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  • Propionate fermentation  (3)
  • Sulfate-reducing bacterium  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Metabolic pathways and energetics of the acetone-oxidizing, sulfate-reducing bacterium, Desulfobacterium cetonicum (1995)
    Springer
    Archives of microbiology 163 (1995), S. 188-194 
    Details
    ISSN: 1432-072X
    Keywords: Anaerobic degradation ; Acetone ; Carboxylation ; Energetics ; Sulfate-reducing bacterium ; Desulfobacterium cetonicum ; Citric acid cycle ; Glyoxylate cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Acetone degradation by cell suspensions of Desulfobacterium cetonicum was CO2-dependent, indicating initiation by a carboxylation reaction. Degradation of butyrate was not CO2-dependent, and acetate accumulated at a ratio of 1 mol acetate per mol butyrate degraded. In cultures grown on acetone, no CoA transfer apparently occurred, and no acetate accumulated in the medium. No CoA-ligase activities were detected in cell-free crude extracts. This suggested that the carboxylation of acetone to acetoacetate, and its activation to acetoacetyl-CoA may occur without the formation of free acetoacetate. Acetoacetyl-CoA was thiolytically cleaved to two acetyl-CoA, which were oxidized to CO2 via the acetyl-CoA/carbon monoxide dehydrogenase pathway. The measured intracellular acyl-CoA ester concentrations allowed the calculation of the free energy changes involved in the conversion of acetone to acetyl-CoA. At in vivo concentrations of reactants and products, the initial steps (carboxylation and activation) must be energy-driven, either by direct coupling to ATP, or coupling to transmembrane gradients. The ΔG′ of acetone conversion to two acetyl-CoA at the expense of the energetic equivalent of one ATP was calculated to lie very close to 0kJ (mol acetone)-1. Assimilatory metabolism was by an incomplete citric acid cycle, lacking an activity oxidatively decarboxylating 2-oxoglutarate. The low specific activities of this cycle suggested its probable function in anabolic metabolism. Succinate and glyoxylate were formed from isocitrate by isocitrate lyase. Glyoxylate thus formed was condensed with acetyl-CoA to form malate, functioning as an anaplerotic sequence. A glyoxylate cycle thus operates in this strictly anaerobic bacterium. Phosphoenolpyruvate (PEP) carboxykinase formed PEP from oxaloacetate. No pyruvate kinase activity was detected. PEP presumably served as a precursor for polyglucose formation and other biosyntheses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305352
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  • 2
    Electronic Resource
    Electronic Resource
    Slostridium homopropionicum sp. nov., a new strict anaerobe growing with 2-, 3-, or 4-hydroxybutyrate (1990)
    Springer
    Archives of microbiology 154 (1990), S. 342-348 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium homopropionicum sp. nov. ; Clostridium propionicum ; α-Dehydration ; γ-Dehydration ; Butyrate fermentation ; Propionate fermentation ; Bioenergetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From anoxic sewage sludge a new strictly anaerobic, spore-forming bacterium was isolated with 2-hydroxybutyrate as sole substrate. 2-, 3-, and 4-hydroxybutyrate, 4-chlorobutyrate, crotonate, vinylacetate, and pyruvate were fermented to acetate and butyrate. Fructose was converted to acetate, butyrate, butanol, and H2. Lactate and acrylate were fermented to acetate and propionate. Cells pregrown with lactate fermented 2-hydroxybutyrate to butyrate, propionate and acetate. No inorganic electron acceptors were reduced. The DNA base ratio was 32.0±1.0 mol % and was similar to that of Clostridium propionicum, which was determined to be 35.3±0.5 mol %. Strain LuHBu1 is described as type strain of a new species, Clostridium homopropionicum sp. nov. Another isolate obtained from marine sediment degraded 2-and 3-hydroxybutyrate to acetate and butyrate and was in some respects similar to the known species Ilyobacter polytropus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276529
