Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process

Initial rate and biotransformation studies were applied to refine and validate a mathematical model for enzymatic (R)-phenylacetylcarbinol (PAC) production from pyruvate and benzaldehyde using Candida utilis pyruvate decarboxylase (PDC). The rate of PAC formation was directly proportional to the enz...

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Main Authors: Leksawasdi N., Chow Y.Y.S., Breuer M., Hauer B., Rosche B., Rogers P.L.
Format: Article
Language:English
Published: 2014
Online Access:http://www.scopus.com/inward/record.url?eid=2-s2.0-3042511903&partnerID=40&md5=354b724077eeba8a250c7a0cb2813112
http://cmuir.cmu.ac.th/handle/6653943832/666
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spelling th-cmuir.6653943832-6662014-08-29T08:50:34Z Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process Leksawasdi N. Chow Y.Y.S. Breuer M. Hauer B. Rosche B. Rogers P.L. Initial rate and biotransformation studies were applied to refine and validate a mathematical model for enzymatic (R)-phenylacetylcarbinol (PAC) production from pyruvate and benzaldehyde using Candida utilis pyruvate decarboxylase (PDC). The rate of PAC formation was directly proportional to the enzyme activity level up to 5.0 U ml-1 carboligase. Michaelis-Menten kinetics were determined for the effect of pyruvate concentration on the reaction rate. The effect of benzaldehyde followed the sigmoidal shape of the Monod-Wyman-Changeux (MWC) model. The biotransformation model, which also included a term for PDC inactivation by benzaldehyde, was used to determine the overall rate constants for the formation of PAC, acetaldehyde, and acetoin. These values were determined from data for three batch biotransformations performed over a range of initial concentrations (viz. 50-150 mM benzaldehyde, 60-180 mM pyruvate, 1.1-3.4 U ml-1 enzyme activity). The finalised model was then used to predict a batch biotransformation profile at 120/100 mM initial pyruvate/benzaldehyde (initial enzyme activity 3.0 U ml-1). The simulated kinetics gave acceptable fitting (R2=0.9963) to the time courses of these latter experimental data for substrates pyruvate and benzaldehyde, product PAC, by-products acetaldehyde and acetoin, as well as enzyme activity level. © 2004 Elsevier B.V. All rights reserved. 2014-08-29T08:50:34Z 2014-08-29T08:50:34Z 2004 Article 01681656 10.1016/j.jbiotec.2004.04.001 15219404 JBITD http://www.scopus.com/inward/record.url?eid=2-s2.0-3042511903&partnerID=40&md5=354b724077eeba8a250c7a0cb2813112 http://cmuir.cmu.ac.th/handle/6653943832/666 English
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description Initial rate and biotransformation studies were applied to refine and validate a mathematical model for enzymatic (R)-phenylacetylcarbinol (PAC) production from pyruvate and benzaldehyde using Candida utilis pyruvate decarboxylase (PDC). The rate of PAC formation was directly proportional to the enzyme activity level up to 5.0 U ml-1 carboligase. Michaelis-Menten kinetics were determined for the effect of pyruvate concentration on the reaction rate. The effect of benzaldehyde followed the sigmoidal shape of the Monod-Wyman-Changeux (MWC) model. The biotransformation model, which also included a term for PDC inactivation by benzaldehyde, was used to determine the overall rate constants for the formation of PAC, acetaldehyde, and acetoin. These values were determined from data for three batch biotransformations performed over a range of initial concentrations (viz. 50-150 mM benzaldehyde, 60-180 mM pyruvate, 1.1-3.4 U ml-1 enzyme activity). The finalised model was then used to predict a batch biotransformation profile at 120/100 mM initial pyruvate/benzaldehyde (initial enzyme activity 3.0 U ml-1). The simulated kinetics gave acceptable fitting (R2=0.9963) to the time courses of these latter experimental data for substrates pyruvate and benzaldehyde, product PAC, by-products acetaldehyde and acetoin, as well as enzyme activity level. © 2004 Elsevier B.V. All rights reserved.
format Article
author Leksawasdi N.
Chow Y.Y.S.
Breuer M.
Hauer B.
Rosche B.
Rogers P.L.
spellingShingle Leksawasdi N.
Chow Y.Y.S.
Breuer M.
Hauer B.
Rosche B.
Rogers P.L.
Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process
author_facet Leksawasdi N.
Chow Y.Y.S.
Breuer M.
Hauer B.
Rosche B.
Rogers P.L.
author_sort Leksawasdi N.
title Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process
title_short Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process
title_full Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process
title_fullStr Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process
title_full_unstemmed Kinetic analysis and modelling of enzymatic (R)-phenylacetylcarbinol batch biotransformation process
title_sort kinetic analysis and modelling of enzymatic (r)-phenylacetylcarbinol batch biotransformation process
publishDate 2014
url http://www.scopus.com/inward/record.url?eid=2-s2.0-3042511903&partnerID=40&md5=354b724077eeba8a250c7a0cb2813112
http://cmuir.cmu.ac.th/handle/6653943832/666
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