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The Reaction Mechanism and Kinetics Data of Racemic Atenolol Kinetic Resolution via Enzymatic Transesterification Process Using Free Pseudomonas fluorescence Lipase
Author(s) -
Agustian Joni,
Harun Kamaruddin Azlina
Publication year - 2016
Publication title -
international journal of chemical kinetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.341
H-Index - 68
eISSN - 1097-4601
pISSN - 0538-8066
DOI - 10.1002/kin.20986
Subject(s) - chemistry , transesterification , atenolol , kinetics , lipase , vinyl acetate , kinetic resolution , substrate (aquarium) , enzyme , enzyme kinetics , stereochemistry , organic chemistry , chromatography , catalysis , enantioselective synthesis , active site , medicine , physics , polymer , oceanography , quantum mechanics , geology , blood pressure , copolymer , radiology
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.