Emulsion Drops with Complex Interfaces: Globular Versus Flexible Proteins

Erni, Philipp; Windhab, Erich J.; Fischer, Peter

doi:10.1002/mame.201000290

Cited by 62 publications

(41 citation statements)

References 91 publications

(170 reference statements)

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“…The overarching finding is that there is a strong link between interfacial microstructure and its nonlinear response to applied deformations [25,[38][39][40][41][42][43][44]. Consequently, the strength of the interfacial film to resist rupture, which essentially depends on macromolecular interactions and conformational changes, needs to be considered [25,45].…”

Section: The Role Of Proteinmentioning

confidence: 99%

Polysaccharides at fluid interfaces of food systems

Kontogiorgos

2019

Advances in Colloid and Interface Science

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Fabrication of next generation polysaccharides with interfacial properties is driven by the need to create high performance surfactants that operate at extreme environments, as for example in complex food formulations or in the gastrointestinal tract. The present review examines the behaviour of polysaccharides at fluid food interfaces focusing on their performance in the absence of any other intentionally added interfacially active components. Relevant theoretical principles of colloidal stabilisation using concepts that have been developed for synthetic polymers at interfaces are firstly introduced. The role of protein that in most cases is present in polysaccharide preparations either as contaminant or as integral part of the structure is also discussed. Critical assessment of the literature reveals that although protein may contribute to emulsion formation mostly as an anchor for polysaccharides to attach, it is not the determinant factor for the long-term emulsion stability, irrespectively of polysaccharide structure. Interfacial performance of key polysaccharides is also assessed revealing shared characteristics in their modes of adsorption. Conformation of polysaccharides, as affected by the composition of the aqueous solvent needs to be closely controlled, as it seems to be the underlying fundamental cause of stabilisation events and appears to be more important than the constituent polysaccharide sugar-monomers. Finally, polysaccharide adsorption is better understood by regarding them as copolymers, as this approach may assist to better control their properties with the aim to create the next generation biosurfactants.

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Section: The Role Of Proteinmentioning

confidence: 99%

Polysaccharides at fluid interfaces of food systems

Kontogiorgos

2019

Advances in Colloid and Interface Science

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“…Bovine serum albumin has been shown to form soft gel interfaces in both shear and dilatation with moduli magnitudes on the order of 10 −3 to 10 −1 Pa m [4][5][6][7][8][9][10][11][12][13]. Bovine serum albumin adsorbed to interfaces exhibits viscoelastic properties at bulk concentrations as low as 10 mg/ml; magnitudes of interfacial shear viscosity and moduli do not change significantly as a function of bulk concentration.…”

Section: Introductionmentioning

confidence: 99%

Effect of interfacial viscoelasticity on the bulk linear viscoelastic moduli of globular protein solutions

2014

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The role of interfacial rheology on the bulk linear viscoelastic moduli of low concentration bovine albumin solutions is probed. Previously reported soft gel properties of these systems were attributed to either protein aggregation or organization within the bulk. Instead, these behaviors are shown to be attributable to the measurement error caused by interfacial rheology due to adsorption of bovine serum albumin to the air and water interface. Even at low bulk concentrations, fast interfacial adsorption results in erroneous measurements. When these effects are removed, the solutions are viscous dominated with a dynamic viscosity slightly larger than water.

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“…The European Physical Journal Special Topics are extensively presented by Sagis [10] and Erni [11]. Protein stabilized interfaces are especially interesting due to the build up of viscoelastic layers [12][13][14][15]. Most of the protein fraction is irreversibly adsorbed at the interface, leading to formation of wrinkles at the water-oil interface after shape oscillation and generally form multilayer films rendering the use of interfacial rheological models into an extremely challenging issue [6,10,16].…”

mentioning

confidence: 99%

“…So, the pendant drop method, originally developed for surfactants, does not seem suitable for proteins, as they differentiate greatly from surfactants and form complex structures at the interface, leading to a gel like formation i.e. rendering the system from surface tension to surface elasticity governed [1,11,12,15]. To highlight this shortcoming, β-lactoglobulin fibrils at pH 2 were investigated on their kinetic adsorption and dynamic behavior at the wateroil and water-air interface.…”

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confidence: 99%

Protein adsorption and interfacial rheology interfering in dilatational experiment

Rühs

Scheuble

Windhab

et al. 2013

Eur. Phys. J. Spec. Top.

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The static and dilatational response of β-lactoglobulin fibrils and native β-lactoglobulin (monomers) at water-air and water-oil interfaces (pH 2) was measured using the pendant drop method. The resulting adsorption behavior and viscoelasticity is dependent of concentration and adsorption time. The interfacial pressure of the β-lactoglobulin fibrils obtained in static measurements was 16-18 mN/m (against air) and 7 mN/m (against oil) for all concentrations. With higher concentrations, faster adsorption kinetics and slightly higher interfacial and surface pressure is achieved but did not lead to higher viscoelastic moduli. The transient saturation of the interface is similar for both the fibril solution and the monomers, however the fibril solution forms a strong viscoelastic network. To evaluate the superimposed adsorption behavior and rheological properties, the formed interfacial layer was subjected to dilatational experiments, which were performed by oscillating the surface area of the drop in sinusoidal and sawtooth (diagonal) deformation manner. The sinusoidal oscillations (time depended area deformation rate) result in a complex interfacial tension behavior against air and oil interfaces and show remarkable differences during compression and expansion as emphasized by Lissajous figures. For diagonal (constant area deformation rate) experiments, a slight bending of the interfacial tension response was observed at low frequencies emphasizing the influence of protein adsorption during rheological measurements.

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Emulsion Drops with Complex Interfaces: Globular Versus Flexible Proteins

Cited by 62 publications

References 91 publications

Polysaccharides at fluid interfaces of food systems

Polysaccharides at fluid interfaces of food systems

Effect of interfacial viscoelasticity on the bulk linear viscoelastic moduli of globular protein solutions

Protein adsorption and interfacial rheology interfering in dilatational experiment

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