The Reaction Mechanism and Kinetics Data of Racemic Atenolol Kinetic Resolution via Enzymatic Transesterification Process Using Free Pseudomonas fluorescence Lipase JONI AGUSTIAN, 1 AZLINA HARUN KAMARUDDIN 2 1 Department of Chemical Engineering, Universitas Lampung, Bandar Lampung, 35145, Lampung, Indonesia 2 School of Chemical Engineering, Universiti Sains Malaysia, 14300 Nibong Tebal, Seberang Perai Selatan, Penang, Malaysia Received 18 August 2015; revised 16 December 2015; accepted 8 February 2016 DOI 10.1002/kin.20986 Published online 15 March 2016 in Wiley Online Library (wileyonlinelibrary.com). ABSTRACT: 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 competi- tive 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. C  2016 Wiley Periodicals, Inc. Int J Chem Kinet 48: 253–265, 2016 Correspondence to: Azlina Harun Kamaruddin; e-mail: chazlina@usm.my. C  2016 Wiley Periodicals, Inc. INTRODUCTION Atenolol chemically known as 2-{4-[2-hydroxy-3- (propan-2-ylamino)propoxy]phenyl} acetamide is a