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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786 / T. G. Volova [et al.] // Applied Biochemistry and Microbiology. - 2004. - Vol. 40, Is. 2. - P170-177, DOI 10.1023/B:ABIM.0000018921.04863.d5 . - ISSN 0003-6838
Кл.слова (ненормированные):
acetyl coenzyme A acyltransferase -- bacterial enzyme -- carbon -- carbon dioxide -- fructose -- hydrogen -- hydroxybutyrate dehydrogenase -- oxidoreductase -- poly(3 hydroxybutyric acid) -- polyhydroxyalkanoic acid -- synthetase -- article -- bacterial metabolism -- carbon source -- catalysis -- controlled study -- degradation -- depolymerization -- enzyme activity -- enzyme analysis -- molecular dynamics -- nonhuman -- protein function -- Ralstonia eutropha -- recording -- statistical significance -- synthesis -- Bacteria (microorganisms) -- Ralstonia -- Wautersia eutropha
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (?-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of ?-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha / T. G. Volova [и др.] // Prikladnaia biokhimiia i mikrobiologiia. - 2004. - Vol. 40, Is. 2. - С. 201-209 . - ISSN 0555-1099
Кл.слова (ненормированные):
acetoacetyl coenzyme a reductase -- acetoacetyl-CoA reductase -- acetyl coenzyme A acyltransferase -- acyltransferase -- alcohol dehydrogenase -- carboxylesterase -- hydroxybutyrate dehydrogenase -- hydroxybutyric acid -- poly(3 hydroxyalkanoic acid) depolymerase -- poly(3-hydroxyalkanoic acid) depolymerase -- poly(3-hydroxyalkanoic acid) synthase -- polyhydroxyalkanoate synthase -- polymer -- article -- chemistry -- comparative study -- culture medium -- enzymology -- growth, development and aging -- metabolism -- Wautersia eutropha -- Acetyl-CoA C-Acyltransferase -- Acyltransferases -- Alcohol Oxidoreductases -- Carboxylic Ester Hydrolases -- Culture Media -- Cupriavidus necator -- Hydroxybutyrate Dehydrogenase -- Hydroxybutyrates -- Polymers
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of the key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHA synthase, D-hydroxybutyrate dehydrogenase, and PHA depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHA synthase were recorded at the stage of acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only at stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not cause any marked changes in the time course of enzyme activity.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036 Russia. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786 [Text] / T. G. Volova [et al.] // Appl. Biochem. Microbiol. - 2004. - Vol. 40, Is. 2. - P. 170-177, DOI 10.1023/B:ABIM.0000018921.04863.d5. - Cited References: 27 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
POLY-BETA-HYDROXYBUTYRATE
   ORGANISM ALCALIGENES-EUTROPHUS
   ESCHERICHIA-COLI
   PHB
   POLY(3-HYDROXYBUTYRATE)
   BIOSYNTHESIS
   CLONING
   GENES
   CHAIN
   H16
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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    Isolation, Study and Application of Organosolv Lignins / B. N. Kuznetsov [и др.] // J. Sib. Fed. Univ.-Chem. - 2016. - Vol. 9, Is. 4. - С. 454-482, DOI 10.17516/1998-2836-2016-9-4-454-482. - Cited References:137 . - ISSN 1998-2836. - ISSN 2313-6049
Рубрики:
SIZE-EXCLUSION CHROMATOGRAPHY
   MOLECULAR-WEIGHT DISTRIBUTION
Кл.слова (ненормированные):
organosolv lignin -- isolation -- structure -- catalytic depolymerization -- molecular weight -- application -- liquid hydrocarbons -- aerogels
Аннотация: The analysis of the literature on the methods of soluble organosolv lignins isolation, their physical-chemical study and on the method of their processing to porous aerogels and liquid hydrocarbons was carried out. A review of the literature allowed us to choice of the most important areas of research. For isolation from wood the soluble lignins free from sulfur the methods of catalytic peroxide delignification at mild conditions (temperature <= 100 degrees C, atmospheric pressure) and methods of lignin extraction by supercritical organic solvents were used. Molecular mass and molecular-mass distribution of ethanol-lignin samples isolated from aspenwood and abies-wood were studied by gel-permeation chromatography. Weighted molecular mass of ethanol-lignin from abies wood is 478 Da and that from aspen wood ethanol-lignin - 750 Da. Thus, the studied samples of ethanol-lignin have rather low molecular mass, what should facilitate their further processing to liquid hydrocarbons and aerogels. For the depolymerization of organosolv lignins to liquid hydrocarbons the processes of their catalytic conversion in supercritical alcohols have good prospects for the use. In the processes of lignin thermal conversion alcohols can to extract the products of lignin depolymerization and to alkylate these products, preventing their repolymerization to high molecular mass substances. To obtain a new class of nanoporous materials based on lignin the methods of organic aerogels synthesis from mixtures of lignin with other natural polymers and crosslinking agents were applied. It was found that the structure and properties of porous materials of aerogel type depend not only from the reaction mixture composition but from the method of drying. Drying in subcritical conditions leads to the formation of xerogels, in supercritical conditions - to the formation aerogels and the freezdrying - of cryogels. Obtained porous materials can have very low density (around 0.2 g/cm(3)), high specific surface area (to 500 m(2)/g) and the pore volume near 5 cm(3)/g.

WOS,
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Держатели документа:
FRC Krasnoyarsk Sci Ctr SB RAS, Inst Chem & Chem Technol SB RAS, 50-24 Akademgorodok, Krasnoyarsk 660036, Russia.
FRC Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Univ Lorraine, CNRS, UMR 7198, Inst Jean Lamour,ENSTIB, 27 Rue Philippe Seguin,CS 60036, F-88026 Epinal, France.

Доп.точки доступа:
Kuznetsov, Boris N.; Malyar, Yuriy N.; Kuznetsova, Svetlana A.; Grishechko, Lyudmila I.; Kazachenko, Alexander S.; Levdansky, Alexander V.; Pestunov, Andrey V.; Boyandin, Anatoly N.; Celzard, Alan

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