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

Article abstract of DOI:10.1016/S0040-4020(01)89267-X

A semipurified lipase of Candida cylindradea (LS) - easily obtained from commercial crude lipase (LC) - is used in the enantioselective hydrolysis of (R,S) 2-arylpropionates. The semipurification treatment diminishes the lipase activity more than the esterase activity. The addition of lactose (24 h) increases both activities. LS is more active than LC - at the same amount of protein - in the hydrolysis of (R,S) 2-aryl propionates. This semipurification showed a remarkable improvement in yield in the enantioespecific hydrolysis of these esters.