Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation
A method is proposed for identification of kinetic parameters when diffusion of substrates is limiting in reactions catalyzed by immobilized enzymes. This method overcomes conventional sequential procedures, which assume immobilization does not affect the conformation of the enzyme and, thus, consid...
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ftccsdartic:oai:HAL:hal-00294425v1 2023-05-15T13:40:44+02:00 Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation Berendsen, Wouter R Lapin, Alexei Reuss, Matthias Institute of Biochemical Engineering (IBVT) University of Stuttgart 2006 https://hal.archives-ouvertes.fr/hal-00294425 en eng HAL CCSD Wiley info:eu-repo/semantics/altIdentifier/pmid/17022668 hal-00294425 https://hal.archives-ouvertes.fr/hal-00294425 PUBMED: 17022668 ISSN: 8756-7938 Biotechnology Progress https://hal.archives-ouvertes.fr/hal-00294425 Biotechnology Progress, Wiley, 2006 [SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT] info:eu-repo/semantics/article Journal articles 2006 ftccsdartic 2020-12-26T14:08:46Z A method is proposed for identification of kinetic parameters when diffusion of substrates is limiting in reactions catalyzed by immobilized enzymes. This method overcomes conventional sequential procedures, which assume immobilization does not affect the conformation of the enzyme and, thus, consider intrinsic and inherent kinetics to be the same. The coupled equations describing intraparticle mass transport are solved simultaneously using numerical methods and are used for direct estimation of kinetic parameters by fitting modeling results to time-course measurements in a stirred tank reactor. While most traditional procedures were based on Michaelis-Menten kinetics, the method presented here is applicable to more complex kinetic mechanisms involving multiple state variables, such as ping-pong bi-bi. The method is applied to the kinetic resolution of (R/S)-1-methoxy-2-propanol with vinyl acetate catalyzed by Candida antarctica lipase B. A mathematical model is developed consisting of irreversible ping-pong bi-bi kinetics, including competitive inhibition of both enantiomers. The kinetic model, which fits to experimental data over a wide range of both substrates (5-95%) and temperatures (5-56 degrees C), is used for simulations to study typical behavior of immobilized enzyme systems. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
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Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
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language |
English |
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[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT] |
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[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT] Berendsen, Wouter R Lapin, Alexei Reuss, Matthias Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
topic_facet |
[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT] |
description |
A method is proposed for identification of kinetic parameters when diffusion of substrates is limiting in reactions catalyzed by immobilized enzymes. This method overcomes conventional sequential procedures, which assume immobilization does not affect the conformation of the enzyme and, thus, consider intrinsic and inherent kinetics to be the same. The coupled equations describing intraparticle mass transport are solved simultaneously using numerical methods and are used for direct estimation of kinetic parameters by fitting modeling results to time-course measurements in a stirred tank reactor. While most traditional procedures were based on Michaelis-Menten kinetics, the method presented here is applicable to more complex kinetic mechanisms involving multiple state variables, such as ping-pong bi-bi. The method is applied to the kinetic resolution of (R/S)-1-methoxy-2-propanol with vinyl acetate catalyzed by Candida antarctica lipase B. A mathematical model is developed consisting of irreversible ping-pong bi-bi kinetics, including competitive inhibition of both enantiomers. The kinetic model, which fits to experimental data over a wide range of both substrates (5-95%) and temperatures (5-56 degrees C), is used for simulations to study typical behavior of immobilized enzyme systems. |
author2 |
Institute of Biochemical Engineering (IBVT) University of Stuttgart |
format |
Article in Journal/Newspaper |
author |
Berendsen, Wouter R Lapin, Alexei Reuss, Matthias |
author_facet |
Berendsen, Wouter R Lapin, Alexei Reuss, Matthias |
author_sort |
Berendsen, Wouter R |
title |
Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
title_short |
Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
title_full |
Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
title_fullStr |
Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
title_full_unstemmed |
Investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
title_sort |
investigations of reaction kinetics for immobilized enzymes - identification of parameters in the presence of diffusion limitation |
publisher |
HAL CCSD |
publishDate |
2006 |
url |
https://hal.archives-ouvertes.fr/hal-00294425 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 8756-7938 Biotechnology Progress https://hal.archives-ouvertes.fr/hal-00294425 Biotechnology Progress, Wiley, 2006 |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/17022668 hal-00294425 https://hal.archives-ouvertes.fr/hal-00294425 PUBMED: 17022668 |
_version_ |
1766139246095106048 |