Interfacial dilatational elasticity and viscosity of beta-lactoglobulin at air-water interface using pulsating bubble tensiometry

The ability of proteins to provide stability in foams is greatly influenced by their interfacial dilatational rheological properties. Surface tension response of a pulsatingbubble with an adsorbed layer of beta-lactoglobulin was measured for different frequencies and protein concentrations using a pulsating bubble tensiometer. A methodology, accounting for adsorption/desorption as well as variation of surface concentration due to expansion/contraction, was developed for the evaluation of surface dilatational elasticity and viscosity at different frequencies from these measurements. The adsorption rate constants were inferred from the surface pressure dynamics of protein adsorption using a Langmuir minitrough. The desorption rates were shown to be negligible for beta-lactoglobulin from the surface pressure response of a spread monolayer when subjected to compression in a Langmuir minitrough. The proposed model was employed to infer the interfacial dilatational viscosity and elasticity of an adsorbed beta-lactoglobulin layer at the air-water interface from experimental pulsating bubble data for protein concentrations in the range of 0.01-0.5 wt % at pH 7. As expected, the interfacial dilatational rheological properties were found to be higher at higher protein concentrations, this effect being less pronounced for dilatational elasticity. Heating at 80 degrees C for 30 min was found to result in higher interfacial dilatational viscosity and lower interfacial dilatational elasticity though this difference was within experimental error. The traditional approach for the inference of interfacial dilatational rheological properties is found to overpredict the interfacial dilatational elasticity whereas the viscosity values do not differ significantly from those obtained using the current analysis.     

Surface and interfacial properties of water-soluble wheat proteins

Surface and interfacial properties of water-soluble wheat proteins were investigated and compared with six reference proteins (bovine serum albumin, ovalbumin, β-lactoglobulin, trypsin, cytochrom C and β-amylase). Albumins extracted from wheat flour were separated by the free solution isoelectric focusing. The surface activity at the air/water, dodecane/water interfaces and dilatational rheological behaviour of the adsorbed layers was determined by pendant drop technique. Considerably high surface activity of wheat proteins was found at both interfaces exceeding the corresponding values of most of the reference proteins. Exceptionally, low dilatational moduli (typically  < 10 mN/m) were obtained for wheat fractions in the continuous and the stepwise compression experiments with no age effect (1–20 min) and almost no relaxation. Surface/interfacial activity and rheological properties observed imply that water-soluble wheat proteins are generally characterized by strong hydrophobicity and more flexible molecular structure than the reference proteins.     

Shear and dilatational relaxation mechanisms of globular and flexible proteins at the hexadecane/water interface

Proteins adsorbed at fluid/fluid interfaces influence many phenomena: food emulsion and foam stability (Murray et al. Langmuir 2002, 18, 9476 and Borbas et al. Colloids Surf., A 2003, 213, 93), two-phase enzyme catalysis (Cascao-Pereira et al. Biotechnol. Bioeng. 2003, 83, 498; 2002, 78, 595), human lung function (Lunkenheimer et al. Colloids Surf., A 1996, 114, 199; Wustneck et al.; and Banerjee et al. 2000, 15, 14), and cell membrane mechanical properties (Mohandas et al. 1994, 23, 787). Time scales important to these phenomena are broad, necessitating an understanding of the dynamics of biological macromolecules at interfaces. We utilize interfacial shear and dilatational deformations to study the rheology of a globular protein, lysozyme, and a disordered protein, beta-casein, at the hexadecane/water interface. Linear viscoelastic properties are measured using small amplitude oscillatory flow, stress relaxation after a sudden dilatational displacement, and shear creep response to probe the rheological response over broad experimental time scales. Our studies of lysozyme and beta-casein reveal that the interfacial dissipation mechanisms are strongly coupled to changes in the protein structure upon and after adsorption. For beta-casein, the interfacial response is fluidlike in shear deformation and is dominated by interfacial viscous dissipation, particularly at low frequencies. Conversely, the dilatational response of beta-casein is dominated by diffusion dissipation at low frequencies and viscous dissipation at higher frequencies (i.e., when the experimental time scale is faster than the characteristic time for diffusion). For lysozyme in shear deformation, the adsorbed protein layer is primarily elastic with only a weak frequency dependence. Similarly, the interfacial dilatational moduli change very little with frequency. In comparison to beta-casein, the frequency response of lysozyme does not change substantially after washing the protein from the bulk solution. Apparently, it is the irreversibly adsorbed fraction that dominates the dynamic rheological response for lysozyme. Using stress relaxation after a sudden dilatational displacement and shear creep response, the characteristic time of relaxation was found to be 1000 s in both modes of deformation. The very long relaxation time for lysozyme likely results from the formation of a glassy interfacial network. This network develops at high interfacial concentrations where the molecules are highly constrained because of conformation changes that prevent desorption.     

