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A new enzymatic technique to estimate the efficiency of microbial degradation of pollutants [Text] / A. B. Sarangova, L. A. Somova ; ed. RM Wheeler [et al.] // LIFE SCIENCES: LIFE SUPPORT SYSTEMS STUDIES-I. Ser. ADVANCES IN SPACE RESEARCH : PERGAMON PRESS LTD, 1997. - Vol. 20: F4.6, F4.8, F4.2 and F4.9 Symposia of COSPAR Scientific Commission F on Life Sciences - Life Support System Studies-I, at the 31st COSPAR Scientific Assembly (JUL 14-SEP 21, 1996, BIRMINGHAM, ENGLAND), Is. 10. - P. 2049-2052, DOI 10.1016/S0273-1177(97)00940-X. - Cited References: 4 . - ISBN 0273-1177. - ISBN 0-08-043307-3

РУБ Engineering, Aerospace + Astronomy & Astrophysics + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences

Аннотация: Dynamics of active sludge microorganism activity in aerotanks under chemostat conditions has been studied. Dependence of microorganism catalase activity has been found to depend on residual substrate concentration in proportion to the biomass of microorganisms. Experimental data and field observations has formed the basis to develop a technique to evaluate in relative units the amount of the substrate consumed by biocenosis of the active sludge in the air tanks of purification facilities. (C) 1997 COSPAR. Published by Elsevier Science Ltd.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sarangova, A.B.; Somova, L.A.; Wheeler, RM \ed.\; Garland, JL \ed.\; Tibbitts, TW \ed.\; Nielsen, SS \ed.\

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A new enzymatic technique to estimate the efficiency of microbial degradation of pollutants / A. B. Sarangova, L. A. Somova // Advances in Space Research. - 1997. - Vol. 20, Is. 10. - P2049-2052 . - ISSN 0273-1177
Кл.слова (ненормированные):
catalase -- hydrogen peroxide -- aerobic metabolism -- article -- bacterium -- biomass -- bioremediation -- enzymology -- metabolism -- methodology -- microbiology -- sewage -- waste management -- water management -- Aerobiosis -- Bacteria -- Biodegradation, Environmental -- Biomass -- Catalase -- Hydrogen Peroxide -- Sewage -- Waste Management -- Water Microbiology -- Water Purification
Аннотация: Dynamics of active sludge microorganism activity in aerotanks under chemostat conditions has been studied. Dependence of microorganism catalase activity has been found to depend on residual substrate concentration in proportion to the biomass of microorganisms. Experimental data and field observations has formed the basis to develop a technique to evaluate in relative units the amount of the substrate consumed by biocenosis of the active sludge in the air tanks of purification facilities. В© 1997 COSPAR. Published by Elsevier Science Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Krasnoyarsk 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sarangova, A.B.; Somova, L.A.

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Active mixing of immobilised enzymatic system in microfluidic chip / K. A. Lukyanenko [et al.] // Micro Nano Lett. - 2017. - Vol. 12, Is. 6. - P377-381, DOI 10.1049/mnl.2016.0646. - Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041). . - ISSN 1750-0443

РУБ Nanoscience & Nanotechnology + Materials Science, Multidisciplinary
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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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ITMO Univ, St Petersburg 197101, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, Kirill A.; Belousov, Kirill I.; Denisov, Ivan A.; Yakimov, Anton S.; Esimbekova, Elena N.; Bukatin, Anton S.; Evstrapov, Anatoly A.; Belobrov, Peter I.; Russian Science Foundation [15-19-10041]

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Analytical Enzymatic Reactions in Microfluidic Chips / K. A. Lukyanenko [et al.] // Appl. Biochem. Microbiol. - 2017. - Vol. 53, Is. 7. - P775-780, DOI 10.1134/S0003683817070043. - Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041). . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
BIOAVAILABLE HEAVY-METALS
   DEVICES
   POINT
   LAB
Кл.слова (ненормированные):
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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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
St Petersburg Inst Fine Mech & Opt, St Petersburg 197101, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
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.; Russian Science Foundation [15-19-10041]

