Gochev, Georgi G. ; Kovalchuk, Volodymyr I. ; Aksenenko, Eugene V. ; Fainerman, Valentin B. ; Miller, Reinhard (2022)
β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH.
In: Colloids and Interfaces, 5 (1)
doi: 10.3390/colloids5010014
Article, Bibliographie
This is the latest version of this item.
Abstract
The theoretical description of the adsorption of proteins at liquid/fluid interfaces suffers from the inapplicability of classical formalisms, which soundly calls for the development of more complicated adsorption models. A Frumkin-type thermodynamic 2-D solution model that accounts for nonidealities of interface enthalpy and entropy was proposed about two decades ago and has been continuously developed in the course of comparisons with experimental data. In a previous paper we investigated the adsorption of the globular protein β-lactoglobulin at the water/air interface and used such a model to analyze the experimental isotherms of the surface pressure, Π(c), and the frequency-, f-, dependent surface dilational viscoelasticity modulus, E(c)f , in a wide range of protein concentrations, c, and at pH 7. However, the best fit between theory and experiment proposed in that paper appeared incompatible with new data on the surface excess, Γ, obtained from direct measurements with neutron reflectometry. Therefore, in this work, the same model is simultaneously applied to a larger set of experimental dependences, e.g., Π(c), Γ(c), E(Π)f , etc., with E-values measured strictly in the linear viscoelasticity regime. Despite this ambitious complication, a best global fit was elaborated using a single set of parameter values, which well describes all experimental dependencies, thus corroborating the validity of the chosen thermodynamic model. Furthermore, we applied the model in the same manner to experimental results obtained at pH 3 and pH 5 in order to explain the well-pronounced effect of pH on the interfacial behavior of β-lactoglobulin. The results revealed that the propensity of β-lactoglobulin globules to unfold upon adsorption and stretch at the interface decreases in the order pH 3 > pH 7 > pH 5, i.e., with decreasing protein net charge. Finally, we discuss advantages and limitations in the current state of the model
Item Type: | Article |
---|---|
Erschienen: | 2022 |
Creators: | Gochev, Georgi G. ; Kovalchuk, Volodymyr I. ; Aksenenko, Eugene V. ; Fainerman, Valentin B. ; Miller, Reinhard |
Type of entry: | Bibliographie |
Title: | β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH |
Language: | English |
Date: | 2022 |
Publisher: | MDPI |
Journal or Publication Title: | Colloids and Interfaces |
Volume of the journal: | 5 |
Issue Number: | 1 |
Collation: | 26 Seiten |
DOI: | 10.3390/colloids5010014 |
Corresponding Links: | |
Abstract: | The theoretical description of the adsorption of proteins at liquid/fluid interfaces suffers from the inapplicability of classical formalisms, which soundly calls for the development of more complicated adsorption models. A Frumkin-type thermodynamic 2-D solution model that accounts for nonidealities of interface enthalpy and entropy was proposed about two decades ago and has been continuously developed in the course of comparisons with experimental data. In a previous paper we investigated the adsorption of the globular protein β-lactoglobulin at the water/air interface and used such a model to analyze the experimental isotherms of the surface pressure, Π(c), and the frequency-, f-, dependent surface dilational viscoelasticity modulus, E(c)f , in a wide range of protein concentrations, c, and at pH 7. However, the best fit between theory and experiment proposed in that paper appeared incompatible with new data on the surface excess, Γ, obtained from direct measurements with neutron reflectometry. Therefore, in this work, the same model is simultaneously applied to a larger set of experimental dependences, e.g., Π(c), Γ(c), E(Π)f , etc., with E-values measured strictly in the linear viscoelasticity regime. Despite this ambitious complication, a best global fit was elaborated using a single set of parameter values, which well describes all experimental dependencies, thus corroborating the validity of the chosen thermodynamic model. Furthermore, we applied the model in the same manner to experimental results obtained at pH 3 and pH 5 in order to explain the well-pronounced effect of pH on the interfacial behavior of β-lactoglobulin. The results revealed that the propensity of β-lactoglobulin globules to unfold upon adsorption and stretch at the interface decreases in the order pH 3 > pH 7 > pH 5, i.e., with decreasing protein net charge. Finally, we discuss advantages and limitations in the current state of the model |
Uncontrolled Keywords: | β-lactoglobulin, pH effect, adsorption layer, monolayer, secondary layer, adsorption isotherm, surface pressure isotherm, equation of state, surface dilational modulus, protein unfolding |
Classification DDC: | 500 Science and mathematics > 500 Science 500 Science and mathematics > 530 Physics 500 Science and mathematics > 540 Chemistry |
Divisions: | 05 Department of Physics 05 Department of Physics > Institute for Condensed Matter Physics |
Date Deposited: | 02 Aug 2024 12:37 |
Last Modified: | 02 Aug 2024 12:37 |
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β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH. (deposited 02 Feb 2022 13:30)
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