Dynamic properties of soy globulin adsorbed films at the air-water interface

In this paper we present surface dilatational properties of soy globulins (beta-conglycinin, glycinin, and reduced glycinin with 10 mM of dithiothreitol (DTT)) adsorbed onto the air-water interface, as a function of adsorption time. The experiments were performed at constant temperature (20 degrees C), pH (8.0), and ionic strength (0.05 M). The surface rheological parameters were measured as a function of protein concentration (ranging from 1 to 1x10(-3)% wt/wt). We found that the surface dilatational modulus, E, increases, and the phase angle, phi, decreases with time, theta, which may be associated with protein adsorption. These phenomena have been related to protein adsorption, unfolding, and/or protein-protein interactions (at long-term adsorption) as a function of protein concentration in solution. From a rheological point of view, the surface viscoelastic characteristics of soy globulin films adsorbed at the air-water interface are practically elastic. The main conclusion is that the dilatational properties of the adsorbed films depend on the molecular structure of the protein.     

Surface rheology of PEO-PPO-PEO triblock copolymers at the air-water interface: comparison of spread and adsorbed layers

The dilatational rheological properties of monolayers of poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide)-type block copolymers at the air-water interface have been investigated by employing an oscillating ring trough method. The properties of adsorbed monolayers were compared to spread layers over a range of surface concentrations. The studied polymers were PEO26-PPO39-PEO26 (P85), PEO103-PPO40-PEO103 (F88), and PEO99-PPO65-PEO99 (F127). Thus, two of the polymers have similar PPO block size and two of them have similar PEO block size, which allows us to draw conclusions about the relationship between molecular structure and surface dilatational rheology. The dilatational properties of adsorbed monolayers were investigated as a function of time and bulk solution concentration. The time dependence was found to be rather complex, reflecting structural changes in the layer. When the dilatational modulus measured at different concentrations was replotted as a function of surface pressure, one unique master curve was obtained for each polymer. It was found that the dilatational behavior of spread (Langmuir) and adsorbed (Gibbs) monolayers of the same polymer is close to identical up to surface concentrations of approximately 0.7 mg/m2. At higher coverage, the properties are qualitatively alike with respect to dilatational modulus, although some differences are noticeable. Relaxation processes take place mainly within the interfacial layers by a redistribution of polymer segments. Several conformational transitions were shown to occur as the area per molecule decreased. PEO desorbs significantly from the interface at segmental areas below 20 A(2), while at higher surface coverage, we propose that segments of PPO are forced to leave the interface to form a mixed sublayer in the aqueous region.     

Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins

Whipped foams (10%, w/v protein, pH 7.0) were prepared from commercially available samples of whey protein isolate (WPI) and egg white protein (EWP), and subsequently compared based on yield stress (τ₀), overrun and drainage stability. Adsorption rates and interfacial rheological measurements at a model air/water interface were quantified via pendant drop tensiometry to better understand foaming differences among the ingredients. The highest τ₀ and resistance to drainage were observed for standard EWP, followed by EWP with added 0.1% (w/w) sodium lauryl sulfate, and then WPI. Addition of 25% (w/w) sucrose increased τ₀ and drainage resistance of the EWP-based ingredients, whereas it decreased τ₀ of WPI foams and minimally affected their drainage rates. These differing sugar effects were reflected in the interfacial rheological measurements, as sucrose addition increased the dilatational elasticity for both EWP-based ingredients, while decreasing this parameter for WPI. Previously observed relationships between τ₀ and interfacial rheology did not hold across the protein types; however, these measurements did effectively differentiate foaming behaviors within EWP-based ingredients and within WPI. Interfacial data was also collected for purified β-lactoglobulin (β-lg) and ovalbumin, the primary proteins of WPI and EWP, respectively. The addition of 25% (w/w) sucrose increased the dilatational elasticity for adsorbed layers of β-lg, while minimally affecting the interfacial rheology of adsorbed ovalbumin, in contrast to the response of WPI and EWP ingredients. These experiments underscore the importance of utilizing the same materials for interfacial measurements as used for foaming experiments, if one is to properly infer interfacial information/mechanisms and relate this information to bulk foaming measurements. The effects of protein concentration and measurement time on interfacial rheology were also considered as they relate to bulk foam properties. This data should be of practical assistance to those designing aerated food products, as it has not been previously reported that sucrose addition improves the foaming characteristics of EWP-based ingredients while negatively affecting the foaming behavior of WPI, as these types of protein isolates are common to the food industry.     

