The Reaction Mechanism and Kinetics Data of Racemic Atenolol Kinetic Resolution via Enzymatic Transesterification Process Using Free Pseudomonas fluorescence Lipase

A thorough study on free-enzyme transesterification kinetic resolution of racemic atenolol in a batch system was investigated to gain knowledge for (S)-atenolol kinetics. Analyses of enzyme kinetics using Sigma-Plot 11 Enzyme Kinetics Module on the process are based-on Michaelis-Menten and Lineweaver-Burk plot, which give first-order reaction and ordered-sequential Bi-Bi mechanism, where V-max, KM-vinyl acetate, and KM-(S)-atenolol are 0.80 mM/h, 29.22 mM, and 25.42 mM, respectively. Further analyses on enzyme inhibitions find that both substrates inhibit the process where (S)-atenolol and vinyl acetate develop competitive inhibition and mixed inhibition, respectively. Association of (S)-atenolol with free enzyme to inhibit the enzyme is higher than reaction of active enzyme-substrate complex with vinyl acetate.