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Polymers, volume 12, issue 4, pages 832

Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity

Kim Aleksandr L. ¹

Musin Egor V. ¹

Dubrovskii Alexey V ¹

Tikhonenko Sergey A. ¹

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Institute of Theoretical and Experimental Biophysics Russian Academy of Science, Institutskaya st., 3, Puschino 142290, Moscow Reg., Russia |

Publication type: Journal Article

Publication date: 2020-04-06

Multidisciplinary Digital Publishing Institute (MDPI)

Journal: Polymers

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Impact factor: 5

ISSN: 20734360

DOI: 10.3390/polym12040832

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PubMed ID: 32268489

General Chemistry

Polymers and Plastics

Abstract

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 (NH4)2SO4 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 CaCO3 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.

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Polymers	Polymers, 1, 50% Polymers 1 publication, 50%
Journal of Molecular Liquids	Journal of Molecular Liquids, 1, 50% Journal of Molecular Liquids 1 publication, 50%
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Kim A. L. et al. Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity // Polymers. 2020. Vol. 12. No. 4. p. 832.

GOST all authors (up to 50) Copy

Kim A. L., Musin E. V., Dubrovskii A. V., Tikhonenko S. A. Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity // Polymers. 2020. Vol. 12. No. 4. p. 832.

RIS |

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RIS Copy

TY - JOUR

DO - 10.3390/polym12040832

UR - https://doi.org/10.3390%2Fpolym12040832

TI - Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity

T2 - Polymers

AU - Dubrovskii, Alexey V

AU - Kim, Aleksandr L.

AU - Musin, Egor V.

AU - Tikhonenko, Sergey A.

PY - 2020

DA - 2020/04/06 00:00:00

PB - Multidisciplinary Digital Publishing Institute (MDPI)

SP - 832

IS - 4

VL - 12

PMID - 32268489

SN - 2073-4360

ER -

BibTex |

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BibTex Copy

@article{2020_Kim,

author = {Alexey V Dubrovskii and Aleksandr L. Kim and Egor V. Musin and Sergey A. Tikhonenko},

title = {Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity},

journal = {Polymers},

year = {2020},

volume = {12},

publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},

month = {apr},

url = {https://doi.org/10.3390%2Fpolym12040832},

number = {4},

pages = {832},

doi = {10.3390/polym12040832}

}

MLA

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MLA Copy

Kim, Aleksandr L., et al. “Effect of Pollyallylamine on Alcoholdehydrogenase Structure and Activity.” Polymers, vol. 12, no. 4, Apr. 2020, p. 832. https://doi.org/10.3390%2Fpolym12040832.

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Publisher

Multidisciplinary Digital Publishing Institute (MDPI)

Journal

Polymers

Quartile SCImago

Quartile WOS

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ISSN

20734360 (Electronic)

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Laboratory of Cell and Tissue Growth

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