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

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, Federico Luis, Pilosof, Ana María Renata
Publicado:	2014
Materias:	α-Lactalbumin β-Lactoglobulin Air/water interface Bovin serum albumin Hydroxypropylmethylcellulose PH-dependence
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v35_n_p189_Jara 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

id	paper:paper_0268005X_v35_n_p189_Jara
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spelling	paper:paper_0268005X_v35_n_p189_Jara2023-06-08T15:23:54Z Competitive adsorption behavior of β-lactoglobulin, α-lactalbumin, bovin serum albumin in presence of hydroxypropylmethylcellulose. Influence of pH Jara, Federico Luis Pilosof, Ana María Renata 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. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v35_n_p189_Jara 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, Federico Luis Pilosof, Ana María Renata 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.
author	Jara, Federico Luis Pilosof, Ana María Renata
author_facet	Jara, Federico Luis Pilosof, Ana María Renata
author_sort	Jara, Federico Luis
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
publishDate	2014
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v35_n_p189_Jara http://hdl.handle.net/20.500.12110/paper_0268005X_v35_n_p189_Jara
work_keys_str_mv	AT jarafedericoluis competitiveadsorptionbehaviorofblactoglobulinalactalbuminbovinserumalbumininpresenceofhydroxypropylmethylcelluloseinfluenceofph AT pilosofanamariarenata competitiveadsorptionbehaviorofblactoglobulinalactalbuminbovinserumalbumininpresenceofhydroxypropylmethylcelluloseinfluenceofph
_version_	1768546582671654912

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

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