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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Кратасюк В.А., Гительзон И.И.
Заглавие : Использование светящихся бактерий в биолюминесцентном анализе : научное издание
Место публикации : Успехи микробиол. - Москва, 1987. - N 21. - С. 3-30. - ISSN 0566-392X
ГРНТИ : 34.15.33
Предметные рубрики: БАКТЕРИИ
СВЕТЯЩИЕСЯ КУЛЬТУРЫ
СВОЙСТВА
ИММОБИЛИЗОВАННЫЙ ФЕРМЕНТ
ПОЛУЧЕНИЕ
ПРИМЕНЕНИЕ
БИОЛЮМИНЕСЦЕНТНЫЙ АНАЛИЗ
ОБЩИЕ ПРИНЦИПЫ
ОБЗОРЫ
БИБЛ 161
IMMOBILIZED ENZYMES
В О М Е СЕ СЕ
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya O. A., Ronzhin N. O., Artemenko K. S., Bondar V. S.
Заглавие : Creation of Bifunctional Indicating Complex Based on Nanodiamonds and Extracellular Oxidases of Luminous Fungus Neonothopanus nambi
Колич.характеристики :4 с
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2018. - Vol. 480, Is. 1. - С. 135-138. - ISSN 1607-6729, DOI 10.1134/S160767291803002X. - ISSN 1608-3091(eISSN)
Примечания : Cited References:13
Предметные рубрики: PHANEROCHAETE-CHRYSOSPORIUM
NANOPARTICLES
Аннотация: A bifunctional indicating complex was created by immobilization of extracellular oxidases (glucose oxidase and peroxidases) of luminous fungus Neonothopanus nambi onto modified nanodiamonds (MNDs) synthesized by detonation. It was found that the enzymes firmly adsorb onto MND particles and exhibit their catalytic activity. Model in vitro experiments showed that the created MND-enzymes complex is suitable for repeated use for analyte (glucose and phenol) testing and retains its activity after storage at 4 degrees C in deionized water for 1 month. The data obtained offer the prospects for developing a new class of reusable multifunctional indicating and diagnostic test systems on the basis of MNDs and higher fungal enzymes for medical and ecological analytics.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova M. D., Markova S. V., Vysotski E. S.
Заглавие : Bioluminescent and structural features of native folded Gaussia luciferase
Место публикации : J. Photochem. Photobiol. B Biol.: Elsevier B.V., 2018. - Vol. 183. - С. 309-317. - ISSN 10111344 (ISSN) , DOI 10.1016/j.jphotobiol.2018.04.050
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--copepod luciferase--halophilic enzyme--kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lukyanenko K. A., Denisov I. A., Yakimov A. S., Esimbekova E. N., Belousov K. I., Bukatin A. S., Kukhtevich I. V., Sorokin V. V., Evstrapov A. A., Belobrov P. I.
Заглавие : Analytical Enzymatic Reactions in Microfluidic Chips
Колич.характеристики :6 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2017. - Vol. 53, Is. 7. - С. 775-780. - ISSN 0003-6838, DOI 10.1134/S0003683817070043. - ISSN 1573-8183(eISSN)
Примечания : Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041).
Предметные рубрики: BIOAVAILABLE HEAVY-METALS
DEVICES
POINT
LAB
Ключевые слова (''Своб.индексиров.''): bioluminescence--luciferase--microfluidics--microfluidic chip--enzymatic--bioassay
Аннотация: A number of approaches have been proposed and tested to transfer enzymatic reactions into the functional elements of microfluidic chips on the example of the bienzyme bioluminescent reaction involving NAD(P)H:FMN-oxidoreductase and luciferase. Measurement of the catalytic activity of these enzymes (under the influence of pollutants) is the basis of enzymatic bioassay of various liquids. It was found that all of the components of the reaction must be placed in the same cell of the chip to improve the reproducibility of the measurements. The use of starch gel as a carrier for immobilization and gelatin as a scaffold in the reactor of the chip enables the preservation of enzyme activity in the course of sealing the chip at room temperature. It is shown that the components of the reaction should be vigorously stirred in a microfluidic chip reactor to improve the efficiency of the analysis. As a result of the studies, a prototype of microfluidic chip based on the enzymatic bioluminescent reaction is proposed. It is characterized by a detection limit of copper sulfate of 3 mu M that corresponds to the sensitivity of traditional lux-biosensors based on living cells. The analysis time is reduced to 1 min, and the analysis can be performed by individuals without special laboratory skills.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya O. A., Ronzhin N. O., Bondar V. S.
