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Stabilization of Butyrylcholinesterase by the Entrapment into the Natural Polymer-Based Gels / V. I. Lonshakova-Mukina, E. N. Esimbekova, V. A. Kratasyuk // Doklad. Biochem. Biophys. - 2018. - Vol. 479, Is. 1. - P98-100, DOI 10.1134/S1607672918020126 . - ISSN 1607-6729
Аннотация: A new method for obtaining stable butyrylcholinesterase (BuChE) samples based on the enzyme immobilization in starch and gelatin gels followed by drying is proposed. Coimmobilization of BuChE with the thiol group indicator 5,5'-dithiobis(2-nitrobenzoic) acid did not reduce the activity of BuChE, which allowed us to simplify the procedure and reduce the time of analysis of organophosphorus pesticides. The resulting immobilized samples retained activity for at least 300 days. BuChE samples based on the starch gel showed a greater sensitivity in the determination of pesticides as compared to the samples based on the gelatin gel. © 2018, Pleiades Publishing, Ltd.

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Держатели документа:
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Federal Research Center, Krasnoyarsk Research Center, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Lonshakova-Mukina, V. I.; Esimbekova, E. N.; Kratasyuk, V. A.

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Set of Enzymatic Bioassays for Assessment of Soil Contamination / E. M. Kolosova, O. S. Sutormin, E. N. Esimbekova [et al.] // Dokl. Biol. Sci. - 2019. - Vol. 489, Is. 1. - P165-168, DOI 10.1134/S0012496619060024 . - ISSN 1608-3105
Аннотация: A concept of the comprehensive assessment of soil contamination is proposed. According to it, the conclusion regarding the presence of toxic substances in the analyzed sample is based on the inhibition of enzymatic reactions responsible for various functions of a living organism, such as luminescence, respiration, etc. These functions are taken as test functions in classical bioassays with the use of living objects (luminous bacteria, daphnia, algae, and others). The regularities of the impact of different classes of toxicants on the activity of particular enzymes or coupled oligo-enzyme chains have been established. These enzyme reactions are selected as potential test objects: markers of contamination. Three enzyme systems with the maximal sensitivity to different classes of toxicants have been chosen for the set of enzymatic bioassays: butyrylcholinesterase, NAD(P)H:FMN-oxidoreductase + luciferase, and lactate dehydrogenase + NAD(P)H:FMN-oxidoreductase + luciferase. The possibility to use enzymes instead of living organisms in the bioassay of natural complex systems has been shown.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kolosova, E. M.; Sutormin, O. S.; Esimbekova, E. N.; Lonshakova-Mukina, V. I.; Kratasyuk, V. A.

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Gelatin and Starch: What Better Stabilizes the Enzyme Activity? / E. N. Esimbekova, A. E. Govorun, V. I. Lonshakova-Mukina, V. A. Kratasyuk // Dokl. Biol. Sci. - 2020. - Vol. 491, Is. 1. - P43-46, DOI 10.1134/S0012496620020039 . - ISSN 0012-4966
Кл.слова (ненормированные):
butyrylcholinesterase -- enzyme stabilization -- gelatin -- luciferase -- NAD(P)H:FMN oxidoreductase -- starch -- thermal inactivation of enzymes
Аннотация: Abstract: The regularities of the functioning of a number of enzymes in a viscous environment created by natural polymers, starch and gelatin are examined. Based on the analysis of kinetic curves of thermal inactivation, mechanisms of thermal inactivation of enzymes in a viscous microenvironment are proposed. Using the example of butyrylcholinesterase, NAD(P)H:FMN oxidoreductase, and coupled system of the luminous bacteria (NAD(P)H:FMN oxidoreductase + luciferase), the conditions, under which starch and gelatin have a stabilizing effect on enzyme activity during storage and exposure to various physical and chemical environmental factors, were found. A significant increase in the stabilizing effect is achieved by eliminating water during drying the enzyme preparations immobilized in starch and gelatin polymer gels. © 2020, Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Govorun, A. E.; Lonshakova-Mukina, V. I.; Kratasyuk, V. A.

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Software for matching standard activity enzyme biosensors for soil pollution analysis / V. A. Kratasyuk, E. M. Kolosova, O. S. Sutormin [et al.] // Sensors. - 2021. - Vol. 21, Is. 3. - Ст. 1017. - P1-10, DOI 10.3390/s21031017 . - ISSN 1424-8220
Кл.слова (ненормированные):
Bacterial luciferase -- Biosensors -- Butyrylcholinesterase -- Enzyme -- Lactic dehydrogenase -- Software -- Soil pollution -- Biosensors -- Soil pollution -- Soil surveys -- Soils -- Commercial standards -- Environmental Monitoring -- Enzyme biosensors -- Enzyme systems -- Inhibitory effect -- JavaScript programming -- Soil sample -- Toxic agents -- Enzyme activity
Аннотация: This work is dedicated to developing enzyme biosensor software to solve problems regarding soil pollution analysis. An algorithm and specialised software have been developed which stores, analyses and visualises data using JavaScript programming language. The developed software is based on matching data of 51 non-commercial standard soil samples and their inhibitory effects on three enzyme systems of varying complexity. This approach is able to identify the influence of chemical properties soil samples, without toxic agents, on enzyme biosensors. Such software may find wide use in environmental monitoring. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Department of Biophysics, Institute of Fundamental Biology and Biotechology, Siberian Federal University, 79 Svobodny pr, Krasnoyarsk, 660041, Russian Federation
Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, 50/50 Akagemgorodok, Krasnoyarsk, 660036, Russian Federation
Department of High-Efficiency Calculations, Siberian Federal University, 26-ULK building Kirensky St, Krasnoyarsk, 660074, Russian Federation
Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk Research Institute of Agriculture, Russian Academy of Sciences, Siberian Branch, 66 Svobodny pr, Krasnoyarsk, 660037, Russian Federation
Federal Research Center ‘Krasnoyarsk Scientific Center SB RAS’, Krasnoyarsk Research Institute of Agricultural, Siberian Federal University, 79 Svobodny pr, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Kratasyuk, V. A.; Kolosova, E. M.; Sutormin, O. S.; Lonshakova-Mukina, V. I.; Baygin, M. M.; Rimatskaya, N. V.; Sukovataya, I. E.; Shpedt, A. A.

