144315-92-4Relevant articles and documents
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.
Lipase Catalysis in the Optical Resolution of 2-Amino-1-phenylethanol Derivatives
Kanerva, Liisa T.,Rahiala, Katri,Vaenttinen, Eero
, p. 1759 - 1762 (2007/10/02)
The lipase PS- and CCL-catalysed resolution of unsubstituted and N-alkyl substituted 2-amino-1-phenylethanols with 2,2,2-trifluoroethyl butyrate or with butyric anhydride and those of the corresponding diacylated 1,2-amino alcohols with 1-alcohols in organic media have been studied.The enzymatic deacylation of diacylated 2-amino-1-phenylethanol stops at approximately 50percent conversion yielding the two enantiomers with an e.e. of the order of 100percent.Enantioselectivity in the case of N-alkyl substituted compounds is only somewhat lower.Also the enzymatic acylation of 2-amino-1-phenylethanol shows high enantioselectivity when the protection of the NH2 group with CO2Et or CO2CH2Ph has been used.However, the direct acylation of 2-amino-1-phenylethanol or of its N-alkyl substituted derivatives are slow, the reactions stop before 40percent conversion and nonenzymatic aminolysis is usually significant.
