Lipase-mediated hydrolysis and esterification

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-cyclohexanol in organic solvents and hydrolysis of the racemic cis - and trans -isomers of 2-(4-methoxymethoxybenzyl)-1-cyclohexyl acetates were investigated, and all existing enantiomers of 2-(4-methoxymethoxy-benzyl)-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 enzymemediated 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.