title: Compositions and phase diagrams for aqueous systems based on proteins and polysaccharides.
abstract: Limited thermodynamic compatibility of proteins with other proteins and proteins with polysaccharides is a fundamental phenomenon that has been demonstrated in more than 200 biopolymer pairs. These systems can undergo a liquid-liquid phase separation resulting in the different macromolecular components primarily concentrated in the different phases. This occurs under conditions (pH values and ionic strengths) inhibiting attraction between nonidentical biopolymers, i.e., the formation of interbiopolymer complexes. Generally, phase separation takes place when the total concentration of the macromolecular components exceeds a certain critical value. The excluded volume of the macromolecules determines both their thermodynamic activity and phase separation threshold. Phase diagrams of biopolymer mixtures and physicochemical features of biphasic systems are considered here. Attention is centered on the limited compatibility of the main classes of proteins and various polysaccharides and on the effects of variables such as pH, ionic strength, temperature and shear forces on the phase state, equilibrium and structure of these two-phase liquid systems. The general nature of the phenomenon of thermodynamic incompatibility of biopolymers accounts for its importance in structure formation in cytoplasm.
authors.affiliation: Nestlé Research Centre, CH-1000 Lausanne 26, Switzerland.
authors.forename: V
authors.initials: V
authors.lastname: Tolstoguzov
mesh_terms: D000818:Animals; D001704:Biopolymers / Q000737:chemistry; D004655:Emulsions / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011134:Polysaccharides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D001704:Biopolymers; D004655:Emulsions; D011134:Polysaccharides; D011506:Proteins; D014867:Water