Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties

Autores
Baeza, Rosa Isabel; Gugliotta, Luis Marcelino; Pilosof, Ana Maria Renata
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64–88 °C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2–2.4 °C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein–polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties.
Fil: Baeza, Rosa Isabel. Universidad de Buenos Aires; Argentina
Fil: Gugliotta, Luis Marcelino. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires; Argentina
Materia
Thermodynamic Incompatibility
Kinetics
Gelation
Aggregation
Denaturation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/28588
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/28588
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel propertiesBaeza, Rosa IsabelGugliotta, Luis MarcelinoPilosof, Ana Maria RenataThermodynamic IncompatibilityKineticsGelationAggregationDenaturationhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64–88 °C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2–2.4 °C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein–polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties.Fil: Baeza, Rosa Isabel. Universidad de Buenos Aires; ArgentinaFil: Gugliotta, Luis Marcelino. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires; ArgentinaElsevier Science2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/28588Baeza, Rosa Isabel; Gugliotta, Luis Marcelino; Pilosof, Ana Maria Renata; Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 31; 1-4; 12-2003; 81-930927-7765CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/S0927-7765(03)00045-6info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:44Zoai:ri.conicet.gov.ar:11336/28588instacron: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 09:36:45.027CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
title Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
spellingShingle Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
Baeza, Rosa Isabel
Thermodynamic Incompatibility
Kinetics
Gelation
Aggregation
Denaturation
title_short Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
title_full Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
title_fullStr Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
title_full_unstemmed Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
title_sort Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
dc.creator.none.fl_str_mv Baeza, Rosa Isabel
Gugliotta, Luis Marcelino
Pilosof, Ana Maria Renata
author Baeza, Rosa Isabel
author_facet Baeza, Rosa Isabel
Gugliotta, Luis Marcelino
Pilosof, Ana Maria Renata
author_role author
author2 Gugliotta, Luis Marcelino
Pilosof, Ana Maria Renata
author2_role author
author
dc.subject.none.fl_str_mv Thermodynamic Incompatibility
Kinetics
Gelation
Aggregation
Denaturation
topic Thermodynamic Incompatibility
Kinetics
Gelation
Aggregation
Denaturation
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 role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64–88 °C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2–2.4 °C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein–polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties.
Fil: Baeza, Rosa Isabel. Universidad de Buenos Aires; Argentina
Fil: Gugliotta, Luis Marcelino. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires; Argentina
description The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64–88 °C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2–2.4 °C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein–polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties.
publishDate 2003
dc.date.none.fl_str_mv 2003-12
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/11336/28588
Baeza, Rosa Isabel; Gugliotta, Luis Marcelino; Pilosof, Ana Maria Renata; Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 31; 1-4; 12-2003; 81-93
0927-7765
CONICET Digital
CONICET
url http://hdl.handle.net/11336/28588
identifier_str_mv Baeza, Rosa Isabel; Gugliotta, Luis Marcelino; Pilosof, Ana Maria Renata; Gelation of beta-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 31; 1-4; 12-2003; 81-93
0927-7765
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/S0927-7765(03)00045-6
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/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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