Agustian, Joni and Harun@Kamaruddin, Azlina (2016) The Reaction Mechanism and Kinetics Data of Racemic Atenolol Kinetic Resolution via Enzymatic Transesterification Process Using Free Pseudomonas fluorescence Lipase. International Journal of Chemical Kinetics, 48 (5). pp. 253-265. ISSN 1097-4601

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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 Vmax, 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.

Item Type: Article
Subjects: T Technology > TP Chemical technology
Divisions: Fakultas Teknik (FT) > Prodi Teknik Kimia
Depositing User: JONI AGUST
Date Deposited: 04 Oct 2016 01:12
Last Modified: 04 Oct 2016 01:12

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