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The synthesis of hydroxybutyrate and hydroxyvalerate copolymers by the bacterium Ralstonia eutropha / T. G. Volova, G. S. Kalacheva // Mikrobiologiya. - 2005. - Vol. 74, Is. 1. - С. 63-69 . - ISSN 0026-3656
Кл.слова (ненормированные):
?-ketothiolase -- Controlled synthesis -- Poly(hydroxybutyrate-co-hydroxyvalerate) -- Ralstonia eutropha -- Bacteria (microorganisms) -- Cupriavidus necator -- acetoacetyl coenzyme a -- acetyl coenzyme A acyltransferase -- acyl coenzyme A -- acyltransferase -- butyric acid derivative -- carbon dioxide -- fructose -- hydrogen -- poly(3 hydroxybutyrate) co (3 hydroxyvalerate) -- poly(3-hydroxyalkanoic acid) synthase -- poly(3-hydroxybutyrate)-co-(3-hydroxyvalerate) -- polyester -- polyhydroxyalkanoate synthase -- valeric acid derivative -- article -- chemistry -- crystallization -- culture medium -- metabolism -- Wautersia eutropha -- Acetyl-CoA C-Acyltransferase -- Acyl Coenzyme A -- Acyltransferases -- Butyrates -- Carbon Dioxide -- Crystallization -- Culture Media -- Cupriavidus necator -- Fructose -- Hydrogen -- Polyesters -- Valerates
Аннотация: The paper deals with the study of the synthesis of 3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV) copolymers by the bacterium Ralstonia eutropha B-5786 grown under different carbon nutrition conditions (growth on carbon dioxide, fructose, and CO2-valerate and fructose-valerate mixtures). The parameters to be analyzed included the yield of biomass, the yield, synthesis rate, and composition of copolymers, the activity of the key enzymes of polyhydroxyalkanoate (PHA) synthesis (?-ketothiolase, acetoacetyl-CoA reductase, and PHA synthase), the maximum tolerable concentration of valerate to the bacterium, and the conditions that govern the incorporation of hydroxyvalerate to copolymers. This allowed the relationship between cultivation conditions and the proportion of monomers in the copolymers to be deduced. We were able to synthesize a range of 3HB/3HV copolymers and found that the thermal characteristics and the degree of crystallinity of these copolymers depend on the molar fraction of 3HV.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.

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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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Autotrophic synthesis of polyhydroxyalkanoates by the bacteria Ralstonia eutropha in the presence of carbon monoxide / T. G. Volova, G. S. Kalacheva, O. V. Altukhova // Applied Microbiology and Biotechnology. - 2002. - Vol. 58, Is. 5. - P675-678, DOI 10.1007/s00253-002-0941-8 . - ISSN 0175-7598
Кл.слова (ненормированные):
3 hydroxybutyric acid -- acetoacetyl coenzyme a reductase -- acetyl coenzyme A acyltransferase -- beta hydroxyvalerate -- butyrate dehydrogenase -- carbon monoxide -- electrolyte -- hydrogen -- oxidoreductase -- poly(3 hydroxybutyric acid) -- poly(3 hydroxybutyric acid)synthase -- polyhydroxyalkanoic acid -- polymer -- unclassified drug -- valeric acid -- bacterium -- article -- autotrophy -- bacterial growth -- bacterial strain -- biomass production -- controlled study -- crystallization -- enzyme activity -- molecular weight -- nonhuman -- synthesis -- temperature -- Wautersia eutropha -- Carbon Monoxide -- Culture Media -- Cupriavidus necator -- Fatty Acids -- Lipids -- Polyesters -- Bacteria (microorganisms) -- Negibacteria -- Ralstonia -- Wautersia eutropha
Аннотация: It has been found that the carbon monoxide (CO)-resistant strain of the hydrogen bacteria Ralstonia eutropha B5786 is able to synthesise polyhydroxy-alkanoates (PHAs) in the presence of CO under autotrophic conditions. This strain, grown on model gas mixtures containing 5-25% CO (v/v), accumulates up to 70-75% (of absolutely dry matter) PHA, without significant variation in the yield coefficient on hydrogen. No suppression of the activities of the key enzymes of PHA synthesis (?-ketothiolase, acetoacetyl-CoA-reductase, butyrate dehydrogenase and poly-3-hydroxybutyrate synthase) was recorded. The PHA synthesised is a copolymer containing mostly ?-hydroxybutyrate (more than 99 mol%) with trace amounts of ?-hydroxyvalerate. The investigated properties of the polymer (molecular weight, crystallinity, temperature characteristics) do not differ from those of the polymer synthesised on electrolytic hydrogen.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Altukhova, O.V.

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