Production of alkyl esters by a phyllosilicate sol-gel immobilized lipase from Pseudomonas cepacia

Lipase PS-30 from Pseudomonas cepacia was immobilized within a phyllosilicate sol-gel matrix, and its esterification activity was compared to that of papain, lipase L-2, and IM60 enzymes. An immobilized lipase PS-30 (IM PS-30) exhibited high esterification activity with ethanol (315.1 U) and butanol (275.0 U) but relatively poor activity with isopropanol (30.7 U) when a molar ratio of 1:3 (tallow: alcohol) was used. On the other hand, IM60 (immobilized lipase from Rhizomucor miehei) showed the highest esterification activity for the normal alcohols (318.2 U), and lipase L-2 had the best esterification activity with isopropanol (319.3 U). For all the lipases studied, alkyl ester production reached equilibrium within the first 2 to 6 hr of alcoholysis reaction. In this study, IM PS-30 immobilized on phyllosilicate sol-gel matrix produced simple alkyl esters from tallow.