Sorbitan tristearate layers at the air/water interface studied by shear and dilatational interfacial rheology

The shear and dilatational rheology of condensed interfacial layers of the water-insoluble surfactant sorbitan tristearate at the air/water interface is investigated. A new interfacial shear rheometer allows measurements in both stress- and strain-controlled modes, providing comprehensive interfacial rheological information such as the interfacial dynamic shear moduli, the creep response to a stress pulse, the stress relaxation response to a strain step, or steady shear curves. Our experiments show that the interfacial films are both viscoelastic and brittle in nature and subject to fracture at small deformations, as was supported by in-situ Brewster angle microscopy performed during the rheological experiments. Although any large-deformation test is destructive to the sample, it is still possible to study the linear viscoelastic regime if the deformations involved are controlled carefully. Complementary results for the dilatational rheology in area step compression/expansion experiments are reported. The dilatational behavior is predominantly elastic throughout the frequency spectrum measured, whereas the layers exhibit generalized Maxwell behavior in shear mode within a deformation frequency regime as narrow as two decades, indicating the presence of additional relaxation mechanisms in shear as opposed to expansion/compression. If the transient rheological response from stress relaxation experiments is considered, then the data can be described well with a stretched exponential model both in the shear and dilatational deformations.     

Milk protein interfacial layers and the relationship to emulsion stability and rheology

The properties of milk protein-stabilised, oil-in-water emulsions are determined by the structure and surface rheology of the adsorbed layer at the oil-water interface. Analysis of the segment density profiles normal to the surface show differences in the structure between adsorbed layers of disordered casein and globular whey protein. Systematic studies of stability and rheology of model oil-in-water emulsion systems made with milk proteins as sole emulsifiers give insight into the relation between adsorbed layer properties and bulk emulsion stability. Of particular importance are effects of pH, temperature, calcium ions and protein content. Colloidal interactions between adsorbed layers on different surfaces can be inferred from an analysis of dynamic collisions of protein-coated emulsion droplets in shear flow using the colloidal particle scattering technique. The role of competitive adsorption on emulsion properties can be derived from experiments on systems containing mixtures of milk proteins and small-molecule surfactants. Shear-induced destabilisation is especially influenced by the presence of fat crystals in the emulsion droplets. Aggregated gel network properties are dependent on the balance of weak and strong interparticle interactions. In heat-set whey protein emulsion gels, the rheological behaviour is especially sensitive to surfactant type and concentration. Rearrangements of transient caseinate-based emulsion gels can have a profound influence on the quiesent stability behaviour. Computer simulation provides a general link between particle interactions, microstructure and rheological properties.     

Protein adsorption at liquid/liquid interface with low interfacial tension

Adsorption of proteins at the interface of two-liquid systems composed of aqueous ammonium sulfate solution and tert-butanol by phase separation was investigated by drop shape tensiometry. The change of interfacial tension with time and protein concentration as well as upon compression of the adsorbed layer were compared for bovine serum albumin, ovalbumin, β-lactoglobulin, lysozyme, trypsin and horse radish peroxidase. A correlation between the dilatational moduli of various protein films and the partitioning of proteins in the two-liquid system was found, which provides evidence to the role of emulsion stability in protein separation by three-phase partitioning.     

