172658-84-3Relevant academic research and scientific papers
Immobilised Burkholderia cepacia lipase in dry organic solvents and ionic liquids: A comparison
Hara, Piia,Hanefeld, Ulf,Kanerva, Liisa T.
, p. 250 - 256 (2009)
Lipase PS from Burkholderia cepacia in its free, commercial form (BCL-PS), immobilised in a sol-gel (BCLxero) and as a CLEA (BCL-CLEA) was tested in dry organic solvents, ionic liquids and their mixtures. Utilising the acylations of secondary alcohols 1-3 the influence of the enzyme preparation on its activity and enantioselectivity was studied. BCL-CLEA displays higher activity (initial rates) than BCLxero for all substrates in the ILs but loses its activity rapidly. Thus, BCLxero is suitable for kinetic resolution in ILs and in their mixtures with organic solvents. It is not possible to label one IL better than the other without taking the nature of the substrate into account. In neat solvents, the nature of the solvent affects enantioselectivity (E) only when furyl-substituted alcohol 2 serves as a substrate while variation in E is more evident for reactions in solvent mixtures.
Supported ionic liquids in Burkholderia cepacia lipase-catalyzed asymmetric acylation
Hara, Piia,Mikkola, Jyri-Pekka,Murzin, Dmitry Yu.,Kanerva, Liisa T.
scheme or table, p. 129 - 134 (2011/02/24)
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.
