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 mode