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Handheld Enzymatic Luminescent Biosensor for Rapid Detection of Heavy Metals in Water Samples / K. A. Lukyanenko [et al.] // Chemosensors. - 2019. - Vol. 7, Is. 1. - Ст. 16, DOI 10.3390/chemosensors7010016. - Cited References:39. - This research was funded by Russian Foundation for Basic Research, Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, to the research project #18-44-242003: "Designing an enzyme reagent for bioluminescent analysis: mechanisms for increasing sensitivity and accuracy". . - ISSN 2227-9040

РУБ Chemistry, Analytical
Рубрики:
ON-A-CHIP
   SILICON PHOTOMULTIPLIER
   OPTICAL BIOSENSORS
   CELL
Кл.слова (ненормированные):
chemical measurements -- silicon photomultiplier -- optical biosensor -- bioassay -- microfluidics -- luciferase -- bioluminescence
Аннотация: Enzymatic luminescent systems are a promising tool for rapid detection of heavy metals ions for water quality assessment. Nevertheless, their widespread use is limited by the lack of test procedure automation and available sensitive handheld luminometers. Herein we describe integration of disposable microfluidic chips for bioluminescent enzyme-inhibition based assay with a handheld luminometer, which detection system is based on a thermally stabilized silicon photomultiplier (SiPM). Microfluidic chips were made of poly(methyl methacrylate) by micro-milling method and sealed using a solvent bonding technique. The composition of the bioluminescent system in microfluidic chip was optimized to achieve higher luminescence intensity and storage time. Results indicate that developed device provided comparable sensitivity with bench-scale PMT-based commercial luminometers. Limit of detection for copper (II) sulfate reached 2.5 mg/L for developed biosensor. Hereby we proved the concept of handheld enzymatic optical biosensors with disposable chips for bioassay. The proposed biosensor can be used as an early warning field-deployable system for rapid detection of heavy metals salts and other toxic chemicals, which affect bioluminescent signal of enzymatic reaction.

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Держатели документа:
SB RAS, Krasnoyarsk Sci Ctr, Fed Res Ctr, Lab Digital Controlled Drugs & Theranost, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia.
Krasnoyarsk State Med Univ, Res Inst Mol Med & Pathobiochem, Krasnoyarsk 660022, Russia.
SB RAS, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lukyanenko, Kirin A.; Denisov, Ivan A.; Sorokin, Vladimir V.; Yakimov, Anton S.; Esimbekova, Elena N.; Belobrov, Peter, I; Lukyanenko, Kirill; Russian Foundation for Basic Research, Government of Krasnoyarsk Territory [18-44-242003]

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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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Role of Hsp90 and ATP in modulating apyrase activity and firefly luciferase kinetics / M. A. Kirillova [et al.] // Int. J. Biol. Macromol. - 2019. - Vol. 131. - P691-696, DOI 10.1016/j.ijbiomac.2019.03.110 . - ISSN 0141-8130
Кл.слова (ненормированные):
Bioluminescence -- Heat shock protein 90 -- High-throughput screening -- adenosine triphosphate -- apyrase -- bovine serum albumin -- firefly luciferase -- heat shock protein 90 -- stabilizing agent -- Article -- bioluminescence -- clinical study -- conformation -- controlled study -- denaturation -- enzyme activity -- enzyme kinetics -- high throughput screening -- incubation time -- nonhuman -- protein protein interaction -- protein refolding -- temperature -- thermal denaturation -- time
Аннотация: The present manuscript describes a novel bioassay consisting of apyrase and heat shock protein 90 (Hsp90) without additional co-chaperone supplementation; intended for high-throughput screening of anti-cancer drugs and prognosis of stress. In this regard, Hsp90 and adenosine 5?-triphosphate (ATP) mediated firefly luciferase (FLuc) kinetics was investigated using apyrase and FLuc as client proteins. Bioluminescent assay containing Hsp90, ATP, and apyrase led to complete loss of luminescence at 50 °C which indicates the protective role of Hsp90 against thermal denaturation. Similarly, the assay sample comprising Hsp90, ATP, and FLuc showed 2 fold increments in luminescence than their counterparts. Introduction of bovine serum albumin (BSA) to the pre-incubated assay mixture led to an initial rise in the luminescence (28%) in comparison to the sample containing Hsp90, ATP and FLuc. Therefore, FLuc based HTS assays are not suitable for clinical samples which may contain stabilizing agents. However, thermally denatured FLuc and apyrase could not regain their active conformation even when Hsp90 and ATP were introduced in the assay system. This observation justifies the role of Hsp90 to be protective rather than a reparation agent when acts without co-chaperones. © 2019

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Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kirillova, M. A.; Ranjan, R.; Esimbekova, E. N.; Kratasyuk, V. A.

