Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH

Autores
Jara, Federico Luis; Carrera Sánchez, Cecilio; Rodríguez Patino, Juan M.; Pilosof, Ana Maria Renata
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The interfacial properties at the air–water (A/W) of each individual whey proteins (β-lactoglobulin, β-lg; α-lactalbumin, α-la; bovin serum albumin, BSA), and their mixtures with a surface-active polysaccharide, hydroxypropylmethylcellulose (HPMC) were studied at pH 3 or 6. The interfacial films were studied by measurement surface pressure (π) isotherms and dynamics of adsorption. At equilibrium proteins surface activity was affected by pH only at low concentrations (below 1·10−2 % wt/wt), due to their pH-dependent conformational changes. HPMC resulted less surface active at pH 3 (below 1·10−4 % wt/wt concentration) that at pH 6. On kinetic studies (π–t), the behavior of β-lg, HPMC and BSA did not change with pH but α-la presented a higher surface activity at pH 3 than 6, even on saturating bulk concentrations. Mixtures of β-lg or BSA with HPMC showed a behavior in between that of single components revealing a net competence for the interface but the mixture α-la and HPMC at pH 6 showed an enhance adsorption. Rheological studies (surface dilatational elastic, Ed, over time) presented the major differences for pHs evaluated. The α-la formed extremely viscoelastic films at pH 6.0, while at pH 3 has the lowest Ed value. β-lg and HPMC films were more viscoelastic at pH 6, being Ed protein film higher. Finally, BSA presented the lowest viscoelastic films without differences between both pHs. For mixtures: i) at pH 6 β-lg/HPMC mixture Ed was dominated by HPMC; at pH 3.0, Ed begins dominated by HPMC, reaching an intermediate value; ii) α-la/HPMC mixture formed more viscoelastic films at pH 6.0 with an intermediate Ed value, while at pH 3.0 the Ed is dominated by protein; iii) BSA/HPMC mixture presented a similar trend in Ed behavior at both pHs.
Fil: Jara, Federico Luis. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Carrera Sánchez, Cecilio. Universidad de Sevilla; España
Fil: Rodríguez Patino, Juan M.. Universidad de Sevilla; España
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Interfaces
Proteins
Polysaccharides
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:11336/30365

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network_name_str CONICET Digital (CONICET)
spelling Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pHJara, Federico LuisCarrera Sánchez, CecilioRodríguez Patino, Juan M.Pilosof, Ana Maria RenataInterfacesProteinsPolysaccharideshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The interfacial properties at the air–water (A/W) of each individual whey proteins (β-lactoglobulin, β-lg; α-lactalbumin, α-la; bovin serum albumin, BSA), and their mixtures with a surface-active polysaccharide, hydroxypropylmethylcellulose (HPMC) were studied at pH 3 or 6. The interfacial films were studied by measurement surface pressure (π) isotherms and dynamics of adsorption. At equilibrium proteins surface activity was affected by pH only at low concentrations (below 1·10−2 % wt/wt), due to their pH-dependent conformational changes. HPMC resulted less surface active at pH 3 (below 1·10−4 % wt/wt concentration) that at pH 6. On kinetic studies (π–t), the behavior of β-lg, HPMC and BSA did not change with pH but α-la presented a higher surface activity at pH 3 than 6, even on saturating bulk concentrations. Mixtures of β-lg or BSA with HPMC showed a behavior in between that of single components revealing a net competence for the interface but the mixture α-la and HPMC at pH 6 showed an enhance adsorption. Rheological studies (surface dilatational elastic, Ed, over time) presented the major differences for pHs evaluated. The α-la formed extremely viscoelastic films at pH 6.0, while at pH 3 has the lowest Ed value. β-lg and HPMC films were more viscoelastic at pH 6, being Ed protein film higher. Finally, BSA presented the lowest viscoelastic films without differences between both pHs. For mixtures: i) at pH 6 β-lg/HPMC mixture Ed was dominated by HPMC; at pH 3.0, Ed begins dominated by HPMC, reaching an intermediate value; ii) α-la/HPMC mixture formed more viscoelastic films at pH 6.0 with an intermediate Ed value, while at pH 3.0 the Ed is dominated by protein; iii) BSA/HPMC mixture presented a similar trend in Ed behavior at both pHs.Fil: Jara, Federico Luis. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Carrera Sánchez, Cecilio. Universidad de Sevilla; EspañaFil: Rodríguez Patino, Juan M.. Universidad de Sevilla; EspañaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2013-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/30365Jara, Federico Luis; Carrera Sánchez, Cecilio; Rodríguez Patino, Juan M.; Pilosof, Ana Maria Renata; Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH; Elsevier; Food Hydrocolloids; 35; 6-2013; 189-1970268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2013.05.013info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X13001495info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T11:48:50Zoai:ri.conicet.gov.ar:11336/30365instacron: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:34982025-10-29 11:48:50.373CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
title Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
spellingShingle Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
Jara, Federico Luis
Interfaces
Proteins
Polysaccharides
title_short Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
title_full Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
title_fullStr Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
title_full_unstemmed Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
title_sort Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH
dc.creator.none.fl_str_mv Jara, Federico Luis
Carrera Sánchez, Cecilio
Rodríguez Patino, Juan M.
