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Computational Modeling of the Electrochemical System of Lipase Activity Detection
This paper presents computational modeling of response kinetics of bioelectroanalytical system based on solid supported lipase substrate and lipase interaction. The model assumes that lipase substrate is formed by dripping and drying a small amount of the ethanol solution of 9-(5′-ferrocenylpentanoy...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3714667/ https://www.ncbi.nlm.nih.gov/pubmed/27879913 http://dx.doi.org/10.3390/s8063873 |
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author | Puida, Mantas Ivanauskas, Feliksas Ignatjev, Ilja Valinčius, Gintaras Razumas, Valdemaras |
author_facet | Puida, Mantas Ivanauskas, Feliksas Ignatjev, Ilja Valinčius, Gintaras Razumas, Valdemaras |
author_sort | Puida, Mantas |
collection | PubMed |
description | This paper presents computational modeling of response kinetics of bioelectroanalytical system based on solid supported lipase substrate and lipase interaction. The model assumes that lipase substrate is formed by dripping and drying a small amount of the ethanol solution of 9-(5′-ferrocenylpentanoyloxy)nonyl disulfide (FPONDS) and that lipase is capable of cleaving FPONDS ester bonds via hydrolysis mechanism. Two mathematical models have been developed and evaluated trough computational simulation series by comparing them to experimental data. The results of simulation demonstrate that a good fitting might be obtained only taking into account non-linear substrate wash off process. |
format | Online Article Text |
id | pubmed-3714667 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-37146672013-07-18 Computational Modeling of the Electrochemical System of Lipase Activity Detection Puida, Mantas Ivanauskas, Feliksas Ignatjev, Ilja Valinčius, Gintaras Razumas, Valdemaras Sensors (Basel) Article This paper presents computational modeling of response kinetics of bioelectroanalytical system based on solid supported lipase substrate and lipase interaction. The model assumes that lipase substrate is formed by dripping and drying a small amount of the ethanol solution of 9-(5′-ferrocenylpentanoyloxy)nonyl disulfide (FPONDS) and that lipase is capable of cleaving FPONDS ester bonds via hydrolysis mechanism. Two mathematical models have been developed and evaluated trough computational simulation series by comparing them to experimental data. The results of simulation demonstrate that a good fitting might be obtained only taking into account non-linear substrate wash off process. Molecular Diversity Preservation International (MDPI) 2008-06-09 /pmc/articles/PMC3714667/ /pubmed/27879913 http://dx.doi.org/10.3390/s8063873 Text en © 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Puida, Mantas Ivanauskas, Feliksas Ignatjev, Ilja Valinčius, Gintaras Razumas, Valdemaras Computational Modeling of the Electrochemical System of Lipase Activity Detection |
title | Computational Modeling of the Electrochemical System of Lipase Activity Detection |
title_full | Computational Modeling of the Electrochemical System of Lipase Activity Detection |
title_fullStr | Computational Modeling of the Electrochemical System of Lipase Activity Detection |
title_full_unstemmed | Computational Modeling of the Electrochemical System of Lipase Activity Detection |
title_short | Computational Modeling of the Electrochemical System of Lipase Activity Detection |
title_sort | computational modeling of the electrochemical system of lipase activity detection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3714667/ https://www.ncbi.nlm.nih.gov/pubmed/27879913 http://dx.doi.org/10.3390/s8063873 |
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