Glycation of heat treated B-lactoglobulin: effects on foaming properties

Autores
Busti, Pablo Andres; Báez, Germán David; Delorenzi, Nestor Jorge; Verdini, Roxana Andrea
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this paper, the effect of glucose-glycation of beta-lactoglobulin (monomer 88%, dimer 12%) on foaming properties has been studied in 20 mM phosphate buffer at pH 6.8. The results obtained by electrophoresis, circular dichroism and fluorescence quenching showed the presence of small amounts of aggregates of higher molecular weight, while only slight changes in the tertiary structure flexibility of the glycated protein were detected. The improvement on foaming properties (foamability and foam stability) after glycation was promoted by heat treatment in the dry state (96 h at 50 °C) rather than by sugar conjugation. On the other hand, treated beta-lactoglobulin was obtained by heating a protein solution (55 mg mL-1 in 20 mM phosphate buffer at pH 6.8) at 85 °C for 3 min. This heated protein sample (monomer 51%, dimer 27%, trimer 19%) formed foams with good stability. After glycation, spectroscopic measurements demonstrated that no significant changes were introduced in protein conformation, since the substrate used were composed by unfolded species. However, the additional presence of oligomers of the protein founded after sugar conjugation, decreased the volume foam stability, probably due to steric impediment that diminished the viscoelastic stiffness of the interfacial film. The variation of volume foam stability caused by the different treatments assayed in this work, resulted from the action of these treatments on disproportionation rather than on liquid drainage from the foam
Fil: Busti, Pablo Andres. 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: Delorenzi, Nestor Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Verdini, Roxana Andrea. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
Materia
Beta-Lactoglobulin
Glucose-Glycation
Heat Treatment
Foaming 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:11336/5984
Acceder
id CONICETDig_e67dec6c70775f3ed4350ff6c0e3c975
oai_identifier_str oai:ri.conicet.gov.ar:11336/5984
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Glycation of heat treated B-lactoglobulin: effects on foaming propertiesBusti, Pablo AndresBáez, Germán DavidDelorenzi, Nestor JorgeVerdini, Roxana AndreaBeta-LactoglobulinGlucose-GlycationHeat TreatmentFoaming Propertieshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2In this paper, the effect of glucose-glycation of beta-lactoglobulin (monomer 88%, dimer 12%) on foaming properties has been studied in 20 mM phosphate buffer at pH 6.8. The results obtained by electrophoresis, circular dichroism and fluorescence quenching showed the presence of small amounts of aggregates of higher molecular weight, while only slight changes in the tertiary structure flexibility of the glycated protein were detected. The improvement on foaming properties (foamability and foam stability) after glycation was promoted by heat treatment in the dry state (96 h at 50 °C) rather than by sugar conjugation. On the other hand, treated beta-lactoglobulin was obtained by heating a protein solution (55 mg mL-1 in 20 mM phosphate buffer at pH 6.8) at 85 °C for 3 min. This heated protein sample (monomer 51%, dimer 27%, trimer 19%) formed foams with good stability. After glycation, spectroscopic measurements demonstrated that no significant changes were introduced in protein conformation, since the substrate used were composed by unfolded species. However, the additional presence of oligomers of the protein founded after sugar conjugation, decreased the volume foam stability, probably due to steric impediment that diminished the viscoelastic stiffness of the interfacial film. The variation of volume foam stability caused by the different treatments assayed in this work, resulted from the action of these treatments on disproportionation rather than on liquid drainage from the foamFil: Busti, Pablo Andres. 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: Delorenzi, Nestor Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; ArgentinaFil: Verdini, Roxana Andrea. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; ArgentinaElsevier2013-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/5984Busti, Pablo Andres; Báez, Germán David; Delorenzi, Nestor Jorge; Verdini, Roxana Andrea; Glycation of heat treated B-lactoglobulin: effects on foaming properties; Elsevier; Food Research International; 54; 1; 11-2013; 902-9090963-9969enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0963996913004572info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2013.08.013info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:06Zoai:ri.conicet.gov.ar:11336/5984instacron: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 09:45:06.658CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Glycation of heat treated B-lactoglobulin: effects on foaming properties
title Glycation of heat treated B-lactoglobulin: effects on foaming properties
spellingShingle Glycation of heat treated B-lactoglobulin: effects on foaming properties
Busti, Pablo Andres
Beta-Lactoglobulin
Glucose-Glycation
Heat Treatment
Foaming Properties
