L4 lipase was immobilized on four kinds of resins by adsorption, involving ion exchange resins and macroporous resins. The influences of carriers and lipase concentrations on the adsorption amounts and activities of immobilized lipases were investigated. Then the L4 Lipase was immobilized on ion exchange resin (DK110) by a method so called adsorption and cross-linking, in which glutaraldehyde is used as the cross-linking agent. The influences of glutaraldehyde concentration and cross-linking methods on the lipase immobilization were also investigated. The results show that macroporous ion exchange resin (DK110) is proved to be the most suitable immobilization supporter; the activity of the immobilized lipase is 292U/g when the lipase concentration is controlled at 50mg/mL. Lipase concentrations and cross-linking methods have a great impact on the immobilization of lipase, either strengthen or weaken. Under the same conditions, lipases immobilized by adsorption and cross-linking treatment exhibit higher activities compared with the lipases immobilized by simple adsorption. Furthermore, lipases immobilized by JL1 exhibit the highest activities, which are 340U/g, and lipases immobilized by JL2 are very much stable in repeated usage, they remain 53% of the initial activity after six cycles. This research might lay the foundation for the further study on bio-diesel based on the immobilized lipases.