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Antioxidant Activity and Toxicity of Fullerenols via Bioluminescence Signaling: Role of Oxygen Substituents / E. S. Kovel [et al.] // Int J Mol Sci. - 2019. - Vol. 20, Is. 9, DOI 10.3390/ijms20092324 . - ISSN 1422-0067
Кл.слова (ненормированные):
antioxidant activity -- bioactive compound -- bioluminescence bioassay -- fullerenol -- reactive oxygen species -- toxicity
Аннотация: Fullerenols are nanosized water-soluble polyhydroxylated derivatives of fullerenes, a specific allotropic form of carbon, bioactive compounds, and perspective basis for drug development. Our paper analyzes the antioxidant activity and toxicity of a series of fullerenols with different number of oxygen substituents. Two groups of fullerenols were under investigation: (1) C60Oy(OH)x, C60,70Oy(OH)x, where x + y = 24-28 and (2) C60,70Oy(OH)x, Fe0,5C60Oy(OH)x, Gd@C82Oy(OH)x, where x + y = 40-42. Bioluminescent cellular and enzymatic assays (luminous marine bacteria and their enzymatic reactions, respectively) were applied to monitor toxicity in the model fullerenol solutions and bioluminescence was applied as a signaling physiological parameter. The inhibiting concentrations of the fullerenols were determined, revealing the fullerenols' toxic effects. Antioxidant fullerenol' ability was studied in solutions of model oxidizer, 1,4-benzoquinone, and detoxification coefficients of general and oxidative types (DGT and DOxT) were calculated. All fullerenols produced toxic effect at high concentrations (>0.01 g L-1), while their antioxidant activity was demonstrated at low and ultralow concentrations (<0.001 g L-1). Quantitative toxic and antioxidant characteristics of the fullerenols (effective concentrations, concentration ranges, DGT, and DOxT) were found to depend on the number of oxygen substituents. Lower toxicity and higher antioxidant activity were determined in solutions of fullerenols with fewer oxygen substituents (x + y = 24-28). The differences in fullerenol properties were attributed to their catalytic activity due to reversible electron acceptance, radical trapping, and balance of reactive oxygen species in aqueous solutions. The results provide pharmaceutical sciences with a basis for selection of carbon nanoparticles with appropriate toxic and antioxidant characteristics. Based on the results, we recommend, to reduce the toxicity of prospective endohedral gadolinium-fullerenol preparations Gd@C82Oy(OH)x, decreasing the number of oxygen groups to x + y = 24-28. The potential of bioluminescence methods to compare toxic and antioxidant characteristics of carbon nanostructures were demonstrated.

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Держатели документа:
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Physics SB RAS, Krasnoyarsk, 660036, Russian Federation
National Research Tomsk Polytechnic University, Tomsk, 634050, Russian Federation
Institute of Physics SB RAS, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Kovel, E. S.; Sachkova, A. S.; Vnukova, N. G.; Churilov, G. N.; Knyazeva, E. M.; Kudryasheva, N. S.

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Antioxidant Activity of Fullerenols. Bioluminescent Monitoring in vitro / A. S. Sachkova [et al.] ; ed.: A. . Turner, A. . Tang // BIOSENSORS 2016 : ELSEVIER SCIENCE BV, 2017. - Vol. 27: 26th Anniversary World Congress on Biosensors (Biosensors) (MAY 25-27, 2016, Gothenburg, SWEDEN). - P230-231. - (Procedia Technology), DOI 10.1016/j.protcy.2017.04.097. - 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) . -

РУБ Engineering, Biomedical

Кл.слова (ненормированные):
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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Держатели документа:
Natl Res Tomsk Polytech Univ, Lenin Ave 30, Tomsk 634050, Russia.
SB RAS, Inst Biophys, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny Pr 79, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Sachkova, A. S.; Kovel, E. S.; Vorobeva, A. A.; Kudryasheva, N. S.; Turner, A... \ed.\; Tang, A... \ed.\; 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]

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Antioxidant activity of humic substances via bioluminescent monitoring in vitro [Text] / A. S. Tarasova, D. I. Stom, N. S. Kudryasheva // Environ. Monit. Assess. - 2015. - Vol. 187, Is. 3. - Ст. 89, DOI 10.1007/s10661-015-4304-1. - Cited References:51. - This work was supported by the Russian Foundation for Basic Research, Grant No. 15-03-06786a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1. . - ISSN 0167-6369. - ISSN 1573-2959

