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  • 1
    Electronic Resource
    Electronic Resource
    Fermentative degradation of triethanolamine by a homoacetogenic bacterium (1994)
    Springer
    Archives of microbiology 162 (1994), S. 103-107 
    Details
    ISSN: 1432-072X
    Keywords: Anacrobic degradation ; Triethanolamine ; Homoacetogenic fermentation ; Corrinoids ; Triethanolamine degrading enzyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract With triethanolamine as sole source of energy and organic carbon, a strictly anaerobic, gram-positive, rod-shaped bacterium, strain LuTria 3, was isolated from sewage sludge and was assigned to the genus Acetobacterium on the basis of morphological and physiological properties. The G+C content of the DNA was 34.9±1.0 mol %. The new isolate fermented triethanolamine to acetate and ammonia. In cell-free extracts, a triethanolamine-degrading enzyme activity was detected that formed acetaldehyde as reaction product. Triethanolamine cleavage was stimulated 30-fold by added adenosylcobalamin (co-enzyme B12) and inhibited by cyanocobalamin or hydroxocobalamin. Ethanolamine ammonia lyase, acetaldehyde:acceptor oxidoreductase, phosphate acetyltransferase, acetate kinase, and carbon monoxide dehydrogenase were measured in cell-free extracts of this strain. Our results establish that triethanolamine is degraded by a corrinoid-dependent shifting of the terminal hydroxyl group to the subterminal carbon atom, analogous to a diol dehydratase reaction, to form an unstable intermediate that releases acetaldehyde. No anaerobic degradation of triethylamine was observed in similar enrichment assays.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264381
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  • 2
    Electronic Resource
    Electronic Resource
    Demethylation and degradation of phenylmethylethers by the sulfide-methylating homoacetogenic bacterium strain TMBS 4 (1993)
    Springer
    Archives of microbiology 159 (1993), S. 308-315 
    Details
    ISSN: 1432-072X
    Keywords: Methyl transfer ; Demethylation ; Methoxylated aromatic compounds ; Ether cleavage ; Corrinoids ; Homoacetogenic bacteria ; Phloroglucinol pathway ; Dimethylsulfide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Biochemical studies on anaerobic phenylme-thylether cleavage by homoacetogenic bacteria have been hampered so far by the complexity of the reaction chain involving methyl transfer to acetyl-CoA synthase and subsequent methyl group carbonylation to acetyl-CoA. Strain TMBS 4 differs from other demethylating homoacetogenic bacteria in using sulfide as a methyl acceptor, thereby forming methanethiol and dimethylsulfide. Growing and resting cells of strain TMBS 4 used alternatitively CO2 as a precursor of the methyl acceptor CO for homoacetogenic acetate formation. Demethylation was inhibited by propyl iodide and reactivated by light, indicating involvement of a corrinoid-dependent methyltransferase. Strain TMBS 4 contained ca. 750 nmol g dry mass-1 of a corrinoid tentatively identified as 5-hydroxybenzimidazolyl cobamide. A photometric assay for measuring the demethylation activity in cell extracts was developed based on the formation of a yellow complex of Ti3+ with 5-hydroxyvanillate produced from syringate by demethylation. In cell extracts, the methyltransfer reaction from methoxylated aromatic compounds to sulfide or methanethiol depended on reductive activation by Ti3+. ATP and Mg2+ together greatly stimulated this reductive activation without being necessary for the demethylation reaction itself. The specific activity of the transmethylating enzyme system increased proportionally with protein concentration up to 3 mg ml-1 reaching a constant level of 20 nmol min-1 mg-1 at protein concentrations ≥ 10 mg ml-1. The specific rate of activation increased in a non-linear manner with protein concentration. Strain TMBS 4 degraded gallate, the product of sequential demethylations, to 3 acetate through the phloroglucinol pathway as found earlier with Pelobacter acidigallici.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290912
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  • 3
    Electronic Resource
    Electronic Resource
    Fermentation of phenoxyethanol to phenol and acetate by a homoacetogenic bacterium (1994)
    Springer
    Archives of microbiology 162 (1994), S. 199-204 
    Details
    ISSN: 1432-072X
    Keywords: Anaerobic degradation ; Phenoxyethanol ; Ether cleavage ; Homoacetogenic fermentation ; Corrinoids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strictly anaerobic gram-positive, rod-shaped bacterium, strain LuPhet1, was isolated from sewage sludge with phenoxyethanol as sole carbon and energy source, and was assigned to the genus Acetobacterium. The new isolate fermented the alkylaryl ether compound phenoxyethanol stoichiometrically to phenol and acetate, whereas phenoxyacetic acid was not degraded. In cell-free extracts of strain LuPhet1, cleavage of the ether linkage was shown, and acetaldehyde was detected as reaction product. Coenzyme A-dependent acetaldehyde: acceptor oxidoreductase, phosphate acetyltransferase, acetate kinase, and carbon monoxide dehydrogenase were measured in cell-free extracts of this strain. Our results indicate that the ether linkage of phenoxyethanol is cleaved by a shift of the hydroxyl group to the subterminal carbon atom, analogous to a corrinoid-dependent diol dehydratase reaction, to form an unstable hemiacetal that releases phenol and acetaldehyde. Obviously, phenoxyethanol is degraded by the same strategy as in anaerobic degradation of the alkyl ether polyethylene glycol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00314475
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