Correlation between mechanical behavior of protein films at the air/water interface and intrinsic stability of protein molecules

The relation between mechanical film properties of various adsorbed protein layers at the air/water interface and intrinsic stability of the corresponding proteins is discussed. Mechanical film properties were determined by surface deformation in shear and dilation. In shear, fracture stress, sigma(f), and fracture strain, gamma(f), were determined, as well as the relaxation behavior after macroscopic fracture. The dilatational measurements were performed in a Langmuir trough equipped with an infra-red reflection absorption spectroscopy (IRRAS) accessory. During compression and relaxation of the surface, the surface pressure, Pi, and adsorbed amount, Gamma (determined from the IRRAS spectra), were determined simultaneously. In addition, IRRAS spectra revealed information on conformational changes in terms of secondary structure. Possible correlations between macroscopic film properties and intrinsic stability of the proteins were determined and discussed in terms of molecular dimensions of single proteins and interfacial protein films. Molecular properties involved the area per protein molecule at Pi approximately 0 mN/m (A(0)), A(0)/M (M = molecular weight) and the maximum slope of the Pi-Gamma curves (dPi/dGamma). The differences observed in mechanical properties and relaxation behavior indicate that the behavior of a protein film subjected to large deformation may vary widely from predominantly viscous (yielding) to more elastic (fracture). This transition is also observed in gradual changes in A(0)/M. It appeared that in general protein layers with high A(0)/M have a high gamma(f) and behave more fluidlike, whereas solidlike behavior is characterized by low A(0)/M and low gamma(f). Additionally, proteins with a low A(0)/M value have a low adaptability in changing their conformation upon adsorption at the air/water interface. Both results support the conclusion that the hardness (internal cohesion) of protein molecules determines predominantly the mechanical behavior of adsorbed protein layers.     

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.     

Rheological parameters of protein interfacial layers as a criterion of the transition from stable emulsions to microemulsions

Proteins are considered as surface active substances. On the basis of experimentally measured rheological parameters of interfacial layers, protein accumulation at an interface between two immiscible liquids, isotherms of interfacial tension, accounting theoretical ideas elaborated for multicomponent systems, the formation of interfacial layers was referred to phase transition. The property of proteins to stabilise emulsions supposedly is connected with the formation of middle phases of lamellar structure. The correlation between elastic properties of interfacial layers and a phase transition of the middle phase upon addition of salts or lipids has been shown. Lipids being added as cosurfactants lead to the transition from lamellar to other structures, which does not provide emulsion stabilisation.     

Interfacial characterization of beta-lactoglobulin networks: displacement by bile salts

The competitive displacement of a model protein (beta-lactoglobulin) by bile salts from air-water and oil-water interfaces is investigated in vitro under model duodenal digestion conditions. The aim is to understand this process so that interfaces can be designed to control lipid digestion thus improving the nutritional impact of foods. Duodenal digestion has been simulated using a simplified biological system and the protein displacement process monitored by interfacial measurements and atomic force microscopy (AFM). First, the properties of beta-lactoglobulin adsorbed layers at the air-water and the olive oil-water interfaces were analyzed by interfacial tension techniques under physiological conditions (pH 7, 0.15 M NaCl, 10 mM CaCl2, 37 degrees C). The protein film had a lower dilatational modulus (hence formed a weaker network) at the olive oil-water interface compared to the air-water interface. Addition of bile salt (BS) severely decreased the dilatational modulus of the adsorbed beta-lactoglobulin film at both the air-water and olive oil-water interfaces. The data suggest that the bile salts penetrate into, weaken, and break up the interfacial beta-lactoglobulin networks. AFM images of the displacement of spread beta-lactoglobulin at the air-water and the olive oil-water interfaces suggest that displacement occurs via an orogenic mechanism and that the bile salts can almost completely displace the intact protein network under duodenal conditions. Although the bile salts are ionic, the ionic strength is sufficiently high to screen the charge allowing surfactant domain nucleation and growth to occur resulting in displacement. The morphology of the protein networks during displacement is different from those found when conventional surfactants were used, suggesting that the molecular structure of the surfactant is important for the displacement process. The studies also suggest that the nature of the oil phase is important in controlling protein unfolding and interaction at the interface. This in turn affects the strength of the protein network and the ability to resist displacement by surfactants.     

