Growth of wormlike micelles in nonionic surfactant solutions: Quantitative theory vs. experiment.

Despite the considerable advances of molecular-thermodynamic theory of micelle growth, agreement between theory and experiment has been achieved only in isolated cases. A general theory that can provide self-consistent quantitative description of the growth of wormlike micelles in mixed surfactant solutions, including the experimentally observed high peaks in viscosity and aggregation number, is still missing. As a step toward the creation of such theory, here we consider the simplest system - nonionic wormlike surfactant micelles from polyoxyethylene alkyl ethers, CiEj. Our goal is to construct a molecular-thermodynamic model that is in agreement with the available experimental data. For this goal, we systematized data for the micelle mean mass aggregation number, from which the micelle growth parameter was determined at various temperatures. None of the available models can give a quantitative description of these data. We constructed a new model, which is based on theoretical expressions for the interfacial-tension, headgroup-steric and chain-conformation components of micelle free energy, along with appropriate expressions for the parameters of the model, including their temperature and curvature dependencies. Special attention was paid to the surfactant chain-conformation free energy, for which a new more general formula was derived. As a result, relatively simple theoretical expressions are obtained. All parameters that enter these expressions are known, which facilitates the theoretical modeling of micelle growth for various nonionic surfactants in excellent agreement with the experiment. The constructed model can serve as a basis that can be further upgraded to obtain quantitative description of micelle growth in more complicated systems, including binary and ternary mixtures of nonionic, ionic and zwitterionic surfactants, which determines the viscosity and stability of various formulations in personal-care and house-hold detergency.

Rheology of particle/water/oil three-phase dispersions: Electrostatic vs. capillary bridge forces.

HYPOTHESIS: Particle/water/oil three-phase capillary suspensions possess the remarkable property to solidify upon the addition of minimal amount of the second (dispersed) liquid. The hardening of these suspensions is due to capillary bridges, which interconnect the particles (pendular state). Electrostatic repulsion across the oily phase, where Debye screening by electrolyte is missing, could also influence the hardness of these suspensions. EXPERIMENTS: We present data for oil-continuous suspensions with aqueous capillary bridges between hydrophilic SiO2 particles at particle volume fractions 35-45%. The hardness is characterized by the yield stress Y for two different oils: mineral (hexadecane) and vegetable (soybean oil). FINDINGS AND MODELLING: The comparison of data for the "mirror" systems of water- and oil-continuous capillary suspensions shows that Y is lower for the oil-continuous ones. The theoretical model of yield stress is upgraded by including a contribution from electrostatic repulsion, which partially counterbalances the capillary-bridge attraction and renders the suspensions softer. The particle charge density determined from data fits is close to that obtained in experiments with monolayers from charged colloid particles at oil/water interfaces. The results could contribute for better understanding, quantitative prediction and control of the mechanical properties of solid/liquid/liquid capillary suspensions.

Hardening of particle/oil/water suspensions due to capillary bridges: Experimental yield stress and theoretical interpretation.

Suspensions of colloid particles possess the remarkable property to solidify upon the addition of minimal amount of a second liquid that preferentially wets the particles. The hardening is due to the formation of capillary bridges (pendular rings), which connect the particles. Here, we review works on the mechanical properties of such suspensions and related works on the capillary-bridge force, and present new rheological data for the weakly studied concentration range 30-55 vol% particles. The mechanical strength of the solidified capillary suspensions, characterized by the yield stress Y, is measured at the elastic limit for various volume fractions of the particles and the preferentially wetting liquid. A quantitative theoretical model is developed, which relates Y with the maximum of the capillary-bridge force, projected on the shear plane. A semi-empirical expression for the mean number of capillary bridges per particle is proposed. The model agrees very well with the experimental data and gives a quantitative description of the yield stress, which increases with the rise of interfacial tension and with the volume fractions of particles and capillary bridges, but decreases with the rise of particle radius and contact angle. The quantitative description of capillary force is based on the exact theory and numerical calculation of the capillary bridge profile at various bridge volumes and contact angles. An analytical formula for Y is also derived. The comparison of the theoretical and experimental strain at the elastic limit reveals that the fluidization of the capillary suspension takes place only in a deformation zone of thickness up to several hundred particle diameters, which is adjacent to the rheometer's mobile plate. The reported experimental results refer to water-continuous suspension with hydrophobic particles and oily capillary bridges. The comparison of data for bridges from soybean oil and hexadecane surprisingly indicate that the yield strength is greater for the suspension with soybean oil despite its lower interfacial tension against water. The result can be explained with the different contact angles of the two oils in agreement with the theoretical predictions. The results could contribute for a better understanding, quantitative prediction and control of the mechanical properties of three-phase capillary suspensions solid/liquid/liquid.

