Microbial lipases (E.C. 3.1.1.3) are the preferred biocatalysts for the synthesis of various fragrance compounds, such as linalool acetate, citronellal acetate, and geranyl acetate, in organic solvents over chemical synthesis. In this study, a purified alkaline extracellular lipase of Pseudomonas aeruginosa MTCC-4713 was efficiently immobilized onto a synthetic poly(AAc-co-HPMA-cl-EGDMA) hydrogel by surface adsorption, and the bound lipase was evaluated for its hydrolytic potential toward various p-nitrophenyl acyl esters, which differed in their C-chain length. Among four series of hydrogels prepared by the variation of the concentrations of monomer and crosslinker, two hydrogels, namely, I-5d and I-20d, that exhibited relatively higher protein (lipase activity) bindings were selected to perform hydrolytic and synthetic (geranyl butyrate) reactions in aqueous and organic solvents. The hydrogel-bound lipase was highly hydrolytic toward p-nitrophenyl ester (C: 16; p-nitrophenyl palmitate). The hydrogel-immobilized lipase was quite stable and retained approximately 57.6% of its original hydrolytic activity after the fifth cycle of reuse under optimized conditions (pH 8.5, 65 degrees C). The hydrogel-immobilized lipase when used to perform the esterification of geraniol/butyric acid (400 : 100 mM) in n-heptane resulted in 98.8 mM geranyl butyrate at 65 degrees C under shaking (120 rpm) after 15 h of reaction time. The addition of a molecular sieve (3 A x 1.5 mm) to the reaction system at a concentration of 100 mg per reaction volume (1 mL) resulted in the complete conversion of the reactants into geranyl butyrate. (C) 2008 Wiley Periodicals, Inc. J Appl Polym Sci 110: 2681-2692, 2008