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Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results
In this paper, the efficiency of the carbonic anhydrase (CA) enzyme in accelerating the hydration of CO(2) is evaluated using a measurement system which consists of a vessel in which a gaseous flow of mixtures of nitrogen and CO(2) is bubbled into water or water solutions containing a known quantity...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7831361/ https://www.ncbi.nlm.nih.gov/pubmed/33430654 http://dx.doi.org/10.1080/14756366.2020.1864631 |
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author | Parri, Lorenzo Fort, Ada Lo Grasso, Anna Mugnaini, Marco Vignoli, Valerio Capasso, Clemente Del Prete, Sonia Romanelli, Maria Novella Supuran, Claudiu T. |
author_facet | Parri, Lorenzo Fort, Ada Lo Grasso, Anna Mugnaini, Marco Vignoli, Valerio Capasso, Clemente Del Prete, Sonia Romanelli, Maria Novella Supuran, Claudiu T. |
author_sort | Parri, Lorenzo |
collection | PubMed |
description | In this paper, the efficiency of the carbonic anhydrase (CA) enzyme in accelerating the hydration of CO(2) is evaluated using a measurement system which consists of a vessel in which a gaseous flow of mixtures of nitrogen and CO(2) is bubbled into water or water solutions containing a known quantity of CA enzyme. The pH value of the solution and the CO(2) concentration at the measurement system gas exhaust are continuously monitored. The measured CO(2) level allows for assessing the quantity of CO(2), which, subtracted from the gaseous phase, is dissolved into the liquid phase and/or hydrated to bicarbonate. The measurement procedure consists of inducing a transient and observing and modelling the different kinetics involved in the steady-state recovery with and without CA. The main contribution of this work is exploiting dynamical system theory and chemical kinetics modelling for interpreting measurement results for characterising the activity of CA enzymes. The data for model fitting are obtained from a standard bioreactor, in principle equal to standard two-phase bioreactors described in the literature, in which two different techniques can be used to move the process itself away from the steady-state, inducing transients. |
format | Online Article Text |
id | pubmed-7831361 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-78313612021-02-02 Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results Parri, Lorenzo Fort, Ada Lo Grasso, Anna Mugnaini, Marco Vignoli, Valerio Capasso, Clemente Del Prete, Sonia Romanelli, Maria Novella Supuran, Claudiu T. J Enzyme Inhib Med Chem Brief Report In this paper, the efficiency of the carbonic anhydrase (CA) enzyme in accelerating the hydration of CO(2) is evaluated using a measurement system which consists of a vessel in which a gaseous flow of mixtures of nitrogen and CO(2) is bubbled into water or water solutions containing a known quantity of CA enzyme. The pH value of the solution and the CO(2) concentration at the measurement system gas exhaust are continuously monitored. The measured CO(2) level allows for assessing the quantity of CO(2), which, subtracted from the gaseous phase, is dissolved into the liquid phase and/or hydrated to bicarbonate. The measurement procedure consists of inducing a transient and observing and modelling the different kinetics involved in the steady-state recovery with and without CA. The main contribution of this work is exploiting dynamical system theory and chemical kinetics modelling for interpreting measurement results for characterising the activity of CA enzymes. The data for model fitting are obtained from a standard bioreactor, in principle equal to standard two-phase bioreactors described in the literature, in which two different techniques can be used to move the process itself away from the steady-state, inducing transients. Taylor & Francis 2021-01-12 /pmc/articles/PMC7831361/ /pubmed/33430654 http://dx.doi.org/10.1080/14756366.2020.1864631 Text en © 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Brief Report Parri, Lorenzo Fort, Ada Lo Grasso, Anna Mugnaini, Marco Vignoli, Valerio Capasso, Clemente Del Prete, Sonia Romanelli, Maria Novella Supuran, Claudiu T. Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results |
title | Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results |
title_full | Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results |
title_fullStr | Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results |
title_full_unstemmed | Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results |
title_short | Evaluating the efficiency of enzyme accelerated CO(2) capture: chemical kinetics modelling for interpreting measurement results |
title_sort | evaluating the efficiency of enzyme accelerated co(2) capture: chemical kinetics modelling for interpreting measurement results |
topic | Brief Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7831361/ https://www.ncbi.nlm.nih.gov/pubmed/33430654 http://dx.doi.org/10.1080/14756366.2020.1864631 |
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