Enantioselective enzymatic hydrolysis of racemic glycidyl esters by using immobilized porcine pancreas lipase with improved catalytic properties

The crude porcine pancreas lipase (PPL) extract is a mixture of several pro teins (mainly lipases and esterases). In order to develop enzymatic catalys ts with good catalytic properties for hydrolytic enantioselective reactions in aqueous homogeneous medium, we studied the immobilization of the differ ent enzymes contained in the crude PPL extracts by selective sequential ads orption on hydrophobic supports bearing octyl, octadecyl and phenyl groups. Some minor proteins were selectively adsorbed on octyl and octadecyl suppo rts while the most abundant lipase was adsorbed on the support bearing phen yl groups. The enantioselectivity of the different lipase derivatives were tested considering the hydrolysis of esters of 1,2-epoxi-1-propanol (glycid ol). The most abundant lipase contained in the commercial crude PPL extract resulted almost inactive while some lipases contained in low concentration s displayed high activities and enantioselectivities. The most interesting results were obtained with a 28-kDa protein selectively adsorbed on octyl-a garose. With this enzyme derivative, the residual butyric ester of glycidol was recovered with 96% enantiomeric excess at 55% conversion. (C) 2001 Els evier Science B.V. All rights reserved.