РУБ Environmental Sciences
Рубрики:
DETOXIFICATION PROCESSES
   TOXICITY
   BIOASSAYS
   BACTERIA
   ASSAY
Кл.слова (ненормированные):
Antioxidant activity -- Oxidative toxicity -- General toxicity -- Humic -- substances -- Bioassay -- Bioluminescence
Аннотация: This work considers antioxidant properties of natural detoxifying agents-humic substances (HS) in solutions of model inorganic and organic compounds of oxidative nature-complex salt K-3[Fe(CN)(6)] and 1,4-benzoquinone. Bioluminescent system of coupled enzymatic reactions catalyzed by NAD(P) H:FMN-oxidoreductase and bacterial luciferase was used as a bioassay in vitro to monitor toxicity of the oxidizer solutions. Toxicities of general and oxidative types were evaluated using bioluminescent kinetic parameters-bioluminescence intensity and induction period, respectively. Antioxidant activity of HS was attributed to their ability to decrease both general and oxidative toxicities; the HS antioxidant efficiency was characterized with detoxification coefficients D-GT and D-OxT, respectively. Dependencies of D-GT and D-OxT on HS concentration and time of preliminary incubation of the oxidizers with HS were demonstrated. The optimal conditions for detoxification of the oxidizers were >20-min incubation time and 0.5x10(-4) to 2x10(-4) M of HS concentration. The present study promotes application of the enzymatic luminescent bioassay to monitor toxicity of pollutants of oxidative nature in environmental and waste waters in remediation procedures.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Irkutsk State Univ, Irkutsk 664003, Russia.
ИБФ СО РАН

Доп.точки доступа:
Tarasova, A.S.; Stom, D.I.; Kudryasheva, N.S.; Russian Foundation for Basic Research [15-03-06786a]; Russian Academy of Sciences [VI 57.1.1]

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Application of bioluminescent enzymatic method for assessment of the state of the soil [Text] / N. . Rimatskaia [et al.] // Luminescence. - 2014. - Vol. 29. - P76-77. - Cited References: 0 . - ISSN 1522-7235. - ISSN 1522-7243

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Держатели документа:
[Rimatskaia, Nadezhda
Baigina, Elizaveta
Kazanceva, Marina
Kratasyuk, Valentina] Siberian Fed Univ, Krasnoyarsk, Russia
[Kratasyuk, Valentina] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
[Stom, Devard] Irkutsk State Univ, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rimatskaia, N...; Baigina, E...; Kazanceva, M...; Stom, D...; Kratasyuk, V...

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Application of Enzyme Bioluminescence in Ecology [Text] / E. Esimbekova, V. Kratasyuk, O. Shimomura // Adv. Biochem. Eng. Biotechnol. : SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - P67-109. - (Advances in Biochemical Engineering-Biotechnology), DOI 10.1007/978-3-662-43385-0_3. - Cited References:85 . -

РУБ Biotechnology & Applied Microbiology
Рубрики:
BACTERIAL LUCIFERASE
   IN-VITRO
   PYRETHROID INSECTICIDES
   FRESH-WATER
Кл.слова (ненормированные):
Bioluminescence -- Ecological monitoring -- Enzymatic assay -- Immobilization -- Integral water toxicity -- Luciferase
Аннотация: This review examines the general principles of bioluminescent enzymatic toxicity bioassays and describes the applications of these methods and the implementation in commercial biosensors. Bioluminescent enzyme system technology (BEST) has been proposed in the bacterial coupled enzyme system, wherein NADH: FMN-oxidoreductase-luciferase substitutes for living organisms. BEST was introduced to facilitate and accelerate the development of cost-competitive enzymatic systems for use in biosensors for medical, environmental, and industrial applications. For widespread use of BEST, the multicomponent reagent "Enzymolum'' has been developed, which contains the bacterial luciferase, NADH: FMN-oxidoreductase, and their substrates, co-immobilized in starch or gelatin gel. Enzymolum is the central part of Portable Laboratory for Toxicity Detection (PLTD), which consists of a biodetector module, a sampling module, a sample preparation module, and a reagent module. PLTD instantly signals chemical-biological hazards and allows us to detect a wide range of toxic substances. Enzymolum can be integrated as a biological module into the portable biodetector-biosensor originally constructed for personal use. Based on the example of Enzymolum and the algorithm for creating new enzyme biotests with tailored characteristics, a new approach was demonstrated in biotechnological design and construction. The examples of biotechnological design of various bioluminescent methods for ecological monitoring were provided. Possible applications of enzyme bioassays are seen in the examples for medical diagnostics, assessment of the effect of physical load on sportsmen, analysis of food additives, and in practical courses for higher educational institutions and schools. The advantages of enzymatic assays are their rapidity (the period of time required does not exceed 3-5 min), high sensitivity, simplicity and safety of procedure, and possibility of automation of ecological monitoring; the required luminometer is easily available.

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Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ИБФ СО РАН

Доп.точки доступа:
Esimbekova, Elena; Kratasyuk, Valentina; Shimomura, Osamu

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10.

