Enhancing the enantioselectivity of Candida lipase catalyzed ester hydrolysis via noncovalent enzyme modification

Article abstract of DOI:10.1021/ja00161a052

When the lipase of Candida cylindracea was treated with deoxycholate and organic solvents (ether-ethanol, 1:1), the enzyme apparently unfolded and refolded to generate a more stable conformer, termed lipase A-form. This lipase A-form was found to be considerably more enantioselective than the native enzyme toward the hydrolysis of a variety of (±)-arylpropionic and (±)-phenoxypropionic esters.