lactoglobulin led to different effects on foaming and emulsifying properties of the protein, depending on the time of heating. For shorter times of heating, both foamability and foam stability improved, while emulsifying properties diminished. After 10 min of heating at 85 °C, both foaming and emulsifying properties diminished. Formation time scales, as well as size of the sedimentable aggregates and their steric effect on the interfacial film, play an important role in explaining these differences between foaming and emulsifying properties.Fil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; ArgentinaFil: Báez, Germán David. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; ArgentinaFil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina. Universidad Tecnológica Nacional. Facultad Regional Rosario; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; ArgentinaFil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; ArgentinaElsevier2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/5986Moro, Andrea; Báez, Germán David; Ballerini, Griselda A.; Busti, Pablo Andres; Delorenzi, Nestor Jorge; Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment; Elsevier; Food Research International; 51; 1; 4-2013; 1-70963-9969enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2012.11.011info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0963996912004802info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:07:48Zoai:ri.conicet.gov.ar:11336/5986instacron: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:34982025-09-03 10:07:49.107CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
title Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
spellingShingle Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
Moro, Andrea
Beta-Lactoglobulin
Heating Treatment
Protein Aggregates
Foaming Properties
Emulsifying Properties
title_short Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
title_full Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
title_fullStr Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
title_full_unstemmed Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
title_sort Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment
dc.creator.none.fl_str_mv Moro, Andrea
Báez, Germán David
Ballerini, Griselda A.
Busti, Pablo Andres
Delorenzi, Nestor Jorge
author Moro, Andrea
author_facet Moro, Andrea
Báez, Germán David
Ballerini, Griselda A.
Busti, Pablo Andres
Delorenzi, Nestor Jorge
author_role author
author2 Báez, Germán David
Ballerini, Griselda A.
Busti, Pablo Andres
Delorenzi, Nestor Jorge
author2_role author
author
author
author
dc.subject.none.fl_str_mv Beta-Lactoglobulin
Heating Treatment
Protein Aggregates
Foaming Properties
Emulsifying Properties
topic Beta-Lactoglobulin
Heating Treatment
Protein Aggregates
Foaming Properties
Emulsifying Properties
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The effects of heat treatment on emulsifying properties of beta-lactoglobulin were studied in order to compare them with previous studies on foaming properties. Both of them are closely linked to the structural changes on the protein. Aliquots from 5.5% (w/v) beta-lactoglobulin solution in 20 mM phosphate buffer pH 6.8 were heated at 85 ºC for different time periods, from 1 to 15 min. Protein solubilities were measured for unheated and heated beta-lactoglobulin samples. Protein-stabilized O/W emulsions were prepared with these samples and corn oil. Droplet size distribution in the emulsions and emulsifying activity index were determined for each system, as parameters of the emulsifying ability of the protein. Emulsion stability was estimated from three different methods: backscattering, determination of the remaining protein concentration after creaming and monitoring the oiling off process. With the assayed methodology, heat treatment of beta-lactoglobulin led to different effects on foaming and emulsifying properties of the protein, depending on the time of heating. For shorter times of heating, both foamability and foam stability improved, while emulsifying properties diminished. After 10 min of heating at 85 °C, both foaming and emulsifying properties diminished. Formation time scales, as well as size of the sedimentable aggregates and their steric effect on the interfacial film, play an important role in explaining these differences between foaming and emulsifying properties.
Fil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Fil: Báez, Germán David. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Fil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina. Universidad Tecnológica Nacional. Facultad Regional Rosario; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Fil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
description The effects of heat treatment on emulsifying properties of beta-lactoglobulin were studied in order to compare them with previous studies on foaming properties. Both of them are closely linked to the structural changes on the protein. Aliquots from 5.5% (w/v) beta-lactoglobulin solution in 20 mM phosphate buffer pH 6.8 were heated at 85 ºC for different time periods, from 1 to 15 min. Protein solubilities were measured for unheated and heated beta-lactoglobulin samples. Protein-stabilized O/W emulsions were prepared with these samples and corn oil. Droplet size distribution in the emulsions and emulsifying activity index were determined for each system, as parameters of the emulsifying ability of the protein. Emulsion stability was estimated from three different methods: backscattering, determination of the remaining protein concentration after creaming and monitoring the oiling off process. With the assayed methodology, heat treatment of beta-lactoglobulin led to different effects on foaming and emulsifying properties of the protein, depending on the time of heating. For shorter times of heating, both foamability and foam stability improved, while emulsifying properties diminished. After 10 min of heating at 85 °C, both foaming and emulsifying properties diminished. Formation time scales, as well as size of the sedimentable aggregates and their steric effect on the interfacial film, play an important role in explaining these differences between foaming and emulsifying properties.
publishDate 2013
dc.date.none.fl_str_mv 2013-04
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/11336/5986
Moro, Andrea; Báez, Germán David; Ballerini, Griselda A.; Busti, Pablo Andres; Delorenzi, Nestor Jorge; Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment; Elsevier; Food Research International; 51; 1; 4-2013; 1-7
0963-9969
url http://hdl.handle.net/11336/5986
identifier_str_mv Moro, Andrea; Báez, Germán David; Ballerini, Griselda A.; Busti, Pablo Andres; Delorenzi, Nestor Jorge; Emulsifying and foaming properties of beta-lactoglobulin modified by heat treatment; Elsevier; Food Research International; 51; 1; 4-2013; 1-7
0963-9969
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2012.11.011
info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0963996912004802
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.13397

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