Applications of Luminous Bacteria Enzymes in Toxicology [Text] / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959, DOI 10.2174/1386207318666150917100257. - Cited References:88. - The research was supported by the Russian Science Foundation, project No. 15-19-10041. . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
NADHFMN-OXIDOREDUCTASE-LUCIFERASE
HUMIC SUBSTANCES
BIOLUMINESCENT
Кл.слова (ненормированные):
Bioluminescence -- bioluminescent toxicity enzymatic assay -- immobilization -- of enzymes -- luciferase -- total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH: FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Esimbekova, Elena N.; Russian Science Foundation [15-19-10041]

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11.

Applications of luminous bacteria enzymes in toxicology / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescence -- Bioluminescent toxicity enzymatic assay -- Immobilization of enzymes -- Luciferase -- Total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH:FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation
Photobiology Laboratory, Russian Academy of Sciences, Siberian Branch, Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kratasyuk, V. A.; Esimbekova, E. N.

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12.

Biological activity of carbonic nano-structures—comparison via enzymatic bioassay / A. S. Sachkova [et al.] // J. Soils Sed. - 2018, DOI 10.1007/s11368-018-2134-9 . - Article in press. - ISSN 1439-0108
Кл.слова (ненормированные):
Antioxidant activity -- Bioactive compounds -- Fullerenol -- Humic substances -- Reactive oxygen species -- Toxicity
Аннотация: Purpose: The aim of the work is to compare the biological activity of carbonic nano-structures of natural and artificial origination, namely, humic substances (HS) and fullerenols. Materials and methods: The representative of the fullerenol group, С60Оy(OH)x where у + x = 20–22, was chosen. Enzyme-based luminescent bioassay was applied to evaluate toxicity and antioxidant properties of HS and fullerenol (F); chemiluminescent luminol method was used to study a content of reactive oxygen species (ROS) in the solutions. Toxicity of the bioactive compounds was evaluated using effective concentrations ЕС50; detoxification coefficients DOxT were applied to study and compare antioxidant activity of the compounds. Antioxidant activity and ranges of active concentrations of the bioactive compounds were determined in model solutions of organic and inorganic oxidizers—1,4-benzoquinone and potassium ferricianide. Results and discussion: Values of ЕС50 revealed higher toxicity of HS than F (0.005 and 0.108 g L?1, respectively); detoxifying concentrations of F were found to be lower. Antioxidant ability of HS was demonstrated to be time-dependent; the 50-min preliminary incubation in oxidizer solutions was suggested as optimal for the detoxification procedure. On the contrary, F’ antioxidant effect demonstrated independency on time. Antioxidant effect of HS did not depend on amphiphilic characteristics of the media (values of DOxT were 1.3 in the solutions of organic and inorganic oxidizers), while this of F was found to depend: it was maximal (DOxT = 2.0) in solutions of organic oxidizer, 1,4-benzoquinone. Conclusions: Both HS and F demonstrated toxicity and low-concentration antioxidant ability; however, quantitative characteristics of their effects were different. The differences were explained with HS polyfunctionality, higher ability to decrease ROS content, non-rigidity, and diffusion restrictions in their solutions. Antioxidant effect of the bioactive compounds was presumably attributed to catalytic redox activity of their ?-fragments. The paper demonstrates a high potential of luminescent enzymatic bioassay to study biological activity of nano-structures of natural and artificial origination. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.

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Держатели документа:
National Research Tomsk Polytechnic University, Tomsk, 634050, Russian Federation
Institute of Biophysics FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Physics FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Irkutsk National Research Technical University, Irkutsk, 664074, Russian Federation

Доп.точки доступа:
Sachkova, A. S.; Kovel, E. S.; Churilov, G. N.; Stom, D. I.; Kudryasheva, N. S.

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13.

Bioluminescence chemistry of fireworm Odontosyllis / A. A. Kotlobay [et al.] // Proc. Natl. Acad. Sci. U. S. A. - 2019. - Vol. 116, Is. 38. - P18911-18916, DOI 10.1073/pnas.1902095116. - Cited References:16. - We thank the late Dr. Shoji Inoue and Dr. Hisae Kakoi (Meijo University) for providing Odontosyllis materials, Sergey Shakhov for photography, and Drs. Mikhail Baranov and Andrey Mikhaylov for discussions. Some experiments were carried out using equipment provided by the Institute of Bioorganic Chemistry of the Russian Academy of Sciences.ore Facility. Some experiments were supported by Planta LLC. Structural and mechanistic studies were supported by Russian Science Foundation Grant 18-74-10102. Isolation, purification, and biochemical studies were supported by Russian Science Foundation Grant 16-14-00052p. B.R.B. acknowledges support from the Air Force Office of Scientific Research (FA9550-18-1-0017). . - ISSN 0027-8424

