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Leonard Sagis
Rheology of complex fluid-fluid interfaces: a unified approach based on nonequilibrium thermodynamics

Appl. Rheol. 20:2 (2010) 24380 (8 pages)

Surface rheological properties affect the dynamics of vesicles, nanoparticles, emulsion droplets, foam bubbles, polymer microcapsules, liquid jets, living cells, lung avioli, thin liquid films, and many other multiphase systems. Surface rheology is therefore relevant for a wide range of disciplines in the areas of physics, chemistry, engineering, biology, and medicine. Currently used descriptions of surface rheology have a number of limitations, and in particular are hard to generalize to the large deformation regime. Data are often analyzed with constitutive equations based on straightforward generalizations of models developed for describing bulk phase rheology. Since the latter are in general designed to describe incompressible materials, they are not guaranteed to describe highly compressible interfaces correctly. Here we discuss a unified approach to surface rheology based on nonequilibrium thermodynamics (NET) that provides a consistent set of balance and constitutive equations for the unambiguous determination of surface rheological parameters, both near and far beyond equilibrium. A closer integration of experimental surface rheology and multiphase nonequilibrium thermodynamics would clearly be beneficial for both disciplines.

Cite this publication as follows:
Sagis L: Rheology of complex fluid-fluid interfaces: a unified approach based on nonequilibrium thermodynamics, Appl. Rheol. 20 (2010) 24380.

Christopher Klein, Paul Venema, Leonard Sagis, Dagmar van Dusschoten, Manfred Wilhelm, Hans Wolfgang Spiess, Erik van der Linden, Salman S. Rogers, Athene M. Donald
Rheo-optical Measurements using Fast Fourier Transform and Oversampling

Appl. Rheol. 17:4 (2007) 45210 (7 pages)

Rheo-optics is a method that allows the analysis of optical properties, like birefringence and dichroism under steady and oscillatory shear. It is possible to correlate macroscopic mechanical responses with induced microscopic changes in the material. We describe how this method was improved several fold and implemented on a commercially available setup. However, the here presented ideas are applicable to any rheo-optical setup, based on modulation of the laser light. Additionally it does not need a lock-in amplifier and therefore reduces the costs of the setup.

Cite this publication as follows:
Klein C, Venema P, Sagis L, vanDusschoten D, Wilhelm M, Spiess HW, vanderLinden E, Rogers SS, Donald AM: Rheo-optical Measurements using Fast Fourier Transform and Oversampling, Appl. Rheol. 17 (2007) 45210.

Suzanne Bolder, Hanneke Hendrickx, Leonard Sagis, Erik van der Linden
Ca2+-induced cold-set gelation of whey protein isolate fibrils

Appl. Rheol. 16:5 (2006) 258-264

In this paper we describe the rheological behaviour of Ca2+-induced cold-set gels of whey protein mixtures. Coldset gels are important applications for products with a low thermal stability. In previous work [J. Agric. Food Chem. 54 (2006) 4229], we determined the state diagram for whey protein mixtures that were heated for 10 h at pH 2 at 80°C. Under these conditions, the major whey protein, β-lactoglobulin (β-lg), forms fibrils. When whey protein mixtures are heated at protein concentrations in the liquid solution regime of the state diagram, cold-set gels can be formed by adding Ca2+ ions at pH 7. We studied the rheological behaviour of cold-set gels for various sample compositions for whey protein mixtures. When keeping the total whey protein concentration constant, the elastic modulus, G., for the cold-set gels decreased for increasing α-lactalbumin and bovine serum albumin ratios, because less material (blg fibrils) was available to form a gel network. In the cold-set gels the interactions between the β-lg fibrils induced by the calcium ions are dominant. The β-lg fibrils are forming the cold-set gel network and therefore determine the gel strength. α-Lactalbumin and bovine serum albumin are not incorporated in the stress-bearing structure of the gels.

Cite this publication as follows:
Bolder S, Hendrickx H, Sagis L, vanderLinden E: Ca2+-induced cold-set gelation of whey protein isolate fibrils, Appl. Rheol. 16 (2006) 258.


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