Заглавие : Estimating levels of light emission and extracellular peroxidase activity of mycelium of luminous fungus Neonothopanus nambi treated with ?-glucosidase
Место публикации : Curr. Res. Environ. Appl. Mycol. J. Fungal: Beijing Academy of Agriculture and Forestry Sciences, Institute of Plant and Environment Protection, 2018. - Vol. 8, Is. 1. - С. 75-85. - ISSN 22292225 (ISSN) , DOI 10.5943/cream/8/1/6
Ключевые слова (''Своб.индексиров.''): basidiomycetes--cell wall--luminescence--polysaccharide sheath
Аннотация: The present study estimates the level of extracellular peroxidase activity and light emission intensity of mycelium of luminescent basidiomycete Neonothopanus nambi treated with ?-glucosidase. A hypothesis has been proposed that treatment with ?-glucosidase may trigger biochemical mechanisms of activation of ROS (primarily hydrogen peroxide) generation in N. nambi mycelium. The results obtained indicate that the enzyme causes partial disintegration of the slimy sheath of fungal hyphae and intracellular matrix, which leads to release of the extracellular peroxidases to the incubation medium. Mycelial cells treated with the enzyme reach the peak of their luminescence sooner. It has been assumed that partial loss of extracellular peroxidases, as important enzymes of antioxidant defense, may be compensated for by an increase in the level of light emission by the fungus. © 2018 Beijing Academy of Agriculture and Forestry Sciences.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kotlobay A. A., Sarkisyan K. S., Mokrushina Y. A., Marcet-Houben M., Serebrovskaya E. O., Markina N. M., Somermeyer L. G., Gorokhovatsky A. Y., Vvedensky A., Purtov K. V., Petushkov V. N., Rodionova N. S., Chepurnyh T. V., Fakhranurova L. I., Guglya E. B., Ziganshin R., Tsarkova A. S., Kaskova Z. M., Shender V., Abakumov M., Abakumova T. O., Povolotskaya I. S., Eroshkin F. M., Zaraisky A. G., Mishin A. S., Dolgov S. V., Mitiouchkina T. Y., Kopantzev E. P., Waldenmaier H. E., Oliveira A. G., Oba Y., Barsova E., Bogdanova E. A., Gabaldon T., Stevani C. V., Lukyanov S., Smirnov I. V., Gitelson J. I., Kondrashov F. A., Yampolsky I. V.
Заглавие : Genetically encodable bioluminescent system from fungi
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: National Academy of Sciences, 2018. - Vol. 115, Is. 50. - С. 12728-12732. - ISSN 00278424 (ISSN) , DOI 10.1073/pnas.1803615115
Ключевые слова (''Своб.индексиров.''): bioluminescence--fungal luciferase--fungal luciferin biosynthesis
Аннотация: Bioluminescence is found across the entire tree of life, conferring a spectacular set of visually oriented functions from attracting mates to scaring off predators. Half a dozen different luciferins, molecules that emit light when enzymatically oxidized, are known. However, just one biochemical pathway for luciferin biosynthesis has been described in full, which is found only in bacteria. Here, we report identification of the fungal luciferase and three other key enzymes that together form the biosynthetic cycle of the fungal luciferin from caffeic acid, a simple and widespread metabolite. Introduction of the identified genes into the genome of the yeast Pichia pastoris along with caffeic acid biosynthesis genes resulted in a strain that is autoluminescent in standard media. We analyzed evolution of the enzymes of the luciferin biosynthesis cycle and found that fungal bioluminescence emerged through a series of events that included two independent gene duplications. The retention of the duplicated enzymes of the luciferin pathway in nonluminescent fungi shows that the gene duplication was followed by functional sequence divergence of enzymes of at least one gene in the biosynthetic pathway and suggests that the evolution of fungal bioluminescence proceeded through several closely related stepping stone nonluminescent biochemical reactions with adaptive roles. The availability of a complete eukaryotic luciferin biosynthesis pathway provides several applications in biomedicine and bioengineering. © 2018 National Academy of Sciences. All Rights Reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya, Olga, Ronzhin, Nikita, Artemenko, Karina, Bondar, Vladimir
Заглавие : Nanodiamonds as an effective adsorbent for immobilization of extracellular peroxidases from luminous fungus Neonothopanus nambi to construct a phenol detection system
Колич.характеристики :9 с
Коллективы : Russian Academy of Sciences [0356-2016-0709]
Место публикации : Biocatal. Biotransform.: TAYLOR & FRANCIS LTD, 2019. - Vol. 37, Is. 2. - С. 97-105. - ISSN 1024-2422, DOI 10.1080/10242422.2018.1472586. - ISSN 1029-2446(eISSN)
Примечания : Cited References:50. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences [project no. 0356-2016-0709].