РУБ Multidisciplinary Sciences
Рубрики:
MECHANISM
DECARBOXYLATION
OXIDATION
Кл.слова (ненормированные):
bioluminescence -- Odontosyllis luciferin -- oxyluciferin -- heterocycles
Аннотация: Marine polychaetes Odontosyllis undecimdonta, commonly known as fireworms, emit bright blue-green bioluminescence. Until the recent identification of the Odontosyllis luciferase enzyme, little progress had been made toward characterizing the key components of this bioluminescence system. Here we present the biomolecular mechanisms of enzymatic (leading to light emission) and nonenzymatic (dark) oxidation pathways of newly described O. undecimdonta luciferin. Spectral studies, including 1D and 2D NMR spectroscopy, mass spectrometry, and X-ray diffraction, of isolated substances allowed us to characterize the luciferin as an unusual tricyclic sulfur-containing heterocycle. Odontosyllis luciferin does not share structural similarity with any other known luciferins. The structures of the Odontosyllis bioluminescent system's low molecular weight components have enabled us to propose chemical transformation pathways for the enzymatic and nonspecific oxidation of luciferin.

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Держатели документа:
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi 141701, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.
Russian Acad Sci, AN Nesmeyanov Inst Organoelement Cpds, Moscow 119991, Russia.
Natl Res Ctr, Kurchatov Inst, Moscow 123182, Russia.
St Petersburg Natl Res Acad Univ, Russian Acad Sci, St Petersburg 194021, Russia.
Connecticut Coll, New London, CT 06320 USA.
European Mol Biol Lab Hamburg, D-22603 Hamburg, Germany.
Chubu Univ, Dept Environm Biol, Kasugai, Aichi 4878501, Japan.

Доп.точки доступа:
Kotlobay, Alexey A.; Dubinnyi, Maxim A.; Purtov, Konstantin V.; Guglya, Elena B.; Rodionova, Natalja S.; Petushkov, Valentin N.; Bolt, Yaroslav V.; Kublitski, Vadim S.; Kaskova, Zinaida M.; Ziganshin, Rustam H.; Nelyubina, Yulia V.; Dorovatovskii, Pavel V.; Eliseev, Igor E.; Branchini, Bruce R.; Bourenkov, Gleb; Ivanov, Igor A.; Oba, Yuichi; Yampolsky, Ilia V.; Tsarkova, Aleksandra S.; Kaskova, Zinaida; Russian Science FoundationRussian Science Foundation (RSF) [18-74-10102, 16-14-00052p]; Air Force Office of Scientific ResearchUnited States Department of DefenseAir Force Office of Scientific Research (AFOSR) [FA9550-18-1-0017]

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14.

Bioluminescent Enzymatic Assay as a Tool for Studying Antioxidant Activity and Toxicity of Bioactive Compounds / N. S. Kudryasheva [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P536-540, DOI 10.1111/php.12639. - Cited References:40. - The work was supported by the Russian Foundation for Basic Research, Grants 15-03-06786 and 15-43-04377-sibir; the state budget allocated to the fundamental research at the Russian Academy of Sciences (project 01201351504). . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
LUMINOUS MARINE-BACTERIA
HUMIC SUBSTANCES
DETOXIFICATION PROCESSES
Аннотация: A bioluminescent assay based on a system of coupled enzymatic reactions catalyzed by bacterial luciferase and NADH:FMN-oxidoreductase was developed to monitor toxicity and antioxidant activity of bioactive compounds. The assay enables studying toxic effects at the level of biomolecules and physicochemical processes, as well as determining the toxicity of general and oxidative types. Toxic and detoxifying effects of bioactive compounds were studied. Fullerenols, perspective pharmaceutical agents, nanosized particles, water-soluble polyhydroxylated fullerene-60 derivatives were chosen as bioactive compounds. Two homologous fullerenols with different number and type of substituents, C60O2-4(OH)(20-24) and Fe0.5C60(OH) O-x(y) (x + y = 40-42), were used. They suppressed bioluminescent intensity at concentrations 0.01 g L-1 and 0.001 g L-1 for C60O2-4(OH)(20-24) and Fe0.5C60(OH)(x)O-y, respectively; hence, a lower toxicity of C60O2-4(OH)(20-24) was demonstrated. Antioxidant activity of fullerenols was studied in model solutions of organic and inorganic oxidizers; changes in toxicities of general and oxidative type were determined; detoxification coefficients were calculated. Fullerenol C60O2-4(OH)(20-24) revealed higher antioxidant ability at concentrations 10(-17)-10(-5) g L-1. The difference in the toxicity and antioxidant activity of fullerenols was explained through their electron donor/acceptor properties and different catalytic activity. Principles of bioluminescent enzyme assay application for evaluating the toxic effect and antioxidant activity of bioactive compounds were summarized and the procedure steps were described.

