The incorporation of soft hydrophilic particles at the interface of water in non-polar oil emulsion droplets is crucial for several applications. However, the stabilization of water in non-polar oil emulsions with hydrophilic soft material alone is, besides certain exceptions, not possible. In our previous works, we showed that stabilizing the emulsions with well-characterized spherical hydrophobic silica nanospheres (SNs) and soft equally charged microgel particles (MGs) is a robust strategy to stabilize w/o emulsions while still incorporating a large amount of MGs at the interface. In the present study, we address the question of what the maximum amount of MGs at the interface in these kinds of emulsion droplets can be. By using well-characterized mono-disperse SNs, we are able to calculate the fraction of interface covered by the SNs and complementary that of the present MG. We found that it is not possible to decrease the SN coverage below 56% irrespective of MG softness and SN size. The findings elucidate new perspectives to the broader topic of soft/solid stabilized emulsions.

Foam film’s properties have a high impact on the properties of the macroscopic foams. This work focusses on protein stabilized foam films. The direct comparison of three different proteins with a concentration normalized to the protein surface enables to distinguish between electrostatic, steric and network stabilization effects. In order to untangle those effects, we study and compare two globular proteins (β − lactoglobulin, BLG, and bovine serum albumin, BSA) and a disordered, flexible protein (whole casein, CN) at low ionic strengths with varying solution pH. Image intensity measurement as a recently developed image analysis method in this field allows to record spatially resolved disjoining pressure isotherms in a Thin Film Pressure Balance (TFPB). This reveals insights into the structure formation in inhomogeneous protein films. As a novel method we introduce tracking inhomogeneities (features) which enables the measurement of interfacial mobility and stiffness of foam films. Around the isoelectric point (IEP), Newton Black Films (NBF) form which are stable for the globular proteins while they are unstable for the disordered flexible one. This difference in film stability is explained by different characteristics of the network structures which is supported by findings in the bulk and at the surface of the respective protein solutions.