Organic reactions catalyzed by immobilized lipases. Part I. Hydrolysis of 2-aryl propionic and 2-aryl butyric esters with immobilized Candida cylindracea lipase

Abstract The alteration of the selectivity of enzymes due to the immobilization methodology is discussed. The hydrolysis of esters of ( R,S ) 2-phenyl propionic and 2-phenyl butyric acids has been used as a reaction test. Lipases from Candida cylindracea immobilized on agarose and alumina have been used as enzymatic derivatives. The stirring speed, [Substrate]/[Enzyme] ratio and pH are the main variables that control the process. An increase in the stirring speed, a diminution of the [Substrate]/[Enzyme] ratio and pH = 7.0 favours the hydrolysis of esters. The effect of the support on the enzymatic activity is discussed. Inorganic supports such as Al 2 O 3 or SiO 2 stabilize the oil/water interface acting in the same way as Na(I) or Ca(II) in the case of native enzyme. Enzymatic derivative on Al 2 O 3 is the most interesting biocatalyst. The effect of the alkyl chain of the ester is not related to the steric hindrance but to the stability of the microemulsion. The butyl ester is the most interesting ester for carrying out the hydrolysis. A model of the ester-active site interaction is proposed to explain the increase observed in the stereoselectivity of the hydrolysis of ( R,S )-ester. High enantioselective hydrolysis of the racemates (yielding S (+) isomer; ee ≤ 98%) can be achieved using the immobilized derivatives.