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
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/30365
Ver los metadatos del registro completo
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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 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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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 |
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eng |
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Elsevier |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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