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Nanodiamonds as an effective adsorbent for immobilization of extracellular peroxidases from luminous fungus Neonothopanus nambi to construct a phenol detection system / O. Mogilnaya [et al.] // Biocatal. Biotransform. - 2019. - Vol. 37, Is. 2. - P97-105, DOI 10.1080/10242422.2018.1472586. - 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]. . - ISSN 1024-2422. - ISSN 1029-2446

РУБ Biochemistry & Molecular Biology + Biotechnology & Applied Microbiology
Рубрики:
CARBON NANOTUBES
   ARMILLARIA-BOREALIS
   LIGHT-EMISSION
   DEGRADATION
Кл.слова (ненормированные):
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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Держатели документа:
RAS, Inst Biophys, Fed Res Ctr, Krasnoyarsk Sci Ctr,SB, Krasnoyarsk, Russia.

Доп.точки доступа:
Mogilnaya, Olga; Ronzhin, Nikita; Artemenko, Karina; Bondar, Vladimir; Russian Academy of Sciences [0356-2016-0709]

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

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

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

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Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
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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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Vysotski, E. S.

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Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase / O. S. Sutormin [et al.] // Mol. Cat. - 2018. - Vol. 458. - P60-66, DOI 10.1016/j.mcat.2018.08.012 . - ISSN 2468-8231
Кл.слова (ненормированные):
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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Держатели документа:
Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Sutormin, O. S.; Sukovataya, I. E.; Pande, S.; Kratasyuk, V. A.

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Detection of Hispidin by a Luminescent System from Basidiomycete Armillaria borealis / A. P. Puzyr [et al.] // Dokl. Biochem. Biophys. - 2018. - Vol. 480, Is. 1. - P173-176, DOI 10.1134/S1607672918030146. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ANTIOXIDANT
MUSHROOM
Аннотация: In in vitro experiments, the possibility of using a luminescent system extracted from the luminous fungus Armillaria borealis has been shown to detect and determine the concentration of hispidin. A linear dependence of the luminescent response on the content of hispidin in solutions in the concentration range of 5.4 x 10(-5) - 1.4 x 10(-2) mu M was detected. The stability of the enzyme system and the high sensitivity of the bioluminescent reaction allows carrying out multiple measurements with the analyte detection limit of 1.3 x 10(-11) g. The obtained results show the prospects of creating a rapid bioluminescent method for the analysis of medical substances or extracts from various biological objects for the presence of hispidin.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Res Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Siberian Branch, Inst Computat Technol, Krasnoyarsk 660049, Russia.
Russian Acad Sci, Siberian Branch, Voevodsky Inst Chem Kinet & Combust, Novosibirsk 630090, Russia.

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Burov, A. E.; Zernov, Yu. P.; Bondar, V. S.

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Monitoring of Low-Intensity Exposures via Luminescent Bioassays of Different Complexity: Cells, Enzyme Reactions, and Fluorescent Proteins / N. S. Kudryasheva, E. S. Kovel // Int J Mol Sci. - 2019. - Vol. 20, Is. 18. - Ст. 4451, DOI 10.3390/ijms20184451 . - ISSN 1422-0067
Кл.слова (ненормированные):
antioxidant activity -- bacterial cells, enzymes -- bioactive compounds -- fluorescent protein -- hormesis -- low-intensity factors -- luminescence bioassays -- radiation
Аннотация: The current paper reviews the applications of luminescence bioassays for monitoring the results of low-intensity exposures which produce a stimulative effect. The impacts of radioactivity of different types (alpha, beta, and gamma) and bioactive compounds (humic substances and fullerenols) are under consideration. Bioassays based on luminous marine bacteria, their enzymes, and fluorescent coelenteramide-containing proteins were used to compare the results of the low-intensity exposures at the cellular, biochemical, and physicochemical levels, respectively. High rates of luminescence response can provide (1) a proper number of experimental results under comparable conditions and, therefore, proper statistical processing, with this being highly important for "noisy" low-intensity exposures; and (2) non-genetic, i.e., biochemical and physicochemical mechanisms of cellular response for short-term exposures. The results of cellular exposures were discussed in terms of the hormesis concept, which implies low-dose stimulation and high-dose inhibition of physiological functions. Dependencies of the luminescence response on the exposure time or intensity (radionuclide concentration/gamma radiation dose rate, concentration of the bioactive compounds) were analyzed and compared for bioassays of different organization levels.

