Enzymatic Resolution of Racemic Ibuprofen Esters Using Immobilized Candida Antarctica Lipase in Organic Media

Abstract

The production of optically pure pharmaceutical intermediates has become increasingly important in modern drug manufacturing due to the distinct biological activity and therapeutic performance of enantiomerically enriched compounds. The present study investigates the enzymatic resolution of racemic ibuprofen esters using immobilized Candida antarctica lipase in organic media under controlled reaction conditions. The research focuses on evaluating enantioselectivity, conversion efficiency, catalytic stability, and process optimization associated with immobilized biocatalytic systems. Experimental analysis was conducted to examine the influence of solvent type, reaction temperature, substrate concentration, enzyme loading, water activity, and reaction time on ester hydrolysis performance and enantiomeric excess of the produced ibuprofen. Results demonstrate that immobilized Candida antarctica lipase effectively catalyzes the selective transformation of racemic ibuprofen esters, resulting in enhanced enantiomeric purity and improved product recovery. The study further reveals that optimized organic reaction media and controlled operational conditions significantly improve enzyme activity and stereoselectivity while minimizing undesired side reactions. Immobilization of the lipase contributed to improved operational stability, reusability, and resistance to solvent-induced deactivation during repeated reaction cycles. Comparative assessment with conventional chemical resolution methods confirms the advantages of enzymatic processes, including milder operating conditions, reduced environmental impact, and superior stereochemical selectivity. In addition, the process demonstrates potential for scalable pharmaceutical manufacturing applications requiring high-purity chiral compounds.