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

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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 wer...

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Autores principales: Jara, F.L., Carrera Sánchez, C., Rodríguez Patino, J.M., Pilosof, A.M.R.
Formato: JOUR
Materias:
α-Lactalbumin
β-Lactoglobulin
Air/water interface
Bovin serum albumin
Hydroxypropylmethylcellulose
PH-dependence
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0268005X_v35_n_p189_Jara
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_0268005X_v35_n_p189_Jara2023-10-03T15:13:44Z Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose. Influence of pH Jara, F.L. Carrera Sánchez, C. Rodríguez Patino, J.M. Pilosof, A.M.R. α-Lactalbumin β-Lactoglobulin Air/water interface Bovin serum albumin Hydroxypropylmethylcellulose PH-dependence 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. © 2013 Elsevier Ltd. Fil:Jara, F.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0268005X_v35_n_p189_Jara
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic α-Lactalbumin
β-Lactoglobulin
Air/water interface
Bovin serum albumin
Hydroxypropylmethylcellulose
PH-dependence
spellingShingle α-Lactalbumin
β-Lactoglobulin
Air/water interface
Bovin serum albumin
Hydroxypropylmethylcellulose
PH-dependence
Jara, F.L.
Carrera Sánchez, C.
Rodríguez Patino, J.M.
Pilosof, A.M.R.
Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose. Influence of pH
topic_facet α-Lactalbumin
β-Lactoglobulin
Air/water interface
Bovin serum albumin
Hydroxypropylmethylcellulose
PH-dependence
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. © 2013 Elsevier Ltd.
format JOUR
author Jara, F.L.
Carrera Sánchez, C.
Rodríguez Patino, J.M.
Pilosof, A.M.R.
author_facet Jara, F.L.
Carrera Sánchez, C.
Rodríguez Patino, J.M.
Pilosof, A.M.R.
author_sort Jara, F.L.
title Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose. Influence of pH
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
url http://hdl.handle.net/20.500.12110/paper_0268005X_v35_n_p189_Jara
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AT carrerasanchezc competitiveadsorptionbehaviorofblactoglobulinalactalbuminbovinserumalbumininpresenceofhydroxypropylmethylcelluloseinfluenceofph
AT rodriguezpatinojm competitiveadsorptionbehaviorofblactoglobulinalactalbuminbovinserumalbumininpresenceofhydroxypropylmethylcelluloseinfluenceofph
AT pilosofamr competitiveadsorptionbehaviorofblactoglobulinalactalbuminbovinserumalbumininpresenceofhydroxypropylmethylcelluloseinfluenceofph
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