Предметные рубрики: CARBON NANOTUBES
ARMILLARIA-BOREALIS
LIGHT-EMISSION
DEGRADATION
Ключевые слова (''Своб.индексиров.''): nanodiamonds--immobilization--luminous fungus--beta-glucosidase--peroxidase--indicator system
Аннотация: Modified nanodiamonds (MNDs) produced by detonation synthesis can be used as an effective adsorbent to immobilize extracellular peroxidases of the luminous basidiomycete Neonothopanus nambi. The enzymes are firmly immobilized on MND particles and exhibit catalytic activity. The indicator system (the MND-enzyme complex) reused many times retains its ability to catalyze reaction of co-oxidation of phenol and 4-aminoantipirine in the presence of hydrogen peroxide and remains functionally active during long-term storage (for 1 month or longer) in aqueous suspensions at 4 degrees C. MNDs and enzymes of higher fungi can be effectively used to construct new reusable indicator systems for analytical applications such as monitoring contamination of aquatic environments by phenolic compounds.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sutormin O. S., Sukovataya I. E., Pande S., Kratasyuk V. A.
Заглавие : Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase
Место публикации : Mol. Cat.: Elsevier B.V., 2018. - Vol. 458. - С. 60-66. - ISSN 24688231 (ISSN) , DOI 10.1016/j.mcat.2018.08.012
Ключевые слова (''Своб.индексиров.''): bioluminescence--coupling of enzymes--in vivo simulated media--metabolic chain--protein stability
Аннотация: One of the current trends of the modern biology figures out cellular enzyme behaviour. Numerous researches look more closely at the chemical composition of creating in vivo simulated media conditions. The aim of this work was to find out a thermodynamic cooperativity of enzymes in a triple-enzyme chain (lactate dehydrogenase + NAD(P)H: FMN-oxidoreductase + bacterial luciferase) under in vivo simulated condition. The thermodynamic cooperativity effects were found out based on the influence of the viscogens (glycerol and sucrose) on the thermal stability of the triple-enzyme system. The results showed that the viscogens do not lead to an increase in the thermal stability of the triple-enzyme system. In addition, organic solvents (sucrose and glycerol) added as viscous agents to the reaction medium altered the kinetics of this triple-enzyme chain, including changing the light emission decay constant (kdec) and quantum yield of luminescence (Q). Plus, sucrose was found to be more efficient in limiting the flexibility of enzymes than glycerol. The high sensitivity of the triple-enzyme system to the viscogens may be connected with a fact that lactate dehydrogenase does not bound with couple enzyme system NAD(P)H: FMN-oxidoreductase + bacterial luciferase inside the real cell. Since this approach may be used as a method to understand the real connection between enzymes in cellular multi-enzyme metabolic chains inside the luminous bacteria cell. © 2018 Elsevier B.V.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petrova A. S., Lukonina A. A., Dementyev D. V., Bolsunovsky A. Ya. , Popov A. V., Kudryasheva N. S.
