The surface of polyacrylonitrile hollow fibers was hydrolyzed and covalently bonded with urease via glutaraldehyde. Immobilized urease retained higher relative activity than native urease when storing at various pHs. The stabilities of immobilized urease to pH were higher than those of native enzyme. Immobilized urease retained 86% of initial activity after reusing 15 times at pH 7. After storing for 42d at 4 degrees C and pH 7, the immobilized urease can hydrolyze 15% of initial concentration of urea at pH 7 and 37 degrees C after 4h, while native urease lost almost its catalytic ability. The removal of urea using urease-immobilized dialyzer was demonstrated with in vitro dialysis and showed faster removing rate of urea than a regular dialyzer by 2 times. Furthermore, the improvement in the urea clearance by the urease immobilization to a dialyzer increased with the dialysate velocity.