In its natural environment lipases catalyze the hydrolysis of triglycerides. However, under appropriate experimental conditions, these enzymes are very active and catalyze the esterification of fatty acids, alcoholysis and transesterification reactions. The versatility of these enzymes leads to several applications in food industry, processing of oils, biocatalytic resolution of pharmaceuticals, among others. The possibility of enzyme recovery and re-usability is an attractive for industrial applications.  Immobilization of lipase on solids supports using different methods is a strategy to insolubilize enzyme and to improve its operational stability. In order to reduce costs associated with immobilization, chitosan, an abundant and cheap raw material, available in Ceará Sate, Brazil, due to the long extent of its seacoast and the high activity of its seafood industry, was used to immobilize Candida antarctica type B lipase by covalent coupling method. For this purpose, prior to enzyme immobilization, the method of support activation was investigated and three different activating agents were tested: glycidol, glutaraldehyde and ethylenediamine (EDA). Best results of enzymatic activity of the immobilized enzyme (422,44 ± 50,4 U/g) and operational stability were obtained when chitosan was activated with 72% of glycidol followed by treatment with ethylenediamine and 5% of glutaraldehyde. Lipase immobilized on chitosan by this activation strategy was 10-fold more thermal stable than the soluble enzyme at 60 °C. This stabilization may have been caused by multipoint covalent attachment since an increase on thermal and alkaline stabilities with increasing immobilization time was observed.