Lipase is an important enzyme, which hydrolyzes fat into fatty acid, diglycerides, monoglycerides and glycerol. The substrate specificity of lipase is often crucial to their application for analytical and industrial purposes. In the present investigation, commercially available porcine pancreas lipase has been immobilized on to plastic brush through covalent bonding using glutaraldehyde. The immobilized lipase retained about 50 % of the initial activity of soluble enzyme and the conjugation yield was 0.04mg/cm2. The optimum pH of lipase enzyme was decreased from pH 7.5 to 6.5 after immobilization; which might be due to the loss of- NH2 groups from the enzyme surface upon conjugation to brush since glutaraldehyde coupling involves the -NH2 groups of enzyme for covalent bonding. The immobilized lipase showed maximum activity at 37°C which is higher than that of the free enzyme (35°C). This indicates an increase in the thermal stability of enzyme after immobilization. The time of incubation for the maximum activity of immobilized enzyme was increased from 20 min to 30 min. The olive oil (substrate) concentration required for the maximum activity or saturation of lipase was decreased from 50 mM to 40mM after immobilization. When immobilized lipase was employed along with the aqueous solution of commercially available detergents (2g/100ml) for the removal of oil stain from cotton clothes, it gave better washing compared to that of detergents alone.