Role of the hydrophobic phase for the unique rheologica properties of saponin adsorption layers

Saponins are a diverse class of natural, plant derived surfactants, with peculiar molecular structure consisting of a hydrophobic scaffold and one or several hydrophilic oligosaccharide chains. Saponins have strong surface activity and are used as natural emulsifiers and foaming agents in food and beverage, pharmaceutical, ore processing, and other industries. Many saponins form adsorption layers at the air–water interface with extremely high surface elasticity and viscosity. The molecular origin of the observed unique interfacial visco-elasticity of saponin adsorption layers is of great interest from both scientific and application viewpoints. In the current study we demonstrate that the hydrophobic phase in contact with water has a very strong effect on the interfacial properties of saponins and that the interfacial elasticity and viscosity of the saponin adsorption layers decrease in the order: air > hexadecane » tricaprylin. The molecular mechanisms behind these trends are analyzed and discussed in the context of the general structure of the surfactant adsorption layers at various nonpolar phase–water interfaces

Hydrodynamic cavitation: a bottom-up approach to liquid aeration

We report the use of hydrodynamic cavitation as a novel, bottom-up method for continuous creation of foams comprising of air microbubbles in aqueous systems containing surface active ingredients, like proteins or particles. The hydrodynamic cavitation was created using a converging-diverging nozzle. The air bubble size obtained using this technique was found to be significantly smaller than that achieved using conventional mechanical entrapment of air via shearing or shaking routes, which are in essence top-down approaches. In addition, the technique provided the possibility of forming non-spherical bubbles due to the high elongational stresses experienced by the bubbles as they flow through the nozzle throat. We show that surface active agents with a high surface elasticity modulus can be used to stabilize the nascent air bubbles and keep their elongated shapes for prolonged periods of time. This combination of the cavitation process with appropriate surface active agents offers an opportunity for creating bubbles smaller than 10 microns, which can provide unique benefits in various applications

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, Esh and ¿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 Esh and ¿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

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 airwater 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 layers 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

Competitive adsorption of the protein hydrophobin and an ionic surfactant: Parallel vs sequential adsorption and dilatational rheology

The competitive adsorption of the protein HFBII hydrophobin and the anionic surfactant sodium dodecyl sulfate (SDS) is investigated in experiments on parallel and sequential adsorption of the two components. The dynamic surface tension and the surface storage and loss dilatational moduli are determined by the oscillating bubble method. A new procedure for data processing is proposed, which allows one to collect data from many different runs on a single master curve and to determine more accurately the dependence of the dilatational elasticity on the surface pressure. Experiments on sequential adsorption are performed by exchanging the HFBII solution around the bubble with an SDS solution. Experiments with separate thin foam films bring additional information on the effect of added SDS. The results indicate that if HFBII has first adsorbed at the air/water interface, it cannot be displaced by SDS at any concentration, both below and above the critical micellization concentration (CMC). In the case of parallel adsorption, there is a considerable difference between the cases below and above the CMC. In the former case, SDS cannot prevent the adsorption of HFBII at the interface, whereas in the latter case adsorption of HFBII is absent, which can be explained with hydrophilization of the hydrophobin aggregates by the SDS in the bulk. The surface dilatational elasticity of the HFBII adsorption layers markedly decreases in the presence of SDS, but it recovers after washing out the SDS. With respect to their dilatational rheology, the investigated HFBII layers exhibit purely elastic behavior, the effect of dilatational viscosity being negligible. As a function of surface tension, the elasticity of the investigated interfacial layers exhibits a high maximum, which could be explained with the occurrence of a phase transition in the protein adsorption layer

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