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Software for Matching Standard Activity Enzyme Biosensors for Soil Pollution Analysis / V. A. Kratasyuk, E. M. Kolosova, O. S. Sutormin [et al.] // Sensors. - 2021. - Vol. 21, Is. 3. - Ст. 1017, DOI 10.3390/s21031017. - Cited References:20. - This research was funded by RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science, Grant number 20-44-243001 and the Ministry of Science and Higher Education of the Russian Federation, Grant number FSRZ-2020-0006. . - ISSN 1424-8220

РУБ Chemistry, Analytical + Engineering, Electrical & Electronic + Instruments

Кл.слова (ненормированные):
biosensors -- enzyme -- butyrylcholinesterase -- lactic dehydrogenase -- bacterial luciferase -- soil pollution -- software
Аннотация: This work is dedicated to developing enzyme biosensor software to solve problems regarding soil pollution analysis. An algorithm and specialised software have been developed which stores, analyses and visualises data using JavaScript programming language. The developed software is based on matching data of 51 non-commercial standard soil samples and their inhibitory effects on three enzyme systems of varying complexity. This approach is able to identify the influence of chemical properties soil samples, without toxic agents, on enzyme biosensors. Such software may find wide use in environmental monitoring.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechol, Dept Biophys, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Krasnoyarsk Sci Ctr SB RAS, Photobiol Lab, Fed Res Ctr,Siberian Branch,Inst Biophys, 50-50 Akagemgorodok, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Dept High Efficiency Calculat, 26 ULK Bldg Kirensky St, Krasnoyarsk 660074, Russia.
Russian Acad Sci, Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk Res Inst Agr, Siberian Branch,Fed Res Ctr, 66 Svobodny Pr, Krasnoyarsk 660037, Russia.
Siberian Fed Univ, Inst Fundamental Biol & Biotechol, Dept Aquat & Terr Ecosyst, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Kolosova, Elizaveta M.; Sutormin, Oleg S.; Lonshakova-Mukina, Viktoriya, I; Baygin, Matvey M.; Rimatskaya, Nadezhda, V; Sukovataya, Irina E.; Shpedt, Alexander A.; RFBRRussian Foundation for Basic Research (RFBR); Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science [20-44-243001]; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]

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Thermal Inactivation of Butyrylcholinesterase in Starch and Gelatin Gels / V. I. Lonshakova-Mukina, E. N. Esimbekova, V. A. Kratasyuk // Catalysts. - 2021. - Vol. 11, Is. 4. - Ст. 492, DOI 10.3390/catal11040492. - Cited References:39. - The research was funded by the Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, and the Russian Foundation for Basic Research [project No 20-44-242001]. . - ISSN 2073-4344

РУБ Chemistry, Physical

Кл.слова (ненормированные):
butyrylcholinesterase -- thermal inactivation -- enzyme stability -- kinetics -- starch -- gelatin
Аннотация: The present study demonstrates a simple approach to enhancing thermal stability of butyrylcholinesterase (BChE) by using natural polymers. Analysis of thermal inactivation of the tetrameric BChE in starch and gelatin gels at 50-64 degrees C showed that thermal inactivation followed second-order kinetics and involved two alternating processes of BChE inactivation, which occurred at different rates (fast and slow processes). The activation enthalpy Delta H-# and the activation entropy Delta S-# for BChE in starch and gelatin gels were evaluated. The values of Delta H-# for the fast and the slow thermal inactivation of BChE in starch gel were 61 +/- 3, and 22 +/- 2 kcal/mol, respectively, and the values of Delta S-# were 136 +/- 12 and -2.03 +/- 0.05 cal center dot K-1 center dot mol(-1), respectively. Likewise, the values of Delta H-# for BChE in gelatin gel were 58 +/- 6 and 109 +/- 11 kcal/mol, and the values of Delta S-# were 149 +/- 16 and 262 +/- 21 cal center dot K-1 center dot mol(-1), respectively. The values of the activation parameters obtained in this study suggest that starch gel produced a stronger stabilizing effect on BChE exposed to elevated temperatures over long periods compared with gelatin gel.

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Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Biophys Dept, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lonshakova-Mukina, Victoria I.; Esimbekova, Elena N.; Kratasyuk, Valentina A.; Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-44-242001]

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