Adhesion of bubbles and drops to solid surfaces, and anisotropic surface tensions studied by capillary meniscus dynamometry.

Here, we review the principle and applications of two recently developed methods: the capillary meniscus dynamometry (CMD) for measuring the surface tension of bubbles/drops, and the capillary bridge dynamometry (CBD) for quantifying the bubble/drop adhesion to solid surfaces. Both methods are based on a new data analysis protocol, which allows one to decouple the two components of non-isotropic surface tension. For an axisymmetric non-fluid interface (e.g. bubble or drop covered by a protein adsorption layer with shear elasticity), the CMD determines the two different components of the anisotropic surface tension, σs and σφ, which are acting along the "meridians" and "parallels", and vary throughout the interface. The method uses data for the instantaneous bubble (drop) profile and capillary pressure, but the procedure for data processing is essentially different from that of the conventional drop shape analysis (DSA) method. In the case of bubble or drop pressed against a substrate, which forms a capillary bridge, the CBD method allows one to determine also the capillary-bridge force for both isotropic (fluid) and anisotropic (solidified) adsorption layers. The experiments on bubble (drop) detachment from the substrate show the existence of a maximal pulling force, Fmax, that can be resisted by an adherent fluid particle. Fmax can be used to quantify the strength of adhesion of bubbles and drops to solid surfaces. Its value is determined by a competition of attractive transversal tension and repulsive disjoining pressure forces. The greatest Fmax values have been measured for bubbles adherent to glass substrates in pea-protein solutions. The bubble/wall adhesion is lower in solutions containing the protein HFBII hydrophobin, which could be explained with the effect of sandwiched protein aggregates. The applicability of the CBD method to emulsion systems is illustrated by experiments with soybean-oil drops adherent to hydrophilic and hydrophobic substrates in egg yolk solutions. The results reveal how the interfacial rigidity, as well as the bubble/wall and drop/wall adhesion forces, can be quantified and controlled in relation to optimizing the properties of foams and emulsions.

Hydrophobic modification of chitin whisker and its potential application in structuring oil.

A facile approach was developed to modify chitin whiskers by reacting them with bromohexadecane, and the potential application of modified whiskers in structuring oil was evaluated. The results of Fourier transform infrared spectra (FT-IR), wide-angle X-ray diffraction (XRD), elemental analysis, solid (13)C NMR, and differential scanning calorimeter (DSC) confirmed that the long alkyl chains were successfully introduced to the chitin whiskers and endowed them with improved hydrophobicity and thermal transition. By hot pressing the modified whiskers, the highly hydrophobic whisker sheets were constructed, showing high contact angles close to 150°. The hydrophobic interaction between the long alkyl chains and chitin backbone induced the crystal alignment with micro-nano structure, leading to the surface roughness and high hydrophobicity of the sheets. Furthermore, the modified whiskers could form a stable dispersion in sunflower oil, displaying a remarkable thickening effect. The viscosity of the oily suspension exhibited temperature dependence and shear-thinning behavior, suggesting great potentials to fabricate oleogel without adding any saturated fat. Furthermore, the intrinsic biocompatibility of α-chitin structure benefits its application in foodstuff, cosmetics, and medical fields.

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.

Shear rheology of mixed protein adsorption layers vs their structure studied by surface force measurements.