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Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Natl Res Tomsk Polytech Univ, Tomsk, Russia.
Inst Phys SB RAS, Krasnoyarsk, Russia.

Доп.точки доступа:
Kudryasheva, Nadezhda S.; Kovel, Ekaterina S.; Sachkova, Anna S.; Vorobeva, Anna A.; Isakova, Viktoriya G.; Churilov, Grigoriy N.; Russian Foundation for Basic Research [15-03-06786, 15-43-04377-sibir]; Russian Academy of Sciences [01201351504]

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15.

Bioluminescent Enzymatic Methods for Toxicological Safety Testing of Food Additives [Text] / A. . Asanova, E. . Esimbekova, V. . Kratasyuk // Luminescence. - 2014. - Vol. 29. - P74-74. - Cited References: 4 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
ASSAY

WOS
Держатели документа:
[Asanova, Anastasiia
Esimbekova, Elena
Kratasyuk, Valentina] Siberian Fed Univ, Krasnoyarsk, Russia
[Esimbekova, Elena
Kratasyuk, Valentina] Inst Biophys SB RAS, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Asanova, A...; Esimbekova, E...; Kratasyuk, V...

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16.

Bioluminescent enzyme inhibition-based assay for the prediction of toxicity of pollutants in urban soils / E. M. Kolosova, O. S. Sutormin, L. V. Stepanova [et al.] // Environ. Technol. Innov. - 2021. - Vol. 24. - Ст. 101842, DOI 10.1016/j.eti.2021.101842 . - ISSN 2352-1864
Кл.слова (ненормированные):
Bioassay -- Bioluminescence -- Industrial contamination -- Soil pollution -- Urbostratozems -- Arsenic -- Chemical analysis -- Enzyme activity -- Enzyme inhibition -- Fluorine compounds -- Soil surveys -- Soil testing -- Soils -- Toxicity -- Arsenic concentration -- Chemical and biologicals -- Comprehensive information -- Contaminated soils -- Environmental assessment methods -- Enzymatic bioassays -- Luminescent bacteria -- Sample preparation -- Soil pollution
Аннотация: There is a need for rapid simple and informative environmental assessment methods. The present investigation is aimed at assessing the possibility of using the combined enzyme system of luminescent bacteria: NAD(P)H:FMN-oxidoreductase + luciferase (Red + Luc) for predicting the potential toxicity of industrial urbostratozems sampled in the city of Krasnoyarsk. Three groups of urbostratozems polluted with fluorine, arsenic and lead, were tested by the methods of chemical analysis and enzymatic bioassay. Only the assessment of the arsenic-contaminated soil samples showed the dependence between the reduced activity of the enzyme system and the arsenic concentration variations. The results reveal that the sensitivity of the Red + Luc enzyme system to the soil pollutants depends on the properties of the studied soil samples. Moreover, the solubility of lead in the soil samples affects the accuracy of the enzymatic bioassays for soil toxicity testing. The results of the enzymatic bioassay of the fluoride-contaminated soil samples are ambiguous. The obtained data show the relevance of the sample preparation during integral bioassays. In addition, soil properties should be taken into account as well. The current study emphasizes the importance of conducting chemical and biological testing as a combined set to obtain comprehensive information about the anthropogenic load. © 2021 Elsevier B.V.

Scopus
Держатели документа:
Department of Biophysics, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Krasnoyarsk Agricultural Research Institute, Federal Research Center ‘Krasnoyarsk Science Center Siberian Branch of the Russian Academy of Sciences’, Krasnoyarsk, 660036, Russian Federation
Department of Aquatic and Terrestrial Ecosystems, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Photobiology Laboratory, Institute of Biophysics, Federal Research Center ‘Krasnoyarsk Science Center Siberian Branch of the Russian Academy of Sciences’, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kolosova, E. M.; Sutormin, O. S.; Stepanova, L. V.; Shpedt, A. A.; Rimatskaya, N. V.; Sukovataya, I. E.; Kratasyuk, V. A.

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17.

