| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 70880 | Journal of Molecular Catalysis B: Enzymatic | 2010 | 6 Pages |
Lipase PS from Burkholderia cepacia was successfully immobilized on Kynol™ ACC 507-15 active carbon cloth with and without ionic liquids as SILE catalysts. Activity, enantioselectivity and reuse of the catalysts were evaluated in the acylation of 1-phenylethanol with vinyl acetate in toluene and in hexane over the temperature range 25–60 °C. The presence of [EMIM][NTf2] clearly stabilized the enzyme against inactivation and preserved enantioselectivity in reuse in a process which is affected by the nature of the IL, solvent and substrate structure.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideResearch highlights▶ The preparation of support/ionic liquid/lipase (SILE) catalysts is described. ▶ [EMIM][NTf2] on Kynol™ ACC 507-15 active carbon cloth stabilizes Burkholderia cepacia lipase (lipase PS) against reuse and temperature. ▶ ACC 507-15/[EMIM][NTf2]/lipase PS works enantioselectively on the acylation of secondary alcohols.
