In bioprocesses lipases are typically used in immobilized form, irrespective of type of reaction systems, to ensure an even distribution of catalysts in water restricted media and/or to facilitate separation and reuse. In these studies we report on the selection of appropriate enzyme-carrier preparation for hydrolysis reaction in aqueous and biphasic systems and transesterification in organic solvent. For this Candida rugosa lipase was bound by adsorption or covalent attachment onto various carriers to give 24 preparations. Selection of proper preparation was based on reactivity, thermal stability (4 h at 60°C), possibility of drying and operational stability in 17-23 successive batch processes of 4-nitrophenyl palmitate hydrolysis in water. Activity of preparations varied from 20 to 5100 U∙mL(-1) but the most stable preparations were those of moderate activity: bound by adsorption or covalent attachment to NH₂-Kieselgel or acrylic carrier (retained activity over 90%). Selected preparations were used for hydrolysis of ethyl (1-butyryloxyethyl)-phenylphosphinate in biphasic system, and, after drying, in ethyl (1-hydroxyethyl)-phenyl-phosphinate transesterification. In this study operational stability was the principal criterion of selection. In water system, lipase covalently bound to NH₂-Kieselgel was the best - preserved 50% of initial activity in consecutive batch processes. In biphasic system and lipase covalently bound to acrylic and NH₂-Kieselgel the values were 90 or 77%, respectively, whereas in organic solvent, when lipase was immobilized on NH₂-Kieselgel by adsorption, it was 50%. Thus, NH₂-Kieselgel appears to be an universal matrix for investigated lipase immobilization and can be used in all reaction systems.