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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lonshakova-Mukina V., Esimbekova E., Kratasyuk V.
Заглавие : Impact of enzyme stabilizers on the characteristics of biomodules for bioluminescent biosensors
Место публикации : Sens Actuators, B Chem. - 2015. - Vol. 213. - С. 244-247. - ISSN 09254005 (ISSN) , DOI 10.1016/j.snb.2015.02.061
Ключевые слова (''Своб.индексиров.''): bioluminescence--body fluids--carrier concentration--enzymes--starch--bioluminescent biosensor--bovine serum albumins--dithiothreitol--maximum permissible concentration--mercaptoethanol--oxidoreductases--storage stability--toxic substances--biosensors
Аннотация: The biomodule of bioluminescent biosensor based on a coupled enzyme system NADH:FMN-oxidoreductase and luciferase, co-immobilized with substrates in dried starch or gelatin gels, has been developed. We studied the impact of several stabilizers - dithiothreitol (DTT), bovine serum albumin (BSA) and mercaptoethanol (ME) on the biomodule's activity, storage stability and sensitivity to toxic substances. The inclusion of stabilizers increases the activity of the biological module by more than 150%. To achieve the combination of high activity, prolonged storage time and acute sensitivity to toxic substances within maximum permissible concentration we used starch gel as a carrier adding 100 ?M DTT to the immobilized preparation. The gelatin-based biological module had greater storage stability than the starch-based one but demonstrated less sensitivity to toxic substances. © 2015 Elsevier B.V. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deeva, Anna A., Zykova, Evgenia A., Nemtseva, Elena V., Kratasyuk, Valentina A.
Заглавие : Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria
Колич.характеристики :7 с
Коллективы : Russian Foundation for Basic Research [18-44-243009]; Ministry of Education and Science of the Russian Federation [0356-2019-0019, 6.7734.2017]; Krasnoyarsk Region Science and Technology [18-44-243009]
Место публикации : Proteins: WILEY, 2019. - Vol. 87, Is. 9. - С. 723-729. - ISSN 0887-3585, DOI 10.1002/prot.25696. - ISSN 1097-0134(eISSN)
Примечания : Cited References:39. - The Russian Foundation for Basic Research and Krasnoyarsk Region Science and Technology Support Fund, Grant/Award Number: 18-44-243009; Ministry of Education and Science of the Russian Federation, Grant/Award Numbers: 0356-2019-0019, 6.7734.2017
Предметные рубрики: ESCHERICHIA-COLI
FLAVIN OXIDOREDUCTASE
CRYSTAL-STRUCTURE
Аннотация: In luminous bacteria NAD(P)H:flavin-oxidoreductases LuxG and Fre, there are homologous enzymes that could provide a luciferase with reduced flavin. Although Fre functions as a housekeeping enzyme, LuxG appears to be a source of reduced flavin for bioluminescence as it is transcribed together with luciferase. This study is aimed at providing the basic conception of Fre and LuxG evolution and revealing the peculiarities of the active site structure resulted from a functional variation within the oxidoreductase family. A phylogenetic analysis has demonstrated that Fre and LuxG oxidoreductases have evolved separately after the gene duplication event, and consequently, they have acquired changes in the conservation of functionally related sites. Namely, different evolutionary rates have been observed at the site responsible for specificity to flavin substrate (Arg 46). Also, Tyr 72 forming a part of a mobile loop involved in FAD binding has been found to be conserved among Fre in contrast to LuxG oxidoreductases. The conservation of different amino acid types in NAD(P)H binding site has been defined for Fre (arginine) and LuxG (proline) oxidoreductases.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sarangova A.B., Somova L.A., Pechurkin N.S.
Заглавие : On monitoring the bacterial component as an indicator of the state of small man-made ecosystems
Место публикации : Advances in Space Research. - 2001. - Vol. 27, Is. 9. - С. 1605-1609. - ISSN 02731177 (ISSN) , DOI 10.1016/S0273-1177(01)00256-3
Ключевые слова (''Своб.индексиров.''): bacteria--ecosystems--substrates--intracellular substrate concentration--space research--catalase--oxidoreductase--artificial ecosystem--article--bacterial phenomena and functions--biomass--culture medium--ecosystem--enzymology--growth, development and aging--metabolism--microbiology--oxygen consumption--pseudomonas--bacterial physiology--biomass--catalase--culture media--ecosystem--oxidoreductases--oxygen consumption--pseudomonas--water microbiology
Аннотация: High reproduction rates make the bacterial component of ecosystems a good indicator of the state of the system on the whole. This determines the necessity to develop rapid monitoring of the functional state of the bacterial component of small ecosystems. Information about substrate concentration in the population is indicative of the state of the bacterial culture. Conventional methods of monitoring the concentration of integral substrate in the system take time much longer than the changes in the ecosystem. The paper presents theoretical foundations for the logical sequence "catalase activity - intracellular substrate concentration - estimate of substrate consumed by bacteria" for experimental verification and as a consequence of development of the integral method of monitoring the bacterial population on the basis of determining bacterial catalase activity. В© 2001 COSPAR. Published by Elsevier Science Ltd. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T.G., Kalacheva G.S., Gorbunova O.V., Zhila N.O.
Заглавие : Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha
Место публикации : Prikladnaia biokhimiia i mikrobiologiia. - 2004. - Vol. 40, Is. 2. - С. 201-209. - ISSN 05551099 (ISSN)
Ключевые слова (''Своб.индексиров.''): acetoacetyl coenzyme a reductase--acetoacetyl-coa reductase--acetyl coenzyme a acyltransferase--acyltransferase--alcohol dehydrogenase--carboxylesterase--hydroxybutyrate dehydrogenase--hydroxybutyric acid--poly(3 hydroxyalkanoic acid) depolymerase--poly(3-hydroxyalkanoic acid) depolymerase--poly(3-hydroxyalkanoic acid) synthase--polyhydroxyalkanoate synthase--polymer--article--chemistry--comparative study--culture medium--enzymology--growth, development and aging--metabolism--wautersia eutropha--acetyl-coa c-acyltransferase--acyltransferases--alcohol oxidoreductases--carboxylic ester hydrolases--culture media--cupriavidus necator--hydroxybutyrate dehydrogenase--hydroxybutyrates--polymers
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of the key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHA synthase, D-hydroxybutyrate dehydrogenase, and PHA depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHA synthase were recorded at the stage of acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only at stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not cause any marked changes in the time course of enzyme activity.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V.A., Esimbekova E.N., Gladyshev M.I., Khromichek E.B., Kuznetsov A.M., Ivanova E.A.
Заглавие : The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems
Место публикации : Chemosphere. - 2001. - Vol. 42, Is. 8. - С. 909-915. - ISSN 00456535 (ISSN) , DOI 10.1016/S0045-6535(00)00177-6
Ключевые слова (''Своб.индексиров.''): alcohol dehydrogenase--bacterial luciferase--bioluminescence--blooming--pollution--trypsin--water toxicity--alcohol dehydrogenase--benzoquinone--luciferase--trypsin--aquatic ecosystem--bioluminescence--water quality--article--bacterium culture--bioluminescence--blue green alga--ecosystem--pond--seasonal variation--water pollution--water quality--benzoquinones--biological assay--cyanobacteria--ecosystem--environmental monitoring--eutrophication--fmn reductase--indicators and reagents--luminescent measurements--nadh, nadph oxidoreductases--water pollutants--russian federation--algae--bacteria (microorganisms)--chlorophyta--cyanobacteria--uncultured cyanobacterium
Аннотация: A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies. В© 2001 Elsevier Science Ltd.
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