Emulsions droplet interactions

At low surfactant concentrations it is observed that an attraction dominates at short separations. The attraction becomes important at separations below about 12 nm when the surfactant concentration is 0.01 mM, and below about 6 nm when the concentration is increased to 0.1 mM. Once the force barrier has been overcome the surfaces are pulled into direct contact between the hydrophobic surfaces at D = 0, demonstrating that the surfactants leave the gap between the surfaces. The solid surfaces have been flocculated. However, at higher surfactant concentrations (1 mM) the surfactants remain on the surfaces even when the separation between the surfaces is small. The force is now purely repulsive and the surfaces are prevented from flocculating. Emulsion droplets interacting in the same way would coalesce at low surfactant concentrations once they have come close enough to overcome the repulsive barrier, but remain stable at higher surfactant concentrations. Note, however, that the surfactant concentration needed to prevent coalescence of emulsion droplets cannot be accurately determined from surface-force measurements using solid surfaces. 

Stiff o/w emulsions can also result from droplet interactions of the internal phase, but this requires emulsifying such a huge amount of internal phase that the droplets exceed close spherical packing. In this state the emulsified particles are squashed together,... 

This chapter comprises two sections. The first describes the most usual techniques to directly measure force versus distance profiles between solid or liquid surfaces. We then describe different long-range forces (range >5 nm) accessible to evaluation via these techniques for different types of surface active species. The second section is devoted to attractive interactions whose strong amplitude and short range are difficult to determine. In the presence of such interactions, emulsion droplets exhibit flat facets at each contact. The free energy of interaction can be evaluated from droplet deformation and reveals interesting issues. 

G. Gillies and C.A. Prestidge Interaction Forces, Deformation and Nano-Rheology of Emulsion Droplets as Determined by Colloid Probe AFM. Adv. Colloid Interface Sci. 108-109, 197 (2004). 

We first consider emulsion droplets submitted to attractive interactions of the order of ks T. Reversible flocculation may be simply produced by adding excess surfactant in the continuous phase of emulsions. As already mentioned in Chapter 2, micelles may induce an attractive depletion interaction between the dispersed droplets. For equal spheres of radius a at center-to-center separation r, the depletion... 

As for direct emulsions, the presence of excess surfactant induces depletion interaction followed by phase separation. Such a mechanism was proposed by Binks et al. [ 12] to explain the flocculation of inverse emulsion droplets in the presence of microemulsion-swollen micelles. The microscopic origin of the interaction driven by the presence of the bad solvent is more speculative. From empirical considerations, it can be deduced that surfactant chains mix more easily with alkanes than with vegetable, silicone, and some functionalized oils. The size dependence of such a mechanism, reflected by the shifts in the phase transition thresholds, is... 

F. Leal-Calderon, O. Mondain-Monval, K. Pays, N. Royer, and J. Bibette Water-in-Oil Emulsions Role of the Solvent Molecular Size on Droplet Interactions. Langmuir 13, 7008 (1997). 

Figure 3.6 Effect of Ca2+ content on predicted values of osmotic pressure (H, , left axis) of caseinate nanoparticles in emulsion continuous phase and the free energy of the depletion interaction (AGdep, , right axis) between a pair of emulsion droplets (

Ion bridging is a specific type of Coulombic interaction involving the simultaneous binding of polyvalent cations (e.g., Ca, Fe, Cu ) to two different anionic functional groups on biopolymer molecules. This type of ionic interaction is commonly involved in associative self-assembly of biopolymers. As a consequence it is also an important contributory factor in the flocculation (via bridging or depletion) of colloidal particles or emulsion droplets in aqueous media containing adsorbed or non-adsorbed biopolymers (Dickinson and McClements, 1995). 

Hence, from the previously described light-scattering study of caseinate self-assembly in solution, we can postulate that heating/cooling not only alters the nature and strength of the physical (hydrophobic) interactions between emulsion droplets covered by caseinate. It most likely also transforms the nanoscale structural characteristics of the protein network in the bulk and at the interface, thereby affecting the viscoelastic and microstructural properties of the emulsions. 

In an OAV emulsion system containing a mixture of surfactant + polysaccharide, the stability behaviour will generally depend on two sets of factors (i) the nature of the surfactant-polysaccharide interactions at the surface of the emulsion droplets, and (ii) the surfactant-polysaccharide interactions in the aqueous medium between the droplets (Dickinson et ah, 1993 Dickinson, 2003 Aoki el al., 2005 Klinkesom et ah, 2004 Chuah et ah, 2009). 

When a biopolymer mixture is either close to phase separation or lies in the composition space of liquid-liquid coexistence (see Figure 7.6a), the effect of thermodynamically unfavourable interactions is to induce biopolymer multilayer formation at the oil-water interface, as observed for the case of legumin + dextran (Dickinson and Semenova, 1992 Tsapkina et al, 1992). Figure 7.6b shows that there are three concentration regions describing the protein adsorption onto the emulsion droplets. The first one (Cprotein< 0.6 wt%) corresponds to incomplete saturation of the protein adsorption layer. The second concentration region (0.6 wt% < 6 proiem < 6 wt%) represents protein monolayer adsorption (T 2 mg m 2). And the third region (Cprotein > 6 wt%) relates to formation of adsorbed protein multilayers on the emulsion droplets. 

It seems that there is probably greater availability of positively charged residues on the adsorbed protein for electrostatic interaction with sulfate groups of the anionic polysaccharide. This could lead to a greater extent of neutralization of dextran sulfate as a result of complex formation, and consequently to a lower thermodynamic affinity of the complexes for the aqueous medium and a lower value of the ( -potential for emulsion droplets in bilayer emulsions. 

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