COMPARISON OF THE ENZYMATIC-ACTIVITY OF COMMERCIAL AND SEMIPURIFIED LIPASE OF CANDIDA-CYLINDRACEA IN THE HYDROLYSIS OF THE ESTERS OF (R,S) 2-ARYL PROPIONIC ACIDS

a semipurified lipase of Candida cylindradea (LS) -easily obtained fro m commercial crude lipase (LC)- is used in the enantioselective hydrol ysis of (R,S) 2-arylpropionates. The semipurification treatment dimini shes the lipase activity more than the esterase activity. The addition of lactose (24 h) increases both activities. LS is more active than L C -at the same amount of protein- in the hydrolysis of (R,S) 2-aryl pr opionates. This semipurification showed a remarkable improvement in yi eld in the enantioespecific hydrolysis of these esters.