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  • 3
    Electronic Resource
    Electronic Resource
    Propionate acts as carboxylic group acceptor in aspartate fermentation by Propionibacterium freudenreichii (1990)
    Springer
    Archives of microbiology 155 (1990), S. 46-51 
    Details
    ISSN: 1432-072X
    Keywords: Aspartate fermentation ; Transcarboxylase ; Decarboxylases ; Anaerobic cocultures ; Propionate fermentation ; Succinate fermentation ; Propionibacterium freudenreichii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells of Propionibacterium freudenreichii ssp. shermanii and ssp. freudenreichii did not show significant growth or product formation in a mineral medium with 10 mM aspartate or 10 mM fumarate, vitamins, and a small amount (0.05% w/v) of yeast extract. In the presence of added propionate, growth with aspartate or fumarate was possible, and depended strictly on the amount of propionate provided, according to the equation: 3 aspartate + propionate → 3 succinate + acetate + CO2+3 NH3. Cocultures of P. freudenreichii with the succinate-decarboxylating strain Ft2 converted 3 aspartate stoichiometrically to acetate and 2 propionate. High activity of methylmalonyl-CoA: pyruvate transcarboxylase, and lack of methylmalonyl-CoA decarboxylase and oxaloacetate decarboxylase activity in cell-free extracts of aspartate-grown cells indicated that failure to use aspartate as sole substrate was due to the inability of these strains to catalyze a net decarboxylation of C4-dicarboxylic acids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00291273
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  • 4
    Electronic Resource
    Electronic Resource
    A new 3-hydroxybutyrate fermenting anaerobe, Ilyobacter polytropus, gen. nov. sp. nov., possessing various fermentation pathways (1984)
    Springer
    Archives of microbiology 140 (1984), S. 139-146 
    Details
    ISSN: 1432-072X
    Keywords: Ilyobacter polytropus gen. nov. sp. nov. genus and species description ; Anaerobic degradation ; 3-Hydroxybutyrate ; Butyrate fermentation ; Propionate fermentation ; Ethanol fermentation ; Glycerol degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From marine anoxic mud, a new strictly anaerobic, Gram-negative, non-sporeforming bacterium was isolated with 3-hydroxybutyrate as substrate. 3-Hydroxybutyrate and crotonate were fermented to acetate and butyrate. Glycerol was fermented to 1,3-propanediol and 3-hydroxypropionate. Acetate and formate were the only products of pyruvate or citrate fermentation. Glucose and fructose were fermented to acetate, formate and ethanol. Malate and fumarate were fermented to acetate, formate and propionate. Neither sulfate, sulfur, nor nitrate was reduced. The DNA base ratio was 32.2±0.5 mol% guanine plus cytosine. Strain CuHbu1 is described as type strain of a new genus and species, Ilyobacter polytropus gen. nov. sp. nov., in the family Bacteroidaceae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454916
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  • 5
    Electronic Resource
    Electronic Resource
    Metabolic pathways and energetics of the acetone-oxidizing, sulfate-reducing bacterium, Desulfobacterium cetonicum (1995)
    Springer
    Archives of microbiology 163 (1995), S. 188-194 
    Details
    ISSN: 1432-072X
    Keywords: Key words Anaerobic degradation ; Acetone ; Carboxylation ; Energetics ; Sulfate-reducing bacterium ; Desulfobacterium cetonicum ; Citric acid cycle ; Glyoxylate cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Acetone degradation by cell suspensions of Desulfobacterium cetonicum was CO2-dependent, indicating initiation by a carboxylation reaction. Degradation of butyrate was not CO2-dependent, and acetate accumulated at a ratio of 1 mol acetate per mol butyrate degraded. In cultures grown on acetone, no CoA transfer apparently occurred, and no acetate accumulated in the medium. No CoA-ligase activities were