Kinetic resolution of 2-octanol by esterification with mycelium-bound lipase from Rhizopus chinensis

The application of mycelium-bound lipase from Rhizopus chinensis CCTCC M201021 (RCL) to the kinetic resolution of 2-octanol by esterification in nonaqueous media was studied using octanoic acid and isooctane as the acyl donor and solvent, respectively. Water activity did not obviously affect the enantioselectivity of lipase but could notablely improve the initial velocity of the reaction. At the same conversion, the initial velocity of production of (R)-ester was increased by 7.3 times by the addition of 3A molecular sieves to reduce the water content of the system. When the substrate concentration was increased to 0.230 mol/L, ( R)-ester was obtained with 44.4% conversion and 94.7% enantiomeric excess after reaction for 40 h. Compared with three commercial lipases, RCL showed not only high enantioselectivity (E = 103.1) but also more satisfied initial velocity and conversion.