Заглавие : Protein-based fluorescent bioassay for low-dose gamma radiation exposures
Место публикации : Anal. Bioanal. Chem.: Springer Verlag, 2018. - ISSN 16182642 (ISSN) , DOI 10.1007/s00216-018-1282-5
Ключевые слова (''Своб.индексиров.''): bioassay--enzymes--fluorescence/luminescence--fluorescent protein--gamma radiation--radiotoxicity--efficiency--enzymes--fluorescence--gamma rays--proteins--proton transfer--fluorescence characteristics--fluorescence intensities--fluorescence spectra--fluorescence/luminescence--fluorescent protein--photochemical process--physiological liquids--radiotoxicity--bioassay
Аннотация: The study suggests an application of a coelenteramide-containing fluorescent protein (CLM-CFP) as a simplest bioassay for gamma radiation exposures. “Discharged obelin,” a product of the bioluminescence reaction of the marine coelenterate Obelia longissima, was used as a representative of the CLM-CFP group. The bioassay is based on a simple enzymatic reaction—photochemical proton transfer in the coelenteramide-apoprotein complex. Components of this reaction differ in fluorescence color, providing, by this, an evaluation of the proton transfer efficiency in the photochemical process. This efficiency depends on the microenvironment of the coelenteramide within the protein complex, and, hence, can evaluate a destructive ability of gamma radiation. The CLM-CFP samples were exposed to gamma radiation (137Cs, 2 mGy/h) for 7 and 16 days at 20 °C and 5 °C, respectively. As a result, two fluorescence characteristics (overall fluorescence intensity and contributions of color components to the fluorescence spectra) were identified as bioassay parameters. Both parameters demonstrated high sensitivity of the CLM-CFP-based bioassay to the low-dose gamma radiation exposure (up to 100 mGy). Higher temperature (20 °C) enhanced the response of CLM-CFP to gamma radiation. This new bioassay can provide fluorescent multicolor assessment of protein destruction in cells and physiological liquids under exposure to low doses of gamma radiation. [Figure not available: see fulltext.]. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Denisov I., Lukyanenko K., Yakimov A., Kukhtevich I., Esimbekova E., Belobrov P.
Заглавие : Disposable luciferase-based microfluidic chip for rapid assay of water pollution
Место публикации : Lumin. - 2018. - Vol. 33, Is. 6. - С. 1054-1061. - ISSN 15227235 (ISSN) , DOI 10.1002/bio.3508
Ключевые слова (''Своб.индексиров.''): bioassay--lab-on-a-chip--luciferase--microfluidics--solvent bonding
Аннотация: In the present study, we demonstrate the use of a disposable luciferase-based microfluidic bioassay chip for environmental monitoring and methods for fabrication. The designed microfluidic system includes a chamber with immobilized enzymes of bioluminescent bacteria Photobacterium leiognathi and Vibrio fischeri and their substrates, which dissolve after the introduction of the water sample and thus activate bioluminescent reactions. Limits of detection for copper (II) sulfate, 1,3-dihydroxybenzene and 1,4-benzoquinone for the proposed microfluidic biosensor measured 3 ?M, 15 mM, and 2 ?M respectively, and these values are higher or close to the level of conventional environmental biosensors based on lyophilized bacteria. Approaches for entrapment of enzymes on poly(methyl methacrylate) (PMMA) plates using a gelatin scaffold and solvent bonding of PMMA chip plates under room temperature were suggested. The proposed microfluidic system may be used with some available luminometers and future portable luminescence readers. © 2018 John Wiley & Sons, Ltd.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Puzyr A. P., Medvedeva S. E., Bondar V. S.
Заглавие : Biochemical changes causes lack of bioluminescence in fruiting bodies of Armillaria
Место публикации : Mycosphere: Guizhou Key Laboratory of Agricultural Biotechnology, 2017. - Vol. 8, Is. 1. - С. 9-17. - ISSN 20777000 (ISSN) , DOI 10.5943/mycosphere/8/1/2
Ключевые слова (''Своб.индексиров.''): enzymes and substrate of luminescent reaction--kinetics of luminescence--luminous mycelia--nonluminous fruiting bodies of fungus
Аннотация: Mycelium of Armillaria species exhibit bioluminescence in nature and when cultivated on artificial nutrient media. However, fruiting bodies do not emit visible light. The present study investigates biochemical changes which cause this phenomenon. Light emission was studied in experiments with mixtures of cold and hot extracts of the luminous mycelium of Armillaria borealis IBSO 2328 and nonluminous fruiting bodies of this fungus and an unidentified species of the genus (Armillaria sp.). Hot extracts of fruiting bodies of the nonluminous Pholiota squarrosa were used as the substrate analog of the luminescent reaction, as previously this fungus had been found to contain a high amount of this substance. Control experiments showed that cold extracts of A. borealis IBSO 2328 mycelium contained enzymes for the luminescent reaction, which is initiated after addition hot extracts of P. squarrosa fruiting bodies. Parallel experiments with extracts of the fruiting bodies of Armillaria showed that: (i) - cold extracts did not contain enzymes of the luminescent reaction or contain very small amounts of these enzymes and (ii) - hot extracts did not contain substrate of the luminescent reaction. Thus, the reason why fruiting bodies of Armillaria do not emit light is that they do not contain components required for visible luminescence. The study discusses possible causes why the enzymes and substrate of the luminescent reaction are not synthesized in fruiting bodies of Armillaria. © Guizhou Academy of Agricultural Sciences.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Esimbekova E. N., Asanova A. A., Deeva A. A., Kratasyuk V. A.
