The effect of the interaction in the solid state of ovalbumin and of beta-casein with carboxymethylcellulose and with glutamate glucan was studied. The techniques used were rheometry, optical and chiro-optical measurements and differential scanning calorimetry These techniques were applied to the aqueous solutions which were obtained from the freeze-dried polysaccharide, protein and polysaccharide-protein mixed systems after storage of the lyophilizates at 60 degrees C. The thermal treatment at 60 degrees C of the freeze-dried proteins affected the behaviour of their aqueous solutions. The differences between the thermally treated and the native protein solutions were significantly reduced by rite presence of both the carboxymethylcellulose and the glutamate glucan in the lyophilizates. After thermal treatment prolonged over 3 days, glutamate glucan gave a gel whose consistency was increased more by the presence of beta-casein than by the presence of ovalbumin. Tile viscosity of carboxymethylcellulose increased after the interaction with beta-casein. The increase was smaller than that observed in solutions obtained by the simple mixing of the polymers, without arty previous thermal treatment.