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Держатели документа:
Institute of Biophysics, Federal Research Center "Krasnoyarsk Science Center, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Physics, Federal Research Center "Krasnoyarsk Science Center, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kudryasheva, N. S.; Kovel, E. S.

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10.

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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11.

Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties / N. O. Ronzhin, O. A. Mogilnaya, K. S. Artemenko [et al.] // Dokl. Biochem. Biophys. - 2020. - Vol. 490, Is. 1. - P38-42, DOI 10.1134/S1607672920010135. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PEROXIDASE-ACTIVITY
LIGHT-EMISSION
Кл.слова (ненормированные):
extracellular oxidases -- basidiomycete Neonothopanus nambi -- beta-glucosidase -- gel-filtration chromatography -- veratryl alcohol -- phenol -- FAD
Аннотация: Using the original technique of treating biomass with beta-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80-85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K-m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K-m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22-35 and 55-70 degrees C, and pH optimums are 6 and 5, respectively.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci, Inst Biophys,Fed Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Ronzhin, N. O.; Mogilnaya, O. A.; Artemenko, K. S.; Posokhina, E. D.; Bondar, V. S.

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12.

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

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

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

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13.

Enzymatic bioassay of soil: Sensitivity comparison of mono-, double- And triple-enzyme systems to soil toxicants / O. S. Sutormin [и др.] // Tsitologiya. - 2018. - Vol. 60, Is. 10. - С. 826-829, DOI 10.7868/S0041377118100132 . - ISSN 0041-3771
Кл.слова (ненормированные):
Bacterial luciferase -- Bioluminescent analysis -- Coupled enzyme systems -- Ecological monitoring -- Enzymatic toxicity bioassays -- Lactate dehydrogenase -- NADH:FMN-oxidoreductase -- Soil
Аннотация: In this paper, we have investigated the possibilities of application of enzymatic systems with increasing chain length as a bioassay to evaluate the soil contamination status. The sensitivity of monoenzyme reaction as well as double- and triple-enzyme chains based on NAD(P)H:FMN-oxidoreductase and luciferase of luminous bacteria and lactate dehydrogenase to pesticides and copper ions in water and water extracts from soils were estimated. For this, the toxicological parameter IC 20 reflecting the sensitivity limit of the enzyme system to the to-xicant was used. It was revealed that elongation of the coupled enzyme chain (from mono- to triple-enzyme) increases the sensitivity of the bioassay, in some cases by several orders of magnitude. This pattern can be used as a tool to improve the properties of enzymic bioassays. The effect of extracts from uncontaminated soils of various types on enzymatic systems also differs, which makes possible to design the specialized enzymatic bioassays as well. © 2018 Sankt Peterburg.All rights reserved.

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

Доп.точки доступа:
Sutormin, O. S.; Kolosova, E. M.; Nemtseva, A. V.; Iskorneva, I. V.; Lisitsa, A. A.; Matvienko, V. S.; Esimbekova, A. N.; Kratasyuk, V. A.

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14.

Extracellular peroxidase activity and light emission of the mycelium of the basidiomycete neonothopanus nambi in the presence of ?-glucosidase / O. A. Mogilnaya, N. O. Ronzhin, V. S. Bondar // Biophysics. - 2018. - Vol. 63, Is. 1. - P93-99, DOI 10.1134/S0006350918010104 . - ISSN 0006-3509
Кл.слова (ненормированные):
Basidiomycetes -- Cell wall -- Luminescence -- Peroxidase -- ?-glucosidase
Аннотация: A comparative evaluation of the level of extracellular peroxidase activity and light-emission intensity of the mycelium of the luminescent basidiomycete Neonothopanus nambi in the presence of ?-glucosidase was performed. The enzyme activity damages the hyphae of the fungus leading to osmotic imbalance, partial degradation of the mycelium, and release of extracellular peroxidases into the incubation medium. The presence of ?-glucosidase reduces the time necessary to reach the maximum luminescence. Putative biochemical mechanisms that underlie the stimulation of reactive oxygen species formation (first and foremost, of hydrogen peroxide) in the N. nambi mycelium in the presence of ?-glucosidase are proposed. © O.A. Mogilnaya, N.O. Ronzhin, V.S. Bondar and Pleiades Publishing, Inc., 2018.

