The interaction of ovalbumin and of beta-casein with two carboxymethylcellulose samples and with glutamate glucan was studied in aqueous solution at different concentration, pH and ionic strength values. The techniques used were rheometry, optical and chiro-optical measurements and differential scanning calorimetry. In general, glutamate glucan is more effective in interacting with tile protein than carboxymethylcellulose. Because of its disordered conformation, beta-casein is strongly attracted at low pH values to the polysaccharides. When interaction occurs, soluble or insoluble complexes are formed. In the ovalbumin-glutamate glucan and beta-casein-carboxymethyl cellulose systems the polysaccharide hinders rite thermal or Ca(II)-induced aggregation of the protein.