Complex coacervation of proteins and anionic polysaccharides

Coacervation of proteins and anionic polysaccharides is both of practical and theoretical interest. From a large body of literature, it seems that the phase separation is mainly entropically driven, and may most probably be attributed to the delocalisation of the counter ions of the protein and the polysaccharide. The protein and polysaccharide appear to form complexes in solution, which can be viewed as new colloidal entities. These complex particles are neutral and exhibit an attractive interaction, which leads to a phase separation of the gas–liquid type in which a (very) dilute colloidal phase coexists with a very concentrated colloidal phase. In the case of strong poly-acids, usually, a precipitate is formed rather than a liquid coacervate phase. The structure of the concentrated polymer phase seems to resemble a continuous polymer phase in which the protein can diffuse around, as well as the individual polysaccharide molecules. Time scales of diffusion vary from milliseconds to days depending on the strength of the interaction. From a rheological point of view, the concentrated phase is much more viscous than elastic and the rheology resembles the behaviour of a (viscous) concentrated particle dispersion. Theoretical developments are limited probably due to the difficulty to describe the (correlated) charge distribution in the system. There is a strong interest in coacervates for the use of encapsulation. For the same reason, much attention is given to replacing the traditional gelatin by milk and plant proteins.