Заглавие : Inhibition effect of food preservatives on endoproteinases
Место публикации : Food Chem.: Elsevier Ltd, 2017. - Vol. 235. - С. 294-297. - ISSN 03088146 (ISSN) , DOI 10.1016/j.foodchem.2017.05.059
Ключевые слова (''Своб.индексиров.''): endoproteinases--food additives--pancreatic disease--pancreatic enzymes--benzoic acid--enzyme activity--enzymes--food additives--food preservatives--potassium sorbate--sodium--acceptable daily intakes--decay constants--endoproteinases--human metabolisms--inhibition effect--light intensity--protein digestion--sodium benzoate--sorbic acid
Аннотация: The present manuscript proposes a novel approach to assess the impact of food additives on human metabolism by analysing their effect on biomarker enzyme activity. Alterations in the activity of pancreatic enzymes, such as chymotrypsin and trypsin, which are affected by the most common food preservatives, sodium benzoate (E211), potassium sorbate (E202) and sorbic acid (E200), have been evaluated. The proteinase activity was analysed with a bioluminescent method using the light intensity decay constant. Our study revealed that the preservatives reduce proteinase activity by 50% (EC50) at a much lower concentration than their acceptable daily intake (ADI). Thus, sodium benzoate and sorbic acid have an inhibition effect on chymotrypsin at concentrations 14 times lower and 70 times lower than their ADI and this increases with exposure time. Food preservative consumption impacts negatively on protein digestion, which is especially dangerous for patients with pancreatitis. © 2017 Elsevier Ltd
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ranjan, Rajeev, Esimbekova, Elena N., Kratasyuk, Valentina A.
Заглавие : Rapid biosensing tools for cancer biomarkers
Колич.характеристики :13 с
Коллективы : Russian Foundation for Basic Research [16-34-60100, 16-06-00439]; state budget allocated to the fundamental research Russian Academy of Sciences Project [01201351504]
Место публикации : Biosens. Bioelectron.: ELSEVIER ADVANCED TECHNOLOGY, 2017. - Vol. 87. - С. 918-930. - ISSN 0956-5663, DOI 10.1016/j.bios.2016.09.061. - ISSN 1873-4235(eISSN)
Примечания : Cited References:115. - The research was partially supported by the Russian Foundation for Basic Research (Project no. 16-34-60100 and No. 16-06-00439), the state budget allocated to the fundamental research Russian Academy of Sciences (Project no. 01201351504).
Предметные рубрики: POINT-OF-CARE
HIGHLY SENSITIVE DETECTION
ACOUSTIC-WAVE BIOSENSOR
DNA
Ключевые слова (''Своб.индексиров.''): biosensor--cancer biomarker--functional nanomaterials--point-of-care--devices--microfluidics
Аннотация: The present review critically discusses the latest developments in the field of smart diagnostic systems for cancer biomarkers. A wide coverage of recent biosensing approaches involving aptamers, enzymes, DNA probes, fluorescent probes, interacting proteins and antibodies in vicinity to transducers such as electrochemical, optical and piezoelectric is presented. Recent advanced developments in biosensing approaches for cancer biomarker owes much credit to functionalized nanomaterials due to their unique opto-electronic properties and enhanced surface to volume ratio. Biosensing methods for a plenty of cancer biomarkers has been summarized emphasizing the key principles involved.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sachkova A. S., Kovel E. S., Churilov G. N., Guseynov O. A., Bondar A. A., Dubinina I. A., Kudryasheva N. S.
