Lipase‐catalyzed dynamic hydrolytic resolution of (R,S)‐2,2,2‐trifluoroethyl α‐chlorophenyl acetate in water‐saturated isooctane

Abstract The hydrolytic resolution of ( R , S )‐2,2,2‐trifluoroethyl α‐chlorophenylacetate in water‐saturated isooctane containing Lipase MY(I) at 35 °C is selected as the best reaction condition for producing ( R )‐α‐chlorophenyl acetic acid. The kinetic constants, and hence an enantiomeric ratio of 33.6, are estimated and employed for the modeling of time‐course conversions of both substrates by considering product inhibition and enzyme deactivation effects. A successful dynamic kinetic resolution is also achieved, giving the desired ( R )‐α‐chlorophenylacetic acid of 93.0% yield and ee P = 89.5% when 80 mmol dm −3 trioctylamine acting as the racemization catalyst and enzyme activator is initially added. Copyright © 2006 Society of Chemical Industry