Enantioselective enzymatic hydrolysis of racemic glycidyl butyrate by lipase from Bacillus subtilis with improved catalytic properties

Abstract The lipase from Bacillus subtillus (BSL2), a highly active lipase expressed from newly constructed strain of Bacillus subtilis BSL2, is used in the kinetic resolution of glycidyl butyrate. A high enantiomeric ratio ( E  = 108) was obtained by using 1,4-dioxane as co-solvent (18%, v/v) and decreasing the reaction temperature to 5 °C. The ratio is about 16-fold more than that ( E  = 6.52) obtained in pure buffer solutions (25 °C, pH 7.8). Under the optimum conditions, the remained ( R )-glycidyl butyrate with high enantiopure (ee > 98%) was obtained when the conversion was above 52%.