On the Analysis of Ellipsometric Measurements of Adsorption Layers at Fluid Interfaces

Langmuir ◽  
1999 ◽  
Vol 15 (20) ◽  
pp. 7002-7007 ◽  
Author(s):  
R. Teppner ◽  
S. Bae ◽  
K. Haage ◽  
H. Motschmann
Keyword(s):  
Fluid Interfaces ◽  
Adsorption Layers

Studies of a Mixed Adsorption Layer of Butan-1-ol and o-Toluidine on Mercury Electrode

2002 ◽  
Vol 67 (11) ◽  
pp. 1579-1588 ◽  
Author(s):  
Dorota Sieńko ◽  
Dorota Gugała ◽  
Jolanta Nieszporek ◽  
Joanna Jankowska ◽  
Jadwiga Saba
Keyword(s):  
Thermodynamic Analysis ◽  
Adsorption Layer ◽  
Supporting Electrolyte ◽  
Mercury Electrode ◽  
Interaction Constant ◽  
Repulsive Interaction ◽  
Surface Excess ◽  
Adsorption Parameters ◽  
Frumkin Isotherm ◽  
Adsorption Layers

The results of thermodynamic analysis of o-toluidine adsorption on a mercury electrode in the presence of various butan-1-ol amounts complete our previous studies on properties of mixed adsorption layers of toluidine isomers-butan-1-ol. The values of the relative surface excess Γ'°T obtained for o-toluidine show that adsorption of this compound decreases with increasing of butan-1-ol concentration. Analysis of adsorption parameters derived from the Frumkin isotherm indicates that in the presence of 0.33 M BuOH in 1 M NaClO4 with adjusted pH 3 as supporting electrolyte, ∆G0 values for o-toluidine are the highest and, at the same time, the strongest repulsive interaction occurs. In the presence of 0.11 M butan-1-ol, smaller values of ∆G0 for o-toluidine correspond to weaker repulsive interaction. Therefore the change of the Γ'°T value for o-toluidine as a function of butan-1-ol concentration is the result of mutual changes of ∆G0 and interaction constant A between adsorbate molecules.

scholarly journals Surfactant Adsorption to Different Fluid Interfaces

Langmuir ◽  
2021 ◽  
Author(s):  
Jotam Bergfreund ◽  
Sarina Siegenthaler ◽  
Viviane Lutz-Bueno ◽  
Pascal Bertsch ◽  
Peter Fischer
Keyword(s):  
Fluid Interfaces ◽  
Surfactant Adsorption

scholarly journals Proteins from microalgae for the stabilization of fluid interfaces, emulsions, and foams

2021 ◽  
Vol 108 ◽  
pp. 326-342
Author(s):  
Pascal Bertsch ◽  
Lukas Böcker ◽  
Alexander Mathys ◽  
Peter Fischer
Keyword(s):  
Fluid Interfaces

scholarly journals β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH

2021 ◽  
Vol 5 (1) ◽  
pp. 14
Author(s):  
Georgi G. Gochev ◽  
Volodymyr I. Kovalchuk ◽  
Eugene V. Aksenenko ◽  
Valentin B. Fainerman ◽  
Reinhard Miller
Keyword(s):  
Theoretical Description ◽  
Fluid Interfaces ◽  
Interfacial Behavior ◽  
Current State ◽  
Air Interface ◽  
Direct Measurements ◽  
Wide Range ◽  
Dilational Viscoelasticity ◽  
Parameter Values ◽  
Β Lactoglobulin

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.

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