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

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

X-Ray and EPR study on copper (II) complexes with an enamine ligand

AbstractThe enamine (HEAID) obtained from aniline and 2-acetyl-1,3-indandione (2AID) behaves as a bidentate ligand in coordination with copper (II) ion. Two types of crystals, apparently different in shape, were isolated and studied by single-crystal X-ray diffraction. The X-ray data for the brown rhombic crystals of compound 1 shows a mononuclear complex of Cu(II) coordinated with two EAID-anions, Cu(EAID)2. The X-ray data for the green crystals of compound 2 shows a dinuclear Cu(II) complex with two OH− groups acting as bridging ligands, [Cu2(μ-OH)2(EAID)2]. In both cases the ligand coordinates after deprotonation of the amine group

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 4. Impact on the Stability of Foam Films and Foams

The complexity and high sensitivity of proteins to environmental factors give rise to a multitude of variables, which affect the stabilization mechanisms in protein foams. Interfacial and foaming properties of proteins have been widely studied, but the reported unique effect of pH, which can be of great interest to applications, has been investigated to a lesser extent. In this paper, we focus on the impact of pH on the stability of black foam films and corresponding foams obtained from solutions of a model globular protein—the whey β-lactoglobulin (BLG). Foam stability was analyzed utilizing three characteristic parameters (deviation time, transition time and half-lifetime) for monitoring the foam decay, while foam film stability was measured in terms of the critical disjoining pressure of film rupture. We attempt to explain correlations between the macroscopic properties of a foam system and those of its major building blocks (foam films and interfaces), and thus, to identify structure-property relationships in foam. Good correlations were found between the stabilities of black foam films and foams, while relations to the properties of adsorption layers appeared to be intricate. That is because pH-dependent interfacial properties of proteins usually exhibit an extremum around the isoelectric point (pI), but the stability of BLG foam films increases with increasing pH (3–7), which is well reflected in the foam stability. We discuss the possible reasons behind these intriguingly different behaviors on the basis of pH-induced changes in the molecular properties of BLG, which seem to be determining the mechanism of film rupture at the critical disjoining pressure

Exploring proteins at soft interfaces and in thin liquid films – From classical methods to advanced applications of reflectometry

The history of the topic of proteins at soft interfaces dates back to the 19th century, and until the present day, it has continuously attracted great scientific interest. A multitude of experimental methods and theoretical approaches have been developed to serve the research progress in this large domain of colloid and interface science, including the area of soft colloids such as foams and emulsions. From classical methods like surface tension adsorption isotherms, surface pressure-area measurements for spread layers, and surface rheology probing the dynamics of adsorption, nowadays, advanced surface-sensitive techniques based on spectroscopy, microscopy, and the reflection of light, X-rays and neutrons at liquid/fluid interfaces offers important complementary sources of information. Apart from the fundamental characteristics of protein adsorption layers, i.e., surface tension and surface excess, the nanoscale structure of such layers and the interfacial protein conformations and morphologies are of pivotal importance for extending the depth of understanding on the topic. In this review article, we provide an extensive overview of the application of three methods, namely, ellipsometry, X-ray reflectometry and neutron reflectometry, for adsorption and structural studies on proteins at water/air and water/oil interfaces. The main attention is placed on the development of experimental approaches and on a discussion of the relevant achievements in terms of notable experimental results. We have attempted to cover the whole history of protein studies with these techniques, and thus, we believe the review should serve as a valuable reference to fuel ideas for a wide spectrum of researchers in different scientific fields where proteins at soft interface may be of relevance