We have studied oil-in-water emulsions stabilized by monodisperse, fluorescent silica colloids presenting either a smooth or a rough surface. The presence of the fluorescent core allows for direct visualization of the colloids on the surface of the emulsion droplets. Droplet interfacial tension, measured by micropipet tensiometry, is not modified by particle adsorption at the interface, suggesting a purely steric stabilization mechanism. Surface roughness is shown to considerably lessen the ability of particles to stabilize droplets. At variance with what is commonly assumed, no straightforward relation exists between the extent of particle interfacial adsorption and emulsion macroscopic stability; stable emulsions can be obtained even with very low droplet surface coverage. Finally, we directly monitor the Brownian motion of the adsorbed particles, showing that their surface diffusion coefficient is very close to the bulk value. Evidence of a possible role of particle surface dynamics on the stabilization of poorly covered droplets is presented.

A waxy crude oil which gels below a threshold temperature has been investigated under static and dynamic conditions, using a combination of rheological methods, optical microscopy, and DSC. Particular attention is given in this work to the influence of the mechanical history on gel strength and to describing the time-dependent rheological behavior. The gels display a strong dependence of the yield stress and moduli on the shear history, cooling rate, and stress loading rate. Of particular interest is the partial recovery of the gel structure after application of small stress or strain (much smaller than the critical values needed for flow onset) during cooling, which can be used to reduce the ultimate strength of the crude oil gel formed below the pour point. A second focus of this study is to further develop the physical interpretation of the mechanism by which wax crystallization produces gelation. Gelation of the waxy crude oil studied is suggested to be the result of the association between wax crystals, which produces an extended network structure, and it is shown that the system displays features common to attractive colloidal gels, for one of which, fumed silica (Aerosil 200) in paraffin oil, rheological data are reported. The colloidal gel model provides a simple and economical basis for explaining the response of the gelled oil to various mechanical perturbations and constitutes a fruitful basis from which to develop technologies for controlling the gelation phenomenon, as suggested by the rheological results reported.

The high-molecular-weight paraffinic (‘wax’) fraction separates from crude oils at low temperatures, a process that can lead to a sol–gel transition when the mass of wax solids exceeds 1–2%. Attractive interactions between the micron-size wax solids suspended in the non-polar medium have been suggested to be responsible for gel formation. The present study reports an optically transparent model oil system, based on a mixture of linear and branched paraffins. Rheological measurements and optical microscopy show that the model system reproduces essential features of crude oil gels. Small-angle light scattering studies conducted at temperatures intermediate between the cloud point (58 °C) and sol–gel transition (39 °C) show that phase separation and wax solid aggregation are rapid processes, leading to the formation of dynamically arrested structures well above the sol–gel transition determined rheologically. Analysis of gravity settling effects has provided a rough estimate for the yield stress of the wax particle network formed (greater than 0.7 Pa at 45 °C and 0.07 Pa at 55 °C). Clusters formed by the aggregated wax solids possess a fractal dimension of about 1.8, consistent with diffusion-limited cluster–cluster aggregation.

Solubilization of membrane proteins requires surfactants, whose structural properties play a crucial role in determining the protein phase behavior. We show that ionization of a pH-sensitive surfactant, lauryldymethylamino-N-oxide, bound to the bacterial photosynthetic Reaction Center, induces protein phase segregation in micrometric "droplets." Liquid-liquid phase separation takes place in a narrow pH range, is promoted by increasing temperature, and vanishes by adding salt. After a fast initial droplet growth, the nearly arrested kinetics at a later stage leaves the system in a finely divided, long-lasting emulsified state.

Streptococcus agalactiae is an etiological agent of several infective diseases in humans. We previously demonstrated that FbsA, a fibrinogen-binding protein expressed by this bacterium, elicits a fibrinogen-dependent aggregation of platelets. In the present communication, we show that the binding of FbsA to fibrinogen is specific and saturable, and that the FbsA-binding site resides in the D region of fibrinogen. In accordance with the repetitive nature of the protein, we found that FbsA contains multiple binding sites for fibrinogen. By using several biophysical methods, we provide evidence that the addition of FbsA induces extensive fibrinogen aggregation and has noticeable effects on thrombin-catalyzed fibrin clot formation. Fibrinogen aggregation was also found to depend on FbsA concentration and on the number of FbsA repeat units. Scanning electron microscopy evidentiated that, while fibrin clot is made of a fine fibrillar network, FbsA-induced Fbg aggregates consist of thicker fibers organized in a cage-like structure. The structural difference of the two structures was further indicated by the diverse immunological reactivity and capability to bind tissue-type plasminogen activator or plasminogen. The mechanisms of FbsA-induced fibrinogen aggregation and fibrin polymerization followed distinct pathways since Fbg assembly was not inhibited by GPRP, a specific inhibitor of fibrin polymerization. This finding was supported by the different sensitivity of the aggregates to the disruptive effects of urea and guanidine hydrochloride. We suggest that FbsA and fibrinogen play complementary roles in contributing to thrombogenesis associated with S. agalactiae infection.