144315-91-3Relevant articles and documents
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.