Capillary meniscus dynamometry­method for determining the surface tension of drops and bubbles with isotropic and anisotropic surface stress distributions.

The stresses acting in interfacial adsorption layers with surface shear elasticity are, in general, anisotropic and non-uniform. If a pendant drop or buoyant bubble is covered with such elastic layer, the components of surface tension acting along the "meridians" and "parallels", σ(s) and σ(φ), can be different and, then, the conventional drop shape analysis (DSA) is inapplicable. Here, a method for determining σ(s) and σ(φ) is developed for axisymmetric menisci. This method, called 'capillary meniscus dynamometry' (CMD), is based on processing data for the digitized drop/bubble profile and capillary pressure. The principle of the CMD procedure for data processing is essentially different from that of DSA. Applying the tangential and normal surface stress balance equations, σ(s) and σ(φ) are determined in each interfacial point without using any rheological model. The computational procedure is fast and could be used in real time, during a given process. The method is applied to determine σ(s) and σ(φ) for bubbles and drops formed on the tip of a capillary immersed in solutions of the protein HFBII hydrophobin. Upon a surface compression, meridional wrinkles appear on the bubble surface below the bubble "equator", where the azimuthal tension σ(φ) takes negative values. The CMD method allows one to determine the local tensions acting in anisotropic interfacial layers (films, membranes), like those formed from proteins, polymers, asphaltenes and phospholipids. The CMD is applicable also to fluid interfaces (e.g. surfactant solutions), for which it gives the same surface tension as the conventional methods.

Interfacial layers from the protein HFBII hydrophobin: dynamic surface tension, dilatational elasticity and relaxation times.

The pendant-drop method (with drop-shape analysis) and Langmuir trough are applied to investigate the characteristic relaxation times and elasticity of interfacial layers from the protein HFBII hydrophobin. Such layers undergo a transition from fluid to elastic solid films. The transition is detected as an increase in the error of the fit of the pendant-drop profile by means of the Laplace equation of capillarity. The relaxation of surface tension after interfacial expansion follows an exponential-decay law, which indicates adsorption kinetics under barrier control. The experimental data for the relaxation time suggest that the adsorption rate is determined by the balance of two opposing factors: (i) the barrier to detachment of protein molecules from bulk aggregates and (ii) the attraction of the detached molecules by the adsorption layer due to the hydrophobic surface force. The hydrophobic attraction can explain why a greater surface coverage leads to a faster adsorption. The relaxation of surface tension after interfacial compression follows a different, square-root law. Such behavior can be attributed to surface diffusion of adsorbed protein molecules that are condensing at the periphery of interfacial protein aggregates. The surface dilatational elasticity, E, is determined in experiments on quick expansion or compression of the interfacial protein layers. At lower surface pressures (<11 mN/m) the experiments on expansion, compression and oscillations give close values of E that are increasing with the rise of surface pressure. At higher surface pressures, E exhibits the opposite tendency and the data are scattered. The latter behavior can be explained with a two-dimensional condensation of adsorbed protein molecules at the higher surface pressures. The results could be important for the understanding and control of dynamic processes in foams and emulsions stabilized by hydrophobins, as well as for the modification of solid surfaces by adsorption of such proteins.