The hydrophobins are proteins that form the most rigid adsorption layers at liquid interfaces in comparison with all other investigated proteins. The mixing of hydrophobin HFBII with other conventional proteins is expected to reduce the surface shear elasticity and viscosity, E(sh) and η(sh), proportional to the fraction of the conventional protein. However, the experiments show that the effect of mixing can be rather different depending on the nature of the additive. If the additive is a globular protein, like ß-lactoglobulin and ovalbumin, the surface rigidity is preserved, and even enhanced. The experiments with separate foam films indicate that this is due to the formation of a bilayer structure at the air/water interface. The more hydrophobic HFBII forms the upper layer adjacent to the air phase, whereas the conventional globular protein forms the lower layer that faces the water phase. Thus, the elastic network formed by the adsorbed hydrophobin remains intact, and even reinforced by the adjacent layer of globular protein. In contrast, the addition of the disordered protein ß-casein leads to softening of the HFBII adsorption layer. Similar (an even stronger) effect is produced by the nonionic surfactant Tween 20. This can be explained with the penetration of the hydrophobic tails of ß-casein and Tween 20 between the HFBII molecules at the interface, which breaks the integrity of the hydrophobin interfacial elastic network. The analyzed experimental data for the surface shear rheology of various protein adsorption layers comply with a viscoelastic thixotropic model, which allows one to determine E(sh) and η(sh) from the measured storage and loss moduli, G' and G″. The results could contribute for quantitative characterization and deeper understanding of the factors that control the surface rigidity of protein adsorption layers with potential application for the creation of stable foams and emulsions with fine bubbles or droplets.

Growth of bubbles on a solid surface in response to a pressure reduction.

A diffusion-controlled method is presented to study the growth of bubbles on a solid surface. The bubbles are nucleated spontaneously on a hydrophobic smooth surface in response to a sudden pressure reduction and then grow with an expanding contact line. The evolution of the bubbles in the early stage is found to grow with a constant bubble radius and a decreasing contact angle, while the bubbles continue their growth with a constant contact angle and an increasing bubble radius after the contact angle reaches its equilibrium value. A total variation of about 60° of the contact angle is observed during the growth of the bubbles with the size scale of 10-100 µm in radius. The growing process is described by the diffusion theory with the validation of the growth constant.

Sonication-microfluidics for fabrication of nanoparticle-stabilized microbubbles.

An approach based upon sonication-microfluidics is presented to fabricate nanoparticle-coated microbubbles. The gas-in-liquid slug flow formed in a microchannel is subjected to ultrasound, leading to cavitation at the gas-liquid interface. Therefore, microbubbles are formed and then stabilized by the nanoparticles contained in the liquid. Compared to the conventional sonication method, this sonication-microfluidics continuous flow approach has unlimited gas nuclei for cavitation that yields continuous production of foam with shorter residence time. By controlling the flow rate ratios of the gas to the liquid, this method also achieves a higher production volume, smaller bubble size, and less waste of the nanoparticles needed to stabilize the microbubbles.

Surface pressure and elasticity of hydrophobin HFBII layers on the air-water interface: rheology versus structure detected by AFM imaging.

Here, we combine experiments with Langmuir trough and atomic force microscopy (AFM) to investigate the reasons for the special properties of layers from the protein HFBII hydrophobin spread on the air-water interface. The hydrophobin interfacial layers possess the highest surface dilatational and shear elastic moduli among all investigated proteins. The AFM images show that the spread HFBII layers are rather inhomogeneous, (i.e., they contain voids, monolayer and multilayer domains). A continuous compression of the layer leads to filling the voids and transformation of a part of the monolayer into a trilayer. The trilayer appears in the form of large surface domains, which can be formed by folding and subduction of parts from the initial monolayer. The trilayer appears also in the form of numerous submicrometer spots, which can be obtained by forcing protein molecules out of the monolayer and their self-assembly into adjacent pimples. Such structures are formed because not only the hydrophobic parts, but also the hydrophilic parts of the HFBII molecules can adhere to each other in the water medium. If a hydrophobin layer is subjected to oscillations, its elasticity considerably increases, up to 500 mN/m, which can be explained with compaction. The relaxation of the layer's tension after expansion or compression follows the same relatively simple law, which refers to two-dimensional diffusion of protein aggregates within the layer. The characteristic diffusion time after compression is longer than after expansion, which can be explained with the impedence of diffusion in the more compact interfacial layer. The results shed light on the relation between the mesoscopic structure of hydrophobin interfacial layers and their unique mechanical properties that find applications for the production of foams and emulsions of extraordinary stability; for the immobilization of functional molecules at surfaces, and as coating agents for surface modification.

