Mixtures of gum arabic and whey protein (whey protein isolate, WP) form an electrostatic complex in a specific pH range. Three phase boundaries (pH(c), pHphi(1), pHphi(2)) have been determined using an original titration method, newly applied to complex coacervation. It consists of monitoring the turbidity and light scattering intensity under slow acidification in situ with glucono-delta-lactone. Furthermore, the particle size could also be measured in parallel by dynamic light scattering. When the pH is lowered, whey proteins and gum arabic first form soluble complexes. This boundary is designated as pH(c). When the interaction is stronger (at lower pH), phase separation takes place (at pHphi(1)). Finally, at pHphi(2) complexation was suppressed by the charge reduction of the gum arabic. The major constituent of the whey protein preparation used was beta-lactoglobulin (beta-lg), and it was shown that beta-lg was indeed the main complex-forming protein. Moreover, an increase of the ionic strength shifted the pH boundaries to lower pH values, which was summarized in a state diagram. The experimental pH(c) values were compared to a newly developed theory for polyelectrolyte adsorption on heterogeneous surfaces. Finally, the influence of the total biopolymer concentration (0-20% w/w) was represented in a phase diagram. For concentrations below 12%, the results are consistent with the theory on complex coacervation developed by Overbeek and Voorn. However, for concentrations above 12%, phase diagrams surprisingly revealed a "metastable" region delimited by a percolation line. Overall, a strong similarity is seen between the behavior of this system and a colloidal gas-liquid phase separation.

We report on the biosynthesis of 65 kDa A-B-A triblock copolymers consisting of pH-responsive (acidic) silklike blocks and nonresponsive collagenlike blocks, and we show that at pH values where the silklike blocks become uncharged, these polymers form transparent high-modulus gels, that is, 7-15 kPa at 8 g • L -1 , that consist of supramolecular nanotapes with a height of 2.8 nm, a width of ∼14 nm, and an average length of >10 µm. At the concentrations employed, both of these protein triblocks essentially form the same structure, irrespective of block order. The amount of product isolated from the extracellular medium is in the gram per liter range. This high yield makes various applications of this promising class of biocompatible materials possible.

Fat-perception is thought to be related to a complex interplay between fat-associated flavor release and mouth-feel. Friction sensed between the tongue and the palate seems to play a prominent role: in previous work, we have shown that emulsions that are more sensitive toward coalescence give rise to a lowering of the orally perceived and experimentally measured friction and, probably as a consequence, to an enhanced fat-perception. In this paper, we study in detail the factors determining friction of protein-stabilized emulsions using a novel mouth-mimicking tribometer and model surfaces consisting of PDMS modified in various ways (hydrophobicity, deformability, roughness). We show that unlike in many technological applications where lubrication is essentially hydrodynamic, for physiologically relevant loads, the modified PDMS is boundary and/or mixed lubricated, which is like in-mouth lubrication. We find that an increased sensitivity of the emulsions toward coalescence results in a lower friction, confirming previous results obtained with pig's tongue. Surface-induced coalescence (or spreading of emulsion droplets) seems to be very important in this, surface hydrophobicity being the dominant trigger. Viscosity of the dispersed phase does not have such a strong influence on both the measured friction and the oral perceived friction. We do find a strong influence of the presence of bulk proteins and saliva on friction. Finally, hardly any dependence of measured friction on fat content of the emulsion was observed, indicating that only a small amount of fat is needed to alter the friction.

Existing theoretical approaches to polymer adsorption on heterogeneous surfaces are applied to the problems of polyelectrolyte and polyampholyte adsorption on randomly charged surfaces. Also, analytical estimates are developed for the critical pH at which weakly charged polyelectrolytes and globular proteins start forming soluble complexes. Below a critical salt concentration, soluble complexes form “on the wrong side” of the protein isoelectric point due to the heterogeneity of the protein surface charge distribution. The analytical estimates are consistent with experimental data on soluble complexes in mixtures of gum arabic and whey protein isolate.