Effect of thermal treatment on interfacial properties of beta-lactoglobulin

The changes in the secondary conformation and surface hydrophobicity of beta-lactoglobulin subjected to different thermal treatments were characterized at pH values of 7, 5.5 and 4 using circular dichroism (CD) and hydrophobic dye binding. Heating resulted in a decrease in alpha-helix content with a corresponding increase in random coil at all pH values, this change being more pronounced for small heating times. Heating also resulted in an increase in surface hydrophobicity as a result of partial denaturation, this increase being more pronounced at pH 4. Thermal treatment resulted in a shift of the spread monolayer isotherm at air-water interface to smaller area per molecule due to increased flexibility and more loop formation. Thermal treatment led to an increase in interfacial shear elasticity and viscosity of adsorbed beta-lactoglobulin layer at pH 5.5 and 7. Interfacial shear elasticity, shear viscosity, stability of beta-lactoglobulin stabilized emulsion and average coalescence time of a single droplet at a planar oil-water interface with adsorbed protein layer exhibited a maximum for protein subjected to 15 min heat treatment at pH 7. At pH 5.5, the interfacial shear rheological properties and average single drop coalescence time were maximum for 15 min heat treatment whereas emulsion stability was maximum for 5 min heat treatment. At pH 7, thermal treatment was found to enhance foam stability. Analysis of thin film drainage indicated that interfacial shear rheological properties do not influence thin film drainage.     

Disruption of viscoelastic beta-lactoglobulin surface layers at the air-water interface by nonionic polymeric surfactants

Nonequilibrium interfacial layers formed by competitive adsorption of beta-lactoglobulin and the nonionic triblock copolymer PEO99-PPO65-PEO99 (F127) to the air-water interface were investigated in order to explain the influence of polymeric surfactants on protein film surface rheology and foam stability. Surface dilatational and shear rheological methods, surface tension measurements, dynamic thin-film measurements, diffusion measurements (from fluorescence recovery after photo bleaching), and determinations of foam stability were used as methods. The high surface viscoelasticity, both the shear and dilatational, of the protein films was significantly reduced by coadsorption of polymeric surfactant. The drainage rate of single thin films, in the presence of beta-lactoglobulin, increased with the amount of added F127, but equilibrium F127 films were found to be thicker than beta-lactoglobulin films, even at low concentration of the polymeric surfactant. It is concluded that the effect of the nonionic triblock copolymer on the interfacial rheology of beta-lactoglobulin layers is similar to that of low molecular weight surfactants. They differ however in that F127 increases the thickness of thin liquid films. In addition, the significant destabilizing effect of low molecular weight surfactants on protein foams is not found in the investigated system. This is explained as due to long-range steric forces starting to stabilize the foam films at low concentrations of F127.     

Modulating surface rheology by electrostatic protein/polysaccharide interactions

There is a large interest in mixed protein/polysaccharide layers at air-water and oil-water interfaces because of their ability to stabilize foams and emulsions. Mixed protein/polysaccharide adsorbed layers at air-water interfaces can be prepared either by adsorption of soluble protein/polysaccharide complexes or by sequential adsorption of complexes or polysaccharides to a previously formed protein layer. Even though the final protein and polysaccharide bulk concentrations are the same, the behavior of the adsorbed layers can be very different, depending on the method of preparation. The surface shear modulus of a sequentially formed beta-lactoglobulin/pectin layer can be up to a factor of 6 higher than that of a layer made by simultaneous adsorption. Furthermore, the surface dilatational modulus and surface shear modulus strongly (up to factors of 2 and 7, respectively) depend on the bulk -lactoglobulin/pectin mixing ratio. On the basis of the surface rheological behavior, a mechanistic understanding of how the structure of the adsorbed layers depends on the protein/polysaccharide interaction in bulk solution, mixing ratio, ionic strength, and order of adsorption to the interface (simultaneous or sequential) is derived. Insight into the effect of protein/polysaccharide interactions on the properties of adsorbed layers provides a solid basis to modulate surface rheological behavior.     

In-situ investigation of the adsorption of globular model proteins on stimuli-responsive binary polyelectrolyte brushes

Binary brushes constituted from two incompatible polymers can be used in the form of ultrathin polymeric layers as a versatile tool for surface engineering to tune physicochemical surface characteristics such as wettability, surface charge, chemical composition, and morphology and furthermore to create responsive surface properties. Mixed brushes of oppositely charged weak polyelectrolytes represent a special case of responding surfaces that are sensitive to changes in the pH value of the aqueous environment and therefore represent interesting tools for biosurface engineering. The polyelectrolyte brushes used for this study were composed of two oppositely charged polyelelctrolytes poly(2-vinylpyridine) (P2VP) and poly(acrylic acid) (PAA). The in-situ properties and surface characteristics such as as surface charge, surface tension, and extent of swelling of these brush layers are functions of the pH value of the surrounding aqueous solution. To test the behavior of the mixed polylelctrolyte brushes in contact with biosystems, protein adsorption experiments with globular model proteins were performed at different pH values and salt concentrations (confinement of counterions) of the buffer solutions. The influence of the pH value, buffer salt concentration, and isoelectric points (IEP) of the brush and protein on the adsorbed amount and the interfacial tension during protein adsorption as well as the protein adsorption mechanism postulated in reference to recently developed theories of protein adsorption on polyelectrolyte brushes is discussed. In the salted regime, protein adsorption was found to be similar to the often-described adsorption at hydrophobic surfaces. However, in the osmotic regime the balance of electrostatic repulsion and a strong entropic driving force, "counterion release", was found to be the main influence on protein adsorption.     

