Interestingly, the immobilized lipase exhibited enhanced specific activity and stability compared to the soluble enzyme. This improvement was attributed to the hydrophilic microenvironment created by the hydrophilic PVA carrier, which probably absorbs the water produced during the enzymatic esterification, thereby shielding the lipase from adverse effects like enzyme inactivation. The implementation of this catalytically active membrane in a pervaporation reactor resulted in a substantial increase in conversion (i.e. from 60% to 83%) compared to the equilibrium-limited esterification process (conducted without pervaporation). A similar strategy was applied for the synthesis of ethyl lactate (a pharmaceutical-grade excipient ), in which a lipase entrapped in sodium alginate membrane was as enzymatic-pervaporation unit .