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, K_{M‐vinyl acetate}, and K_{M‐(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.