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.

Surface shear rheology of adsorption layers from the protein HFBII hydrophobin: effect of added ß-casein.

The surface shear rheology of hydrophobin HFBII adsorption layers is studied in angle-ramp/relaxation regime by means of a rotational rheometer. The behavior of the system is investigated at different shear rates and concentrations of added ß-casein. In angle-ramp regime, the experimental data comply with the Maxwell model of viscoelastic behavior. From the fits of the rheological curves with this model, the surface shear elasticity and viscosity, E(sh) and η(sh), are determined at various fixed shear rates. The dependence of η(sh) on the rate of strain obeys the Herschel-Bulkley law. The data indicate an increasing fluidization (softening) of the layers with the rise of the shear rate. The addition of ß-casein leads to more rigid adsorption layers, which exhibit a tendency of faster fluidization at increasing shear rates. In relaxation regime, the system obeys a modified Andrade's (cubic root) law, with two characteristic relaxation times. The fact that the data comply with the Maxwell model in angle-ramp regime, but follow the modified Andrade's low in relaxation regime, can be explained by the different processes occurring in the viscoelastic protein adsorption layer in these two regimes: breakage and restoration of intermolecular bonds at angle-ramp vs solidification of the layer at relaxation.

Self-assembled bilayers from the protein HFBII hydrophobin: nature of the adhesion energy.

The hydrophobins are a class of amphiphilic proteins which spontaneously adsorb at the air/water interface and form elastic membranes of high mechanical strength as compared to other proteins. The mechanism of hydrophobin adhesion is of interest for fungal biology and for various applications in electronics, medicine, and food industry. We established that the drainage of free foam films formed from HFBII hydrophobin solutions ends with the appearance of a 6 nm thick film, which consists of two layers of protein molecules, that is, it is a self-assembled bilayer (S-bilayer), with hydrophilic domains pointing inward and hydrophobic domains pointing outward. Its formation is accompanied by a considerable energy gain, which is much greater than that typically observed with free liquid films. The experiments at different pH show that this attraction between the "hydrophilic" parts of the HFBII molecules is dominated by the short-range hydrophobic interaction rather than by the patch-charge electrostatic attraction.

Unique properties of bubbles and foam films stabilized by HFBII hydrophobin.

The HFBII hydrophobin is an amphiphilic protein that can irreversibly adsorb at the air/water interface. The formed protein monolayers can reach a state of two-dimensional elastic solid that exhibits a high mechanical strength as compared to adsorption layers of typical amphiphilic proteins. Bubbles formed in HFBII solutions preserve the nonspherical shape they had at the moment of solidification of their surfaces. The stirring of HFBII solutions leads to the formation of many bubbles of micrometer size. Measuring the electrophoretic mobility of such bubbles, the ζ-potential was determined. Upon compression, the HFBII monolayers form periodic wrinkles of wavelength 11.5 µm, which corresponds to bending elasticity k(c) = 1.1 × 10(-19) J. The wrinkled hydrophobin monolayers are close to a tension-free state, which prevents the Ostwald ripening and provides bubble longevity in HFBII stabilized foams. Films formed between two bubbles are studied by experiments in a capillary cell. In the absence of added electrolyte, the films are electrostatically stabilized. The appearance of protein aggregates is enhanced with the increase of the HFBII and electrolyte concentrations and at pH close to the isoelectric point. When the aggregate concentration is not too high (to block the film thinning), the films reach a state with 12 nm uniform thickness, which corresponds to two surface monolayers plus HFBII tetramers sandwiched between them. In water, the HFBII molecules can stick to each other not only by their hydrophobic moieties but also by their hydrophilic parts. The latter leads to the attachment of HFBII aggregates such as dimers, tetramers, and bigger ones to the interfacial adsorption monolayers, which provides additional stabilization of the liquid films.