Заглавие : On mechanism of antioxidant effect of fullerenols
Место публикации : Biochem. Biophys. Rep.: Elsevier B.V., 2017. - Vol. 9. - С. 1-8. - ISSN 24055808 (ISSN) , DOI 10.1016/j.bbrep.2016.10.011
Ключевые слова (''Своб.индексиров.''): antioxidant activity--bacterial enzymes--fullerenol--hormesis--luminous marine bacteria--ultralow concentrations
Аннотация: Fullerenols are nanosized water-soluble polyhydroxylated derivatives of fullerenes, specific allotropic form of carbon, bioactive compounds and perspective pharmaceutical agents. Antioxidant activity of fullerenols was studied in model solutions of organic and inorganic toxicants of oxidative type – 1,4-benzoquinone and potassium ferricyanide. Two fullerenol preparations were tested: С60О2–4(ОН)20–24 and mixture of two types of fullerenols С60О2–4(ОН)20–24+С70О2–4(ОН)20–24. Bacteria-based and enzyme-based bioluminescent assays were used to evaluate a decrease in cellular and biochemical toxicities, respectively. Additionally, the enzyme-based assay was used for the direct monitoring of efficiency of the oxidative enzymatic processes. The bacteria-based and enzyme-based assays showed similar peculiarities of the detoxification processes: (1) ultralow concentrations of fullerenols were active (ca 10–17–10?4 and 10–17–10? 5 g/L, respectively), (2) no monotonic dependence of detoxification efficiency on fullerenol concentrations was observed, and (3) detoxification of organic oxidizer solutions was more effective than that of the inorganic oxidizer. The antioxidant effect of highly diluted fullerenol solutions on bacterial cells was attributed to hormesis phenomenon; the detoxification was concerned with stimulation of adaptive cellular response under low-dose exposures. Sequence analysis of 16S ribosomal RNA was carried out; it did not reveal mutations in bacterial DNA. The suggestion was made that hydrophobic membrane-dependent processes are involved to the detoxifying mechanism. Catalytic activity of fullerenol (10? 8 g/L) in NADH-dependent enzymatic reactions was demonstrated and supposed to contribute to adaptive bacterial response. © 2016 The Authors
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vereshchagina K. P., Lubyaga Y. A., Shatilina Z., Bedulina D., Gurkov A., Axenov-Gribanov D. V., Baduev B., Kondrateva E. S., Gubanov M., Zadereev E., Sokolova I., Timofeyev M.
Заглавие : Salinity modulates thermotolerance, energy metabolism and stress response in amphipods Gammarus lacustris
Место публикации : PeerJ: PeerJ Inc., 2016. - Vol. 2016, Is. 11. - ISSN 21678359 (ISSN) , DOI 10.7717/peerj.2657
Ключевые слова (''Своб.индексиров.''): adaptation--amphipoda--gammarus lacustris--salinity--thermal tolerance
Аннотация: Temperature and salinity are important abiotic factors for aquatic invertebrates. We investigated the influence of different salinity regimes on thermotolerance, energy metabolism and cellular stress defense mechanisms in amphipods Gammarus lacustris Sars from two populations. We exposed amphipods to different thermal scenarios and determined their survival as well as activity of major antioxidant enzymes (peroxidase, catalase, glutathione S-transferase) and parameters of energy metabolism (content of glucose, glycogen, ATP, ADP, AMP and lactate). Amphipods from a freshwater population were more sensitive to the thermal challenge, showing higher mortality during acute and gradual temperature change compared to their counterparts from a saline lake. A more thermotolerant population from a saline lake had high activity of antioxidant enzymes. The energy limitations of the freshwater population (indicated by low baseline glucose levels, downward shift of the critical temperature of aerobic metabolism and inability to maintain steady-state ATP levels during warming) was ob- served, possibly reflecting a trade-off between the energy demands for osmoregulation under the hypo-osmotic condition of a freshwater environment and protection against temperature stress. © 2016 Vereshchagina et al.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya O. A., Ronzhin N. O., Artemenko K. S., Bondar V. S.
