Catalytic properties of commercially available lipases from Candida cylindracea, Rhizopus arrhizus, Aspergillus niger, Penicillium roqueforti, Geotrichum candidum, and porcine pancreas, and those of a crude lipase isolated from G. candidum were studied. Esterification of the racemic cis- and trans-isomers of 2-(4-methoxymethoxybenzyl)-1-cyclohexyl in organic solvents and hydrolysis of the racemic cis- and trans-isomers of 2-(4-methoxymethonybenzyl)-1-cyclohexy acetates were investigated, and all existing enantiomers of 2-(4-methoxymethoxybenzyl)-1-cyclohexanol were prepared, isolated, and characterized by their physicochemical properties. Alcohols 2a and 2b and acetates 4a and 4b were found to be the principle products of enzyme-mediated reactions. The optimum reaction conditions for the enzyme-mediated hydrolysis of 1a and 1b and for the enzyme-mediated esterification of 3a or 3b were found, when G, candidum was used. We also compare the advantages and disadvantages of employing the appropriate enzymes.