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Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Mogilnaya, O. A.; Ronzhin, N. O.; Bondar, V. S.

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15.

Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria / A. A. Deeva [et al.] // Proteins. - 2019. - Vol. 87, Is. 9. - P723-729, DOI 10.1002/prot.25696. - 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 . - ISSN 0887-3585. - ISSN 1097-0134

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ESCHERICHIA-COLI
FLAVIN OXIDOREDUCTASE
CRYSTAL-STRUCTURE
Кл.слова (ненормированные):
bacterial bioluminescence -- Fre -- functional divergence -- gene duplication -- LuxG -- NAD(P)H -- flavin-oxidoreductase
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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Держатели документа:
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Svobodny Prosp 79, Krasnoyarsk 660041, Russia.
RAS, Inst Cell Biophys, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia.
State Inst Informat Technol & Telecommun SIIT & T, Dept Appl Res Informatizat, Moscow, Russia.
RAS, Fed Res Ctr, Krasnoyarsk Sci Ctr SB, Lab Photobiol,Inst Biophys SB, Krasnoyarsk, Russia.

Доп.точки доступа:
Deeva, Anna A.; Zykova, Evgenia A.; Nemtseva, Elena V.; Kratasyuk, Valentina A.; Nemtseva, Elena; 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]

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16.

Principles for Construction of Bioluminescent Enzyme Biotests for Analysis of Complex Media / V. P. Kalyabina [et al.] // Dokl. Biochem. Biophys. - 2019. - Vol. 485, Is. 1. - P107-110, DOI 10.1134/S1607672919020042. - Cited References:10. - The study was supported by the Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science and RFBR (project no. 18-44-242003). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
VEGETABLES
ELEMENTS
Аннотация: In this study, we formulated the principles of designing bioluminescent enzyme tests for assessing the quality of complex media, which consist in providing the maximum sensitivity to potentially toxic chemicals at a minimal impact of uncontaminated complex media. The developed principles served as a basis for designing a new bioluminescent method for an integrated rapid assessment of chemical safety of fruits and vegetables, which is based on using the luminous bacteria enzymes (NAD(P)H:FMN oxidoreductase and luciferase) as a test system.

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

Доп.точки доступа:
Kalyabina, V. P.; Esimbekova, E. N.; Torgashina, I. G.; Kopylova, K. V.; Kratasyuk, V. A.; Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science; RFBR [18-44-242003]

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17.

Bioluminescent assay for toxicological assessment of nanomaterials / E. N. Esimbekova [et al.] // Dokl. Biochem. Biophys. - 2017. - Vol. 472, Is. 1. - P60-63, DOI 10.1134/S1607672917010173. - Cited References:15. - We are sincerely grateful to the staff of the Institute of Physiological Active Compounds (Kharkiv, Ukraine) for providing fullerene samples. This study was supported by the Russian Science Foundation (project no. 16-14-10115). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
LUMINOUS BACTERIA
TOXICITY
Аннотация: A new method for assessing biotoxicity of nanomaterials, based on the use of soluble bioluminescent coupled enzyme system NAD(P)ai...H:FMN oxidoreductase and luciferase, is proposed. The results of this study indicate a significant adverse biological effect exerted by nanoparticles at the molecular level. It was found that the most toxic nanoparticles the nanoparticles are based on copper and copper oxide, as well as single-walled carbon nanotubes and multi-walled carbon nanofibers, which are referred to hazard class II.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Krasnoyarsk State Agr Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Esimbekova, E. N.; Nemtseva, E. V.; Kirillova, M. A.; Asanova, A. A.; Kratasyuk, V. A.; Russian Science Foundation [16-14-10115]

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18.

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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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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19.