Заглавие : Morphological properties and levels of extracellular peroxidase activity and light emission of the basidiomycete Armillaria borealis treated with beta-glucosidase and chitinase
Колич.характеристики :12 с
Коллективы : Russian Academy of Sciences [0356-2016-0709, 0356-2015-0103]
Место публикации : Mycosphere: MYCOSPHERE PRESS, 2017. - Vol. 8, Is. 4. - С. 649-+. - ISSN 2077-7000, DOI 10.5943/mycosphere/8/4/11
Примечания : Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (project no. 0356-2016-0709) and Program No. II. 2 "Integration and Development" of the Siberian Branch of the Russian Academy of Sciences (project no. 0356-2015-0103).
Предметные рубрики: FUNGAL CELL-WALL
OXIDATIVE STRESS
PHANEROCHAETE-CHRYSOSPORIUM
Ключевые слова (''Своб.индексиров.''): basidiomycetes--bioluminescence--cell wall--beta-glucosidase--chitinase--peroxidase
Аннотация: The study estimates morphological properties and levels of extracellular peroxidase activity and light emission of mycelium of the basidiomycete Armillaria borealis IBSO 2328 treated with beta-glucosidase and chitinase. Mycelium incubated with the enzymes shows considerable morphological changes and indications of osmotic shock. Injuries observed in the cell envelope of the fungal hyphae are primarily attributed to the partial (in the beta-glucosidase treatment) or complete (in the chitinase treatment) disintegration of the melanin layer on the surface of the cell wall. Changes in the cell wall of hyphae are accompanied by release of extracellular peroxidases of the fungus into the incubation medium and an increase in light emission relative to the luminescence of the control pellets. We assume that higher level of luminescence of the enzyme-treated mycelium samples could be related to the disintegration of the surface pigment layer of the hyphae and the partial loss of extracellular peroxidases. The data obtained confirm the previously proposed hypothesis in which light producing reaction of the fungus may be an additional way to neutralize active oxygen radicals under stress.
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17.

Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Sachkova A. S., Kovel E. S., Vorobeva A. A., Kudryasheva N. S.
Заглавие : Antioxidant Activity of Fullerenols. Bioluminescent Monitoring in vitro
Колич.характеристики :2 с
Коллективы : Russian Foundation for Basic Research [15-03-06786, 15-43-04377-sibir]; state budget to the fundamental research at the Russian Academy of Sciences [01201351504]
Место публикации : BIOSENSORS 2016: ELSEVIER SCIENCE BV, 2017. - Vol. 27: 26th Anniversary World Congress on Biosensors (Biosensors) (MAY 25-27, 2016, Gothenburg, SWEDEN). - С. 230-231. - (Procedia Technology). - , DOI 10.1016/j.protcy.2017.04.097
Примечания : Cited References:2. - The work was supported by the Russian Foundation for Basic Research, Grants No. 15-03-06786 and 15-43-04377-sibir; the state budget to the fundamental research at the Russian Academy of Sciences (project No 01201351504)
Ключевые слова (''Своб.индексиров.''): bioluminescence--enzymatic assay--toxicity sensor--antioxidant activity--fullerenol
Аннотация: Bioluminescence of isolated enzymes is a perspective phenomenon for biosensors development due to simplicity of registration of a physiological parameter - light intensity. Enzyme-based bioluminescent assay is widely used to evaluate a decrease in biochemical toxicities. Also the enzyme-based assay is used for the direct biochemical monitoring of oxidative toxicity. This work considers antioxidant properties of fullerenols, water-soluble polyhydroxylated derivatives of fullerenes and perspective pharmaceutical agents, in solutions of model inorganic and organic toxicants of oxidative type K-3[Fe(CN)(6)] and 1,4-benzoquinone. Two fullerenol preparations were used: C60O2-4(OH)(20-24) and mixture of two types of fullerenols C60O2-4(OH)(20-24)+C70O2-4(OH)(20-24). The enzyme-based assays showed the peculiarities of the detoxification processes: ultralow concentrations of fullerenols were active (ca 10(-17)-10(-5)g/L); no monotonic dependence of detoxification efficiency on fullerenol concentrations was observed, and detoxification of organic oxidizer solutions was more effective than that of the inorganic oxidizer. The antioxidant effects of highly diluted fullerenol solutions were attributed to hormesis phenomenon; the detoxification was concerned with stimulation of adaptive cellular response under low-dose exposures. (C) 2017 The Authors. Published by Elsevier Ltd.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Puzyr A. P., Medvedeva S. E., Artemenko K. S., Bondar V. S.