РУБ Biotechnology & Applied Microbiology + Engineering, Environmental
Рубрики:
FLUORIDE
   BIOASSAYS
   POLLUTION
   METALS
   WATER
Кл.слова (ненормированные):
Urbostratozems -- Soil pollution -- Industrial contamination -- Bioassay -- Bioluminescence
Аннотация: There is a need for rapid simple and informative environmental assessment methods. The present investigation is aimed at assessing the possibility of using the combined enzyme system of luminescent bacteria: NAD(P)H:FMN-oxidoreductase + luciferase (Red + Luc) for predicting the potential toxicity of industrial urbostratozems sampled in the city of Krasnoyarsk. Three groups of urbostratozems polluted with fluorine, arsenic and lead, were tested by the methods of chemical analysis and enzymatic bioassay. Only the assessment of the arsenic-contaminated soil samples showed the dependence between the reduced activity of the enzyme system and the arsenic concentration variations. The results reveal that the sensitivity of the Red + Luc enzyme system to the soil pollutants depends on the properties of the studied soil samples. Moreover, the solubility of lead in the soil samples affects the accuracy of the enzymatic bioassays for soil toxicity testing. The results of the enzymatic bioassay of the fluoride-contaminated soil samples are ambiguous. The obtained data show the relevance of the sample preparation during integral bioassays. In addition, soil properties should be taken into account as well. The current study emphasizes the importance of conducting chemical and biological testing as a combined set to obtain comprehensive information about the anthropogenic load. (C) 2021 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
Siberian Fed Univ, Dept Biophys, 79 Svobodny St, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Krasnoyarsk Agr Res Inst, Fed Res Ctr Krasnoyarsk Sci Ctr Siberian Branch, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Dept Aquat & Terr Ecosyst, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Photobiol Lab, Inst Biophys, Fed Res Ctr `Krasnoyarsk Sci Ctr Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Kolosova, Elizaveta M.; Sutormin, Oleg S.; Stepanova, L. V.; Shpedt, Aleksandr A.; Rimatskaya, N. V.; Sukovataya, Irina E.; Kratasyuk, Valentina A.; Russian Foundation for Basic Research, the Government of the Krasnoyarsk Region, Russia; Krasnoyarsk Regional Foundation for Supporting Scientific and Technological Activities, Russia [18-47-240005]; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]

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18.

Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class [Text] / S. . Bauer [et al.] // J. Mol. Biol. - 2004. - Vol. 339, Is. 4. - P. 967-979, DOI 10.1016/j.jmb.2004.04.034. - Cited References: 66 . - ISSN 0022-2836

РУБ Biochemistry & Molecular Biology
Рубрики:
GTP CYCLOHYDROLASE-I
   GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE
   6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE
   ESCHERICHIA-COLI
   DIHYDRONEOPTERIN ALDOLASE
   FOLIC-ACID
   ENZYMATIC SYNTHESIS
   DIHYDROPTEROATE SYNTHASE
   REACTION-MECHANISM
   3-DIMENSIONAL STRUCTURE
Кл.слова (ненормированные):
tetrahydrofolate biosynthesis -- aldolase classes -- retroaldol reaction -- purin binding -- Schiff base
Аннотация: Dihydroneopterin aldolase (DHNA) catalyses a retroaldol reaction yielding 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin, tetrahydrofolate. The enzyme is a potential target for antimicrobial and anti-parasite chemotherapy. A gene specifying a dihydroneopterin aldolase from Arabidopsis thaliana was expressed in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity and crystallised using polyethylenglycol as the precipitating agent. The crystal structure was solved by X-ray diffraction analysis at 2.2 Angstrom resolution. The enzyme forms a D-4-symmetric homo-octamer. Each polypeptide chain is folded into a single domain comprising an antiparallel four-stranded beta-sheet and two long alpha-helices. Four monomers are arranged in a tetrameric ring, and two of these rings form a hollow cylinder. Well defined purine derivatives are found at all eight topologically equivalent active sites. The subunit fold of the enzyme is related to substructures of dihydroneopterin triphosphate epimerase, GTP cyclohydrolase I, and pyruvoyltetrahydropterin synthase, which are all involved in the biosynthesis of pteridine type cofactors, and to urate oxidase, although some members of that superfamily have no detectable sequence similarity Due to structural and mechanistical differences of DHNA in comparison with class I and class II aldolases, a new aldolase class is proposed. (C) 2004 Elsevier Ltd. All rights reserved.

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Держатели документа:
Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
Tech Univ Munich, Lehrstuhl Organ Chem & Biochem, D-85747 Garching, Germany
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bauer, S...; Schott, A.K.; Illarionova, V...; Bacher, A...; Huber, R...; Fischer, M...

