Immobilized lipase YlLip2-catalyzed resolution of (±)α-phenylethyl amine in a medium with organic cosolvent

In this paper, we studied the enantioselective aminolysis activity of an immobilized extracellular lipase LIP2 (YlLip2) from Yarrowia lipolytica by catalyzing enantioselective acylation of (±)α-phenylethyl amine with acetic ester in a medium containing cosolvent. The reaction parameters including cosolvent concentration, reaction temperature, amount of the immobilized lipase and the reaction time were optimized. When the reaction was carried out in hexane with the presence of 3% DMSO and six pieces of immobilized lipase at 45 °C for 6 days, the enantiomeric excess of product (e.e.p) markedly increased from 0.35 (in neat hexane) to 0.96 and the enantiomeric ratio (E) improved from 2.5 (in neat hexane) to 190. The immobilized lipase could be reused at least five consecutive batches at high E (≈190).