Soyabean (Glycine maxvar. Ogden) protease was immobilized on bristles of plastic brush by covalent linkage. The immobilized enzyme retained 34% of the initial activity of free enzyme. When compared to the free enzyme the optimum pH of enzyme, temperatures for maximum activity and saturation concentration of substrate was increased, while time of incubation was decreased after immobilization. The pH optima of the immobilized alkaline protease was shifted towards the alkaline side by 1.2 unit. The immobilized protease exhibited good storage stability and re-usability