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Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity
In this article, the effect of polyallylamine (PAA) on the structure and catalytic characteristics of alcohol dehydrogenase (ADH) was studied. For this research, we used methods of stationary kinetics and fluorescence spectroscopy. It has been shown that PAA non-competitively inhibits ADH activity w...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7240490/ https://www.ncbi.nlm.nih.gov/pubmed/32268489 http://dx.doi.org/10.3390/polym12040832 |
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author | Kim, Aleksandr L. Musin, Egor V. Dubrovskii, Alexey V. Tikhonenko, Sergey A. |
author_facet | Kim, Aleksandr L. Musin, Egor V. Dubrovskii, Alexey V. Tikhonenko, Sergey A. |
author_sort | Kim, Aleksandr L. |
collection | PubMed |
description | In this article, the effect of polyallylamine (PAA) on the structure and catalytic characteristics of alcohol dehydrogenase (ADH) was studied. For this research, we used methods of stationary kinetics and fluorescence spectroscopy. It has been shown that PAA non-competitively inhibits ADH activity while preserving its quaternary structure. It was established that 0.1 M ammonium sulfate removes the inhibitory effect of PAA on ADH, which is explained by the binding of sulfate anion (NH(4))(2)SO(4) with polyallylamine amino groups. As a result, the rigidity of the polymer chain increases and the ability to bind to the active loop of the enzyme increases. It is also shown that sodium chloride removes the inhibitory effect of PAA on ADH due to an electrostatic screening of the enzyme from polyelectrolyte. The method of encapsulating ADH in polyelectrolyte microcapsules was adapted to the structure and properties of the enzyme molecule. It was found that the best for ADH is its encapsulation by adsorption into microcapsules already formed on CaCO(3) particles. It was shown that the affinity constant of encapsulated alcohol dehydrogenase to the substrate is 1.7 times lower than that of the native enzyme. When studying the affinity constant of ADH in a complex with PAA to ethanol, the effect of noncompetitive inhibition of the enzyme by polyelectrolyte was observed. |
format | Online Article Text |
id | pubmed-7240490 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-72404902020-06-11 Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity Kim, Aleksandr L. Musin, Egor V. Dubrovskii, Alexey V. Tikhonenko, Sergey A. Polymers (Basel) Article In this article, the effect of polyallylamine (PAA) on the structure and catalytic characteristics of alcohol dehydrogenase (ADH) was studied. For this research, we used methods of stationary kinetics and fluorescence spectroscopy. It has been shown that PAA non-competitively inhibits ADH activity while preserving its quaternary structure. It was established that 0.1 M ammonium sulfate removes the inhibitory effect of PAA on ADH, which is explained by the binding of sulfate anion (NH(4))(2)SO(4) with polyallylamine amino groups. As a result, the rigidity of the polymer chain increases and the ability to bind to the active loop of the enzyme increases. It is also shown that sodium chloride removes the inhibitory effect of PAA on ADH due to an electrostatic screening of the enzyme from polyelectrolyte. The method of encapsulating ADH in polyelectrolyte microcapsules was adapted to the structure and properties of the enzyme molecule. It was found that the best for ADH is its encapsulation by adsorption into microcapsules already formed on CaCO(3) particles. It was shown that the affinity constant of encapsulated alcohol dehydrogenase to the substrate is 1.7 times lower than that of the native enzyme. When studying the affinity constant of ADH in a complex with PAA to ethanol, the effect of noncompetitive inhibition of the enzyme by polyelectrolyte was observed. MDPI 2020-04-06 /pmc/articles/PMC7240490/ /pubmed/32268489 http://dx.doi.org/10.3390/polym12040832 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kim, Aleksandr L. Musin, Egor V. Dubrovskii, Alexey V. Tikhonenko, Sergey A. Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity |
title | Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity |
title_full | Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity |
title_fullStr | Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity |
title_full_unstemmed | Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity |
title_short | Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity |
title_sort | effect of pollyallylamine on alcoholdehydrogenase structure and activity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7240490/ https://www.ncbi.nlm.nih.gov/pubmed/32268489 http://dx.doi.org/10.3390/polym12040832 |
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