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19.

Design of bioluminescent biosensors for assessing contamination of complex matrices / E. N. Esimbekova, V. P. Kalyabina, K. V. Kopylova [et al.] // Talanta. - 2021. - Vol. 233. - Ст. 122509, DOI 10.1016/j.talanta.2021.122509. - Cited By :1 . - ISSN 0039-9140
Кл.слова (ненормированные):
Bioluminescent biosensor -- Complex matrices -- Enzyme inhibition-based assay -- Heavy metals -- Pesticides
Аннотация: The presence of potentially toxic xenobiotics in complex matrices has become rather the rule than the exception. Therefore, there is a need for highly sensitive inexpensive techniques for analyzing environmental and food matrices for toxicants. Enzymes are selectively sensitive to various toxic compounds, and, thus, they can be used as the basis for detection of contaminants in complex matrices. There are, however, a number of difficulties associated with the analysis of complex matrices using enzyme assays, including the necessity to take into account properties and effects of the natural components of the test media for accurate interpretation of results. The present study describes the six-stage procedure for designing new enzyme sensors intended for assessing the quality of complex matrices. This procedure should be followed both to achieve the highest possible sensitivity of the biosensor to potentially toxic substances and to minimize the effect of the uncontaminated components of complex mixtures on the activity of the biosensor. The proposed strategy has been tested in designing a bioluminescent biosensor for integrated rapid assessment of the safety of fruits and vegetables. The biosensor is based on the coupled enzyme system NAD(P)H:FMN-oxidoreductase and luciferase as the biorecognition element. The study describes methods and techniques for attaining the desired result in each stage. The proposed six-stage procedure for designing bioluminescent enzyme biosensors can be used to design the enzymatic biosensors based on other enzymes. © 2021 Elsevier B.V.

Scopus
Держатели документа:
Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Kalyabina, V. P.; Kopylova, K. V.; Torgashina, I. G.; Kratasyuk, V. A.

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20.

Design of bioluminescent biosensors for assessing contamination of complex matrices / E. N. Esimbekova, V. P. Kalyabina, K. V. Kopylova [et al.] // Talanta. - 2021. - Vol. 233. - Ст. 122509, DOI 10.1016/j.talanta.2021.122509. - Cited References:87. - The reported study was funded by Russian Foundation for Basic Research, Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, to the research project No. 20-44-242001 and Ministry of Science and Higher Education of Russian Federation No. FSRZ-2020-0006. . - ISSN 0039-9140. - ISSN 1873-3573

РУБ Chemistry, Analytical
Рубрики:
SAMPLE PREPARATION
   PESTICIDES
   FOOD
   BIOMOLECULES
   SENSITIVITY
Кл.слова (ненормированные):
Bioluminescent biosensor -- Enzyme inhibition-based assay -- Complex -- matrices -- Pesticides -- Heavy metals
Аннотация: The presence of potentially toxic xenobiotics in complex matrices has become rather the rule than the exception. Therefore, there is a need for highly sensitive inexpensive techniques for analyzing environmental and food matrices for toxicants. Enzymes are selectively sensitive to various toxic compounds, and, thus, they can be used as the basis for detection of contaminants in complex matrices. There are, however, a number of difficulties associated with the analysis of complex matrices using enzyme assays, including the necessity to take into account properties and effects of the natural components of the test media for accurate interpretation of results. The present study describes the six-stage procedure for designing new enzyme sensors intended for assessing the quality of complex matrices. This procedure should be followed both to achieve the highest possible sensitivity of the biosensor to potentially toxic substances and to minimize the effect of the uncontaminated components of complex mixtures on the activity of the biosensor. The proposed strategy has been tested in designing a bioluminescent biosensor for integrated rapid assessment of the safety of fruits and vegetables. The biosensor is based on the coupled enzyme system NAD(P)H:FMN-oxidoreductase and luciferase as the biorecognition element. The study describes methods and techniques for attaining the desired result in each stage. The proposed six-stage procedure for designing bioluminescent enzyme biosensors can be used to design the enzymatic biosensors based on other enzymes.

WOS
Держатели документа:
Siberian Fed Univ, 79 Svobodny Prospect, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Esimbekova, Elena N.; Kalyabina, Valeriya P.; Kopylova, Kseniya, V; Torgashina, Irina G.; Kratasyuk, Valentina A.; Kopylova, Kseniya; Esimbekova, Elena; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR); Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science [20-44-242001]; Ministry of Science and Higher Education of Russian Federation [FSRZ-2020-0006]

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