IMMOBILIZATION OF TRYPSIN IN POLYCATION-POLYANION COMPLEXES

Trypsin was immobilized in quasi-soluble polyanion-polycation complexe s with retention of the enzyme activity. The activity of the immobiliz ed enzyme strongly depends on pH of the prepared solution, Composition , relative concentrations and molar masses of the polyelectrolytes. Th e highest activity of trypsin (about 93%) was found in the case of the complexes Na-poly(styrenesulfonate)-poly (diallyldimethylammonium chl oride): trypsin = 10:1, prepared at pH 3.0, with high molar mass of th e polyanion (about one million). This method can be proposed for immob ilization of various serine proteases.