HYDROLYSIS OF (R,S)2-ARYL PROPIONIC ESTERS BY PURE LIPASE-B FROM CANDIDA-CYLINDRACEA

Purified lipase B from Candida cylindracea (LB) has been obtained in large amounts. LB exhibits greater esterase and lipase activities than commercial lipase. The presence of divalent and/or monovalent cations increases the lipase activity with respect to the absence of external cations, using olive oil as substrate. LB is more active than commercial and semipurified lipases in the hydrolysis of (R,S)-2-arylpropionic ethyl esters. The presence of Na(I) or Ca(II) diminishes the enzymatic activity in the hydrolysis of these esters compared to that obtained in the absence of the external ions. LB is stereospecific in the hydrolysis of S(+)2-arylpropionate.