title_short Glycation of heat treated B-lactoglobulin: effects on foaming properties
title_full Glycation of heat treated B-lactoglobulin: effects on foaming properties
title_fullStr Glycation of heat treated B-lactoglobulin: effects on foaming properties
title_full_unstemmed Glycation of heat treated B-lactoglobulin: effects on foaming properties
title_sort Glycation of heat treated B-lactoglobulin: effects on foaming properties
dc.creator.none.fl_str_mv Busti, Pablo Andres
Báez, Germán David
Delorenzi, Nestor Jorge
Verdini, Roxana Andrea
author Busti, Pablo Andres
author_facet Busti, Pablo Andres
Báez, Germán David
Delorenzi, Nestor Jorge
Verdini, Roxana Andrea
author_role author
author2 Báez, Germán David
Delorenzi, Nestor Jorge
Verdini, Roxana Andrea
author2_role author
author
author
dc.subject.none.fl_str_mv Beta-Lactoglobulin
Glucose-Glycation
Heat Treatment
Foaming Properties
topic Beta-Lactoglobulin
Glucose-Glycation
Heat Treatment
Foaming Properties
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In this paper, the effect of glucose-glycation of beta-lactoglobulin (monomer 88%, dimer 12%) on foaming properties has been studied in 20 mM phosphate buffer at pH 6.8. The results obtained by electrophoresis, circular dichroism and fluorescence quenching showed the presence of small amounts of aggregates of higher molecular weight, while only slight changes in the tertiary structure flexibility of the glycated protein were detected. The improvement on foaming properties (foamability and foam stability) after glycation was promoted by heat treatment in the dry state (96 h at 50 °C) rather than by sugar conjugation. On the other hand, treated beta-lactoglobulin was obtained by heating a protein solution (55 mg mL-1 in 20 mM phosphate buffer at pH 6.8) at 85 °C for 3 min. This heated protein sample (monomer 51%, dimer 27%, trimer 19%) formed foams with good stability. After glycation, spectroscopic measurements demonstrated that no significant changes were introduced in protein conformation, since the substrate used were composed by unfolded species. However, the additional presence of oligomers of the protein founded after sugar conjugation, decreased the volume foam stability, probably due to steric impediment that diminished the viscoelastic stiffness of the interfacial film. The variation of volume foam stability caused by the different treatments assayed in this work, resulted from the action of these treatments on disproportionation rather than on liquid drainage from the foam
Fil: Busti, Pablo Andres. 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: Delorenzi, Nestor Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Verdini, Roxana Andrea. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
description In this paper, the effect of glucose-glycation of beta-lactoglobulin (monomer 88%, dimer 12%) on foaming properties has been studied in 20 mM phosphate buffer at pH 6.8. The results obtained by electrophoresis, circular dichroism and fluorescence quenching showed the presence of small amounts of aggregates of higher molecular weight, while only slight changes in the tertiary structure flexibility of the glycated protein were detected. The improvement on foaming properties (foamability and foam stability) after glycation was promoted by heat treatment in the dry state (96 h at 50 °C) rather than by sugar conjugation. On the other hand, treated beta-lactoglobulin was obtained by heating a protein solution (55 mg mL-1 in 20 mM phosphate buffer at pH 6.8) at 85 °C for 3 min. This heated protein sample (monomer 51%, dimer 27%, trimer 19%) formed foams with good stability. After glycation, spectroscopic measurements demonstrated that no significant changes were introduced in protein conformation, since the substrate used were composed by unfolded species. However, the additional presence of oligomers of the protein founded after sugar conjugation, decreased the volume foam stability, probably due to steric impediment that diminished the viscoelastic stiffness of the interfacial film. The variation of volume foam stability caused by the different treatments assayed in this work, resulted from the action of these treatments on disproportionation rather than on liquid drainage from the foam
publishDate 2013
dc.date.none.fl_str_mv 2013-11
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/11336/5984
Busti, Pablo Andres; Báez, Germán David; Delorenzi, Nestor Jorge; Verdini, Roxana Andrea; Glycation of heat treated B-lactoglobulin: effects on foaming properties; Elsevier; Food Research International; 54; 1; 11-2013; 902-909
0963-9969
url http://hdl.handle.net/11336/5984
identifier_str_mv Busti, Pablo Andres; Báez, Germán David; Delorenzi, Nestor Jorge; Verdini, Roxana Andrea; Glycation of heat treated B-lactoglobulin: effects on foaming properties; Elsevier; Food Research International; 54; 1; 11-2013; 902-909
0963-9969
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0963996913004572
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2013.08.013
info:eu-repo/semantics/altIdentifier/doi/
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
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
_version_ 1842268709857525760
score 13.13397

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