Investigation of synthetic lipase and its use in transesterification reactions

Abstract

A novel synthetic polymer selective for p-nitrophenylpalmitate was synthesized by molecular imprinting technique. We have combined the principle of molecular imprinting with the ability of histidine, glutamic acid and serine to form a catalytic cavity that can promote the catalytic degradation of p-nitrophenyl palmitate. For the creation of such catalytic sites we first synthesized appropriate monomers and used p-nitrophenyl palmitate as a template to synthesize the imprinted polymers and the binding characteristics of the polymers were evaluated. The optimum pH was determined by evaluating different pH values and the hydrolytic activity of synthetic lipase was evaluated in the framework of Micheaelis-Menten kinetics. In addition, the values of maximal rate: Vm (0.68 mM/min) and Michaelis-Menten constant, Km (1.4 x 10(-2) mM) were obtained from Lineweaver-Burk plots for the imprinted polymeric catalyst