A new method to determine optimum temperature and activation energies for enzymatic reactions

A new method for determination of the optimum temperature and activation energies based on an idea of the average rate of enzymatic reaction has been developed. A mathematical model describing the effect of temperature on a dimensionless activity for enzyme deactivation following the first-order kin...

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Detalles Bibliográficos
Autores principales: Wojcik, M., Miłek, J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2016
Materias:
Short Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945675/
https://www.ncbi.nlm.nih.gov/pubmed/27066801
http://dx.doi.org/10.1007/s00449-016-1596-7
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author Wojcik, M.
Miłek, J.
author_facet Wojcik, M.
Miłek, J.
author_sort Wojcik, M.
collection PubMed
description A new method for determination of the optimum temperature and activation energies based on an idea of the average rate of enzymatic reaction has been developed. A mathematical model describing the effect of temperature on a dimensionless activity for enzyme deactivation following the first-order kinetics has been derived. The necessary condition for existence of the function extreme of the optimal temperature has been applied in the model. The developed method has been verified using the experimental data for inulinase from Kluyveromyces marxianus.
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spelling pubmed-49456752016-07-26 A new method to determine optimum temperature and activation energies for enzymatic reactions Wojcik, M. Miłek, J. Bioprocess Biosyst Eng Short Communication A new method for determination of the optimum temperature and activation energies based on an idea of the average rate of enzymatic reaction has been developed. A mathematical model describing the effect of temperature on a dimensionless activity for enzyme deactivation following the first-order kinetics has been derived. The necessary condition for existence of the function extreme of the optimal temperature has been applied in the model. The developed method has been verified using the experimental data for inulinase from Kluyveromyces marxianus. Springer Berlin Heidelberg 2016-04-11 2016 /pmc/articles/PMC4945675/ /pubmed/27066801 http://dx.doi.org/10.1007/s00449-016-1596-7 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Short Communication
Wojcik, M.
Miłek, J.
A new method to determine optimum temperature and activation energies for enzymatic reactions
title A new method to determine optimum temperature and activation energies for enzymatic reactions
title_full A new method to determine optimum temperature and activation energies for enzymatic reactions
title_fullStr A new method to determine optimum temperature and activation energies for enzymatic reactions
title_full_unstemmed A new method to determine optimum temperature and activation energies for enzymatic reactions
title_short A new method to determine optimum temperature and activation energies for enzymatic reactions
title_sort new method to determine optimum temperature and activation energies for enzymatic reactions
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945675/
https://www.ncbi.nlm.nih.gov/pubmed/27066801
http://dx.doi.org/10.1007/s00449-016-1596-7
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