detected in cell-free crude extracts. This suggested that the carboxylation of acetone to acetoacetate, and its activation to acetoacetyl-CoA may occur without the formation of free acetoacetate. Acetoacetyl-CoA was thiolytically cleaved to two acetyl-CoA, which were oxidized to CO2 via the acetyl-CoA/carbon monoxide dehydrogenase pathway. The measured intracellular acyl-CoA ester concentrations allowed the calculation of the free energy changes involved in the conversion of acetone to acetyl-CoA. At in vivo concentrations of reactants and products, the initial steps (carboxylation and activation) must be energy-driven, either by direct coupling to ATP, or coupling to transmembrane gradients. The ΔG' of acetone conversion to two acetyl-CoA at the expense of the energetic equivalent of one ATP was calculated to lie very close to 0 kJ (mol acetone)–1. Assimilatory metabolism was by an incomplete citric acid cycle, lacking an activity oxidatively decarboxylating 2-oxoglutarate. The low specific activities of this cycle suggested its probable function in anabolic metabolism. Succinate and glyoxylate were formed from isocitrate by isocitrate lyase. Glyoxylate thus formed was condensed with acetyl-CoA to form malate, functioning as an anaplerotic sequence. A glyoxylate cycle thus operates in this strictly anaerobic bacterium. Phosphoenolpyruvate (PEP) carboxykinase formed PEP from oxaloacetate. No pyruvate kinase activity was detected. PEP presumably served as a precursor for polyglucose formation and other biosyntheses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305352
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  • 6
    Electronic Resource
    Electronic Resource
    Anaerobic degradation of 3-aminobenzoate by a newly isolated sulfate reducer and a methanogenic enrichment culture (1992)
    Springer
    Archives of microbiology 158 (1992), S. 328-334 
    Details
    ISSN: 1432-072X
    Keywords: 3-Aminobenzoate ; Anaerobic degradation ; Sulfate-reducing bacterium ; Methanogenic enrichment culture ; 3-Aminobenzoyl ; CoA synthetase ; 3-Aminobenzoyl-CoA reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A new rod-shaped, gram-negative, non-sporing sulfate reducer, strain mAB1, was enriched and isolated from marine sediment samples with 3-aminobenzoate as sole electron and carbon source. Strain mAB1 degraded 3-aminobenzoate completely to CO2 and NH3 with stoichiometric reduction of sulfate to sulfide. Cells contained carbon monoxide dehydrogenase, cytochromes, and sulfite reductase P582. Strain mAB1 degraded also benzoate, 4-aminobenzoate, hydroxybenzoates, and some aliphatic compounds. Besides sulfates, also sulfite was reduced with 3-aminobenzoate as electron donor, but not thiosulfate, sulfur, nitrate, or fumarate. The strain grew in sulfide-reduced mineral medium supplemented with 7 vitamins. Strain mAB1 was tentatively affiliated with the genus Desulfobacterium. Experiments with dense cell supsensions showed benzoate accumulation during 3-aminobenzoate degradation under conditions of sulfate limitation or cyanide inhibition. 3-Aminobenzoate was activated to 3-aminobenzoyl-CoA by cell extracts in the presence of ATP, coenzyme A, and Mg2+. Acitivity of 3-aminobenzoyl-CoA synthetase was 16 nmol per min and mg protein, with a KM for 3-aminobenzoate lower than 50 μM. Cell extract of 3-aminobenzoate-grown cells activated also 3-hydroxybenzoate (31.7 nmol per min and mg protein) and benzoate (2.3 nmol per min and mg protein), but not 2-aminobenzoate or 4-aminobenzoate. In the presence of NADH of NADPH, 3-aminobenzoyl-CoA was further metabolized to a not yet identified reduced product. Freshwater enrichments with 3-aminobenzoate in the absence of an extenal electron acceptor led to a stable methanogenic enrichment culture consisting of three types of bacteria. 3-Aminobenzoate was degraded completely to CO2 and stoichiometric amounts of CH4, with intermediary acetate accumulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245361
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