Effect of binding of an oligomeric cationic fluorosurfactant on the dilational rheological properties of gelatin adsorbed at the air-water interface

The effect of binding of an oligomeric cationic fluorooxetane surfactant on the interfacial properties of adsorbed gelatin-fluorooxetane complexes has been studied using dynamic surface tension and dilational rheological measurements. Adsorption kinetics of gelatin-fluorooxetane complexes are reminiscent of a mixed (barrier/diffusion limited) process, while the dilational rheological properties of the interface exhibit a strong dependence on surfactant concentration. At low surfactant concentrations, dilational surface moduli as well as phase angles are relatively insensitive to the presence of the fluorooxetane. However, at the critical aggregation concentration of the polymer-surfactant system, there is a sharp increase in the complex modulus. Further increase in the fluorooxetane concentration does not significantly affect the complex modulus. The phase angle, however, does increase with increasing fluorooxetane concentration due to the transport of bound fluorooxetane from the subsurface to the solution-air interface. These results indicate that, at fluorooxetane concentrations exceeding the critical aggregation concentration, the polymer-surfactant complexes adsorb to form cross-linked multilayers at the solution-air interface.     

Transient interfacial tension and dilatational rheology of diffuse polymer-polymer interfaces

We demonstrate the influence of molecular weight and molecular weight asymmetry across an interface on the transient behavior of the interfacial tension. The interfacial tension was measured as a function of time for a range of polymer combinations with a broad range of interfacial properties using a pendant/sessile drop apparatus. The results show that neglecting mutual solubility, assumed to be a reasonable approximation in many cases, very often does not sustain. Instead, a diffuse interface layer develops in time with a corresponding transient interfacial tension. Depending on the specific combination of polymers, the transient interfacial tension is found to increase or decrease with time. The results are interpreted in terms of a recently proposed model [Shi et al., Macromolecules 37, 1591 (2004)], giving relative characteristic diffusion time scales in terms of molecular weight, molecular weight distribution, and viscosities. However, the time scales obtained from this theoretical approach do not give a conclusive trend. Using oscillatory dilatational interfacial experiments the viscoelastic behavior of these diffusive interfaces is demonstrated. The time evolution of the interfacial tension and the dilatational elasticity show the same trend as predicted by the theory of diffuse interfaces, supporting the idea that the polymer combinations under consideration indeed form diffuse interfaces. The dilatational elasticity and the dilatational viscosity show a frequency dependency that is described qualitatively by a simple Fickian diffusion model and quantitatively by a Maxwell model. The characteristic diffusion times provided by the latter show that the systems with thick interfaces (tens of microseconds and more) can be considered as slower diffusive systems compared to the systems with thinner interfaces (a few micrometers in thickness and less) can be considered as fast diffusive systems.     

Interfacial rheology of protein–surfactant mixtures

The distribution of proteins and surfactants at fluid interfaces (air–water and oil–water) is determined by the competitive adsorption between the two types of emulsifiers and by the nature of the protein–surfactant interactions, both at the interface and in the bulk phase, with a pronounced impact on the interfacial rheological properties of these systems. Therefore, the interfacial rheology is of practical importance for food dispersion (emulsion or foam) formulation, texture, and stability. In this review, the existence of protein–surfactant interactions, the mechanical behaviour and/or the composition of emulsifiers at the interface are indirectly determined by interfacial rheology of the mixed films. The effect on the interfacial rheology of protein–surfactant mixed films of the protein, the surfactant, the interface and bulk compositions, the method of formation of the interfacial film, the interactions between film forming components, and the displacement of protein by surfactant have been analysed. The last section tries to understand the role of interfacial rheology of protein–surfactant mixed films on food dispersion formation and stability. The emphasis of the present review is on the interfacial dilatational rheology.