Efficient purification-immobilization of an organic solvent-tolerant lipase from Staphylococcus warneri EX17 on porous styrene-divinylbenzene beads

Lipase from Staphylococcus warneri EX17 (SWL) was purified and immobilized via interfacial adsorption using the hydrophobic supports Octyl-sepharose, Immobead 150, and MCI GEL CHP20P. The purity of the obtained immobilized biocatalysts, Octyl-SWL, Immobead-SWL, and MCI-SWL, was evaluated by SDS-PAGE and their thermal and solvent stability were tested. Results indicated that the intensity of the interaction between the lipase and the support surface interferes with the properties of the immobilized enzyme. The immobilized preparations Octyl-SWL and MCI-SWL were stable in the presence of 50% butanol, ethanol, n-hexane, isopropanol, and methanol. Containing only 8 mg g−1 of enzyme in relation to the support, Octyl-SWL and MCI-SWL preparations catalyzed the synthesis of ethyl butyrate in a 24 h reaction, showing conversions of 28% (51.3 mmol mg−1), and 35.6% (65.2 mmol mg−1), respectively. These results indicate that Octyl-SWL and MCI-SWL preparations present very high specific activities.