4.6 Review

Protein-polysaccharide interactions: phase-ordering kinetics, thermodynamic and structural aspects

Journal

CURRENT OPINION IN COLLOID & INTERFACE SCIENCE
Volume 8, Issue 4-5, Pages 401-414

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/S1359-0294(03)00093-1

Keywords

protein-polysaccharide interactions; phase separation; complex coacervation; thermodynamic incompatibility; kinetics; structure

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If the most important parameters affecting protein-polysaccharide interactions are now well documented, recent advances concern the structure-building kinetics, thermodynamics and structure of mixtures. As far as complex coacervation is concerned, experimental tools such as light scattering techniques, confocal and electron microscopy and high-sensitivity or isothermal titration calorimetry have brought insights on the molecular structure of the systems and gave access to thermodynamic parameters. These experimental data, combined with intensive numerical simulations on polyelectrolyte systems, are used to build up various models of protein-polysaccharide interaction taking into account both intrinsic and extrinsic parameters. In the case of thermodynamic incompatibility, probing interfaces of phase-separated systems is bringing some insights on the spatial and temporal behavior of such systems. The recent use of w/w emulsion like approach successfully allowed better control of the morphology of segregative phase-separated systems. (C) 2003 Elsevier Ltd. All rights reserved.

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