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Kinetics of the L ‐aminoacylase‐catalyzed resolution of N ‐acetyl‐ DL ‐butyrine
Author(s) -
Bódalo Antonio,
Gómez José L,
Gómez Elisa,
Máximo M Fuensanta,
Montiel M Claudia
Publication year - 2002
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.617
Subject(s) - kinetics , chemistry , catalysis , hydrolysis , enzyme , divalent , kinetic energy , batch reactor , reaction rate constant , enzyme kinetics , stereochemistry , nuclear chemistry , organic chemistry , active site , physics , quantum mechanics
The kinetics of the asymmetric hydrolysis of N ‐acetyl‐ DL ‐butyrine catalyzed by L ‐aminoacylase to obtain optically pure L ‐butyrine is described. Some of the constants are determined from the initial reaction rates and others from long‐term experiments in batch reactors by the numerical integration of the reactor design equation and minimization of the kinetic parameters. The methodology described can be applied to the kinetic study of other complex biocatalytic systems. Studies on enzyme activation by adding different divalent metal ions and enzymatic deactivation are also included. © 2002 Society of Chemical Industry