Pilosof, Ana Maria Renata
author Jara, Federico Luis
author_facet Jara, Federico Luis
Carrera Sánchez, Cecilio
Rodríguez Patino, Juan M.
Pilosof, Ana Maria Renata
author_role author
author2 Carrera Sánchez, Cecilio
Rodríguez Patino, Juan M.
Pilosof, Ana Maria Renata
author2_role author
author
author
dc.subject.none.fl_str_mv Interfaces
Proteins
Polysaccharides
topic Interfaces
Proteins
Polysaccharides
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 interfacial properties at the air–water (A/W) of each individual whey proteins (β-lactoglobulin, β-lg; α-lactalbumin, α-la; bovin serum albumin, BSA), and their mixtures with a surface-active polysaccharide, hydroxypropylmethylcellulose (HPMC) were studied at pH 3 or 6. The interfacial films were studied by measurement surface pressure (π) isotherms and dynamics of adsorption. At equilibrium proteins surface activity was affected by pH only at low concentrations (below 1·10−2 % wt/wt), due to their pH-dependent conformational changes. HPMC resulted less surface active at pH 3 (below 1·10−4 % wt/wt concentration) that at pH 6. On kinetic studies (π–t), the behavior of β-lg, HPMC and BSA did not change with pH but α-la presented a higher surface activity at pH 3 than 6, even on saturating bulk concentrations. Mixtures of β-lg or BSA with HPMC showed a behavior in between that of single components revealing a net competence for the interface but the mixture α-la and HPMC at pH 6 showed an enhance adsorption. Rheological studies (surface dilatational elastic, Ed, over time) presented the major differences for pHs evaluated. The α-la formed extremely viscoelastic films at pH 6.0, while at pH 3 has the lowest Ed value. β-lg and HPMC films were more viscoelastic at pH 6, being Ed protein film higher. Finally, BSA presented the lowest viscoelastic films without differences between both pHs. For mixtures: i) at pH 6 β-lg/HPMC mixture Ed was dominated by HPMC; at pH 3.0, Ed begins dominated by HPMC, reaching an intermediate value; ii) α-la/HPMC mixture formed more viscoelastic films at pH 6.0 with an intermediate Ed value, while at pH 3.0 the Ed is dominated by protein; iii) BSA/HPMC mixture presented a similar trend in Ed behavior at both pHs.
Fil: Jara, Federico Luis. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Carrera Sánchez, Cecilio. Universidad de Sevilla; España
Fil: Rodríguez Patino, Juan M.. Universidad de Sevilla; España
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The interfacial properties at the air–water (A/W) of each individual whey proteins (β-lactoglobulin, β-lg; α-lactalbumin, α-la; bovin serum albumin, BSA), and their mixtures with a surface-active polysaccharide, hydroxypropylmethylcellulose (HPMC) were studied at pH 3 or 6. The interfacial films were studied by measurement surface pressure (π) isotherms and dynamics of adsorption. At equilibrium proteins surface activity was affected by pH only at low concentrations (below 1·10−2 % wt/wt), due to their pH-dependent conformational changes. HPMC resulted less surface active at pH 3 (below 1·10−4 % wt/wt concentration) that at pH 6. On kinetic studies (π–t), the behavior of β-lg, HPMC and BSA did not change with pH but α-la presented a higher surface activity at pH 3 than 6, even on saturating bulk concentrations. Mixtures of β-lg or BSA with HPMC showed a behavior in between that of single components revealing a net competence for the interface but the mixture α-la and HPMC at pH 6 showed an enhance adsorption. Rheological studies (surface dilatational elastic, Ed, over time) presented the major differences for pHs evaluated. The α-la formed extremely viscoelastic films at pH 6.0, while at pH 3 has the lowest Ed value. β-lg and HPMC films were more viscoelastic at pH 6, being Ed protein film higher. Finally, BSA presented the lowest viscoelastic films without differences between both pHs. For mixtures: i) at pH 6 β-lg/HPMC mixture Ed was dominated by HPMC; at pH 3.0, Ed begins dominated by HPMC, reaching an intermediate value; ii) α-la/HPMC mixture formed more viscoelastic films at pH 6.0 with an intermediate Ed value, while at pH 3.0 the Ed is dominated by protein; iii) BSA/HPMC mixture presented a similar trend in Ed behavior at both pHs.
publishDate 2013
dc.date.none.fl_str_mv 2013-06
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/11336/30365
Jara, Federico Luis; Carrera Sánchez, Cecilio; Rodríguez Patino, Juan M.; Pilosof, Ana Maria Renata; Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH; Elsevier; Food Hydrocolloids; 35; 6-2013; 189-197
0268-005X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/30365
identifier_str_mv Jara, Federico Luis; Carrera Sánchez, Cecilio; Rodríguez Patino, Juan M.; Pilosof, Ana Maria Renata; Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose: influence of pH; Elsevier; Food Hydrocolloids; 35; 6-2013; 189-197
0268-005X
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/j.foodhyd.2013.05.013
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X13001495
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
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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