Catalase from bovine liver was covalently immobilized on hydrophilic polyurethane composite (CoFoam). The activity of the enzyme was assayed in the decomposition of H2O2 at pH 7.0 and 25 degrees C. The effects of water-to-prepolymer ratio, the addition of a crosslinking agent, and the utilization of a spacer on enzyme activity were examined. The results of immobilization of the enzyme in a large-scale unit are reported. The advantage of the CoFoam composite lies in the low, drop in pressure in a packed-bed reactor at fairly large flow rates. For example, at flow rates of 10-12 L/min, the drop in pressure is typically 3 kPa. Enzymes immobilized on CoFoam represent a novel use as catalysts in packed-bed reactors owing to the low drop in pressure.