High throughput covalent urease immobilization was performed through the amide bond formation between the urease and the amino-functional MNPs. The enzyme's performances, including shelf-life, reusability, enzymatic kinetics, and the enzyme relative activity in organic media was improved. At optimal conditions, the immobilization efficiency was calculated about 95.0% with keeping 94.7% of the urease initial specific activity. The optimal pH for maximum activity of the free and immobilized urease was calculated as 7.0 at 37.0 degrees C and 8.0 at 60.0 degrees C, respectively. The kinetics studies showed the K-m of 26.0 mM and 8.0 mM and the V-max of 5.31 mu mol mg(-1 )min(-1 )and 3.93 mu mol mg(-1) min(-1 )for the free and immobilized urease, respectively. The ratio K-cat/K(m )as a measure of catalytic efficiency and enzyme specificity was calculated as 0.09 mg(-1 )min(-1) and 0.22 mg(-1) min(-1 )for the free and immobilized urease, respectively, indicating an improvement in the enzymatic kinetics. The shelf-life and operational studies of immobilized urease indicated that approximately 97.7% and 88.5% of its initial activity was retained after 40 days and 17 operational cycles, respectively. The immobilized urease was utilized to urea removal from water samples with an efficiency between 91.5-95.0%.