Mechanism and color modulation of fungal bioluminescence / Z. M. Kaskova [et al.] // Sci. Adv. - 2017. - Vol. 3, Is. 4. - Ст. e1602847, DOI 10.1126/sciadv.1602847. - Cited References:40. - This work was supported by the Sao Paulo Research Foundation [FAPESP grants 10/11578-5 (to A.G.O.), 13/16885-1 (to C.V.S.), 14/14866-2 (to E.L.B.), 13/07914-8 (to E.P. and F.A.D.), and 2012/12663-1 (to P.D.M.) and CEPID Redoxoma 2013/07937-8 (to P.D.M.)], the National Council for Scientific and Technological Development (CNPq) [301307/2013-0 (to P.D.M.)], NAP Redoxoma (PRPUSP) [2011.1.9352.1.8. (to P.D.M.)], the Japan Society for the Promotion of Science Grants-in-Aid for Scientific Research (KAKENHI) [grant no. 16K07715 (to Y.O.)], Chubu University [grant AII28II M01 (to Y.O.)], and the Russian Science Foundation (grant 16-14-00052 to all Russian authors). . - ISSN 2375-2548

РУБ Multidisciplinary Sciences
Рубрики:
SINGLET MOLECULAR-OXYGEN
QUANTUM YIELDS
CHEMILUMINESCENCE
Аннотация: Bioluminescent fungi are spread throughout the globe, but details on their mechanism of light emission are still scarce. Usually, the process involves three key components: an oxidizable luciferin substrate, a luciferase enzyme, and a light emitter, typically oxidized luciferin, and called oxyluciferin. We report the structure of fungal oxyluciferin, investigate the mechanism of fungal bioluminescence, and describe theuseof simple synthetic alpha-pyrones as luciferins to produce multicolor enzymatic chemiluminescence. A high-energy endoperoxide is proposed as an intermediate of the oxidation of the native luciferin to the oxyluciferin, which is a pyruvic acid adduct of caffeic acid. Luciferase promiscuity allows the use of simple alpha-pyrones as chemiluminescent substrates.

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Держатели документа:
Russian Acad Sci, Inst Bioorgan Chem, Miklukho Maklaya 16-10, Moscow 117997, Russia.
Pirogov Russian Natl Res Med Univ, OStrovitianov 1, Moscow 117997, Russia.
SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Univ Sao Paulo, Fac Ciencias Farmaceut, Dept Anal Clin & Toxicolgicas, BR-05508900 Sao Paulo, Brazil.
Nagoya Univ, Grad Sch Bioagr Sci, Nagoya, Aichi 4648601, Japan.
Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-05508900 Sao Paulo, Brazil.
Univ Sao Paulo, Inst Quim, Dept Quim Fundamental, BR-05508900 Sao Paulo, Brazil.
Univ Sao Paulo, Inst Oceanografico, Dept Oceanografia Fis Quim & Geol, BR-05508120 Sao Paulo, Brazil.
Chubu Univ, Dept Environm Biol, Kasugai, Aichi 4878501, Japan.

Доп.точки доступа:
Kaskova, Zinaida M.; Dorr, Felipe A.; Petushkov, Valentin N.; Purtov, Konstantin V.; Tsarkova, Aleksandra S.; Rodionova, Natalja S.; Mineev, Konstantin S.; Guglya, Elena B.; Kotlobay, Alexey; Baleeva, Nadezhda S.; Baranov, Mikhail S.; Arseniev, Alexander S.; Gitelson, Josef I.; Lukyanov, Sergey; Suzuki, Yoshiki; Kanie, Shusei; Pinto, Ernani; Di Mascio, Paolo; Waldenmaier, Hans E.; Pereira, Tatiana A.; Carvalho, Rodrigo P.; Oliveira, Anderson G.; Oba, Yuichi; Bastos, Erick L.; Stevani, Cassius V.; Yampolsky, Ilia V.; Sao Paulo Research Foundation [FAPESP] [10/11578-5, 13/16885-1, 14/14866-2, 13/07914-8, 2012/12663-1]; CEPID Redoxoma [2013/07937-8]; National Council for Scientific and Technological Development (CNPq) [301307/2013-0]; NAP Redoxoma (PRPUSP) [2011.1.9352.1.8]; Japan Society for the Promotion of Science [16K07715]; Chubu University [AII28II M01]; Russian Science Foundation [16-14-00052]

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20.

Inhibition effect of food preservatives on endoproteinases / E. N. Esimbekova [et al.] // Food Chem. - 2017. - Vol. 235. - P294-297, DOI 10.1016/j.foodchem.2017.05.059 . - ISSN 0308-8146
Кл.слова (ненормированные):
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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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation
Siberian Federal University, Institute of Fundamental Biology and Biotechnology, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Institute of Agro-ecological Technologies, Krasnoyarsk, Russian Federation

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

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