Заглавие : Luminescence of cold extracts from mycelium of luminous basidiomycetes during long-term storage
Место публикации : Curr. Res. Environ. Appl. Mycol. J. Fungal: Beijing Academy of Agriculture and Forestry Sciences, Institute of Plant and Environment Protection, 2017. - Vol. 7, Is. 3. - С. 227-235. - ISSN 22292225 (ISSN) , DOI 10.5943/cream/7/3/9
Ключевые слова (''Своб.индексиров.''): armillaria borealis--kinetics of luminescence--lyophilic preparations--mycena citricolor--neonothopanus nambi
Аннотация: Cold extracts with high activities of enzymes of luminescent reaction were prepared from mycelia of luminous fungi Armillaria borealis IBSO 2328, Mycena citricolor IBSO 2331, and Neonothopanus nambi IBSO 2391. The authors describe techniques of preparing cold extracts with high levels of luminescence from mycelial biomass of different species of luminous basidiomycetes. The investigation of cold extracts showed that in experiments with freezing and thawing of the samples as well as in experiments with lyophilization followed by dissolution of the dry samples, the levels of enzyme activity were high, with in vitro luminescence exhibited after addition of NADPH and the hot extract containing the substrate. High activity levels of the enzymes of luminescent reaction were measured in lyophilized cold extracts stored over three years. In lyophilized preparations, the enzymes of luminescent reaction had high thermostability, even when dry preparations of cold extracts were exposed to a temperature of 100°C for 60 minutes. © Beijing Academy of Agriculture and Forestry Sciences.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lukyanenko, Kirill A., Belousov, Kirill I., Denisov, Ivan A., Yakimov, Anton S., Esimbekova, Elena N., Bukatin, Anton S., Evstrapov, Anatoly A., Belobrov, Peter I.
Заглавие : Active mixing of immobilised enzymatic system in microfluidic chip
Колич.характеристики :5 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Micro Nano Lett.: INST ENGINEERING TECHNOLOGY-IET, 2017. - Vol. 12, Is. 6. - С. 377-381. - ISSN 1750-0443, DOI 10.1049/mnl.2016.0646
Примечания : Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041).
Предметные рубрики: POLY(METHYL METHACRYLATE)
SURFACE MODIFICATION
POINT
DEVICES
PMMA
Аннотация: Parameters for sample introduction, dried reagents dissolution and mixing with sample for bienzyme system NAD(H):FMN-oxidoreductase and luciferase immobilised in microfluidic chip were successfully determined. Numerical simulations of reaction chamber geometry, flavin mononucleotide (FMN) escape from starch gel and mixing options were conducted to achieve higher sensitivity of bioluminescent reaction. Results of numerical simulations were verified experimentally. The active mixer for dried reagents was made from an electro-mechanical speaker's membrane which was connected to the input of the chip. Such a mixer provided better efficiency than a passive mixing, and it is simple enough for use in point-of-care devices with any systems based on immobilised enzymes in chips.
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Purtov K. V., Petushkov V. N., Rodionova N. S., Gitelson J. I.
Заглавие : Why does the bioluminescent fungus Armillaria mellea have luminous mycelium but nonluminous fruiting body?
Место публикации : Doklad. Biochem. Biophys.: Maik Nauka Publishing / Springer SBM, 2017. - Vol. 474, Is. 1. - С. 217-219. - ISSN 16076729 (ISSN) , DOI 10.1134/S1607672917030176
Аннотация: By determining the components involved in the bioluminescence process in luminous and nonluminous organs of the honey fungus Armillaria mellea, we have established causes of partial luminescence of this fungus. The complete set of enzymes and substrates required for bioluminescence is formed only in the mycelium and only under the conditions of free oxygen access. Since the synthesis of luciferin precursor (hispidin) and 3-hydroxyhispidin hydroxylase in the fruiting bodies is blocked, the formation of luciferin—the key component of fungal bioluminescent system—was not observed. That is why the fruiting body of Armillaria mellea is nonluminous despite the presence of luciferase, the enzyme that catalyzes the oxidation of luciferin with a photon emission. © 2017, Pleiades Publishing, Ltd.
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