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  • 1
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 39 (1993), S. 400-404 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Several strains of methane-oxidizing bacteria were isolated and studied to determine their physiological suitability for removal of methane in coal mine atmospheres. One strain, Methylomonas fodinarum ACM 3268, was selected as the most suitable culture for use in the development of a continuous biofilter to be used as a ventilation “air scrubber”. The experimental biofilter utilising a biofilm of M. fodinarum was shown to reduce methane levels substantially provided the residence times were sufficiently long. In the range 0.25–1.0% methane in air, commonly experienced in coal mine atmospheres, more than 70% of the methane was removed with a residence time of 15 min, with a 90% reduction at 20 min. Even at a residence time of 5 min approximately 20% of the methane in air was removed. Equal quantities of O2 are consumed during the bacterial oxidation of methane and 1% methane is converted to 0.7% CO2. Scale-up and alternative biofilter packings are likely to reduce the residence times in the biofilter.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 63 (1968), S. 214-223 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Investigations into the properties of 6-PG dehydrogenase in cell free extracts of Escherichia coli revealed a pH optimum at pH 9.5 with a sharp decline on both sides of the optimum. The addition of 1.0×10-2 m MgCl2 produced maximal activity, whereas higher concentrations caused inhibition. The K m values were 2.5×10-4 m for 6-phosphogluconate and 2.5×10-5 m for NADP+ as substrate. The enzyme was extremely stable for at least 5 hours if stored at 4°C in Tris−NaCl−MgCl2 buffer at pH 7.5. 6-PG dehydrogenase activity was shown to be proportional to cell free extract concentration over the range 0–0.3 mg protein. An assay method based on the new optimal conditions has been established and has been shown to be 33% more sensitive than a number of commonly used methods.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 63 (1968), S. 197-213 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Glucose-6-phosphate dehydrogenase activity in cell free extracts o Zymomonas mobilis showed marked differences when compared with the corresponding enzyme of Escherichia coli. It exhibited 3 times higher activity and the reaction rate over 10 min gave linearity only up to a cell free protein concentration of 0.15 mg protein. This different behaviour was not a function of environmental growth conditions of the culture nor of the nine different assay methods employed. A constant relationship existed between the specific G-6-P dehydrogenase protein and the total protein concentration in the cell free extract. The enzyme was stable for at least 5 h at 4°C in Tris-NaCl-MgCl2-buffer. An investigation of the properties of G-6-P dehydrogenase from Z. mobilis revealed a pH optimum of 8.7 with a rapid decline towards the acidic and a small decrease towards the alkaline side. The K m values were 5×10-4 m for glucose-6-phosphate and 3.6×10-5 m NADP+. The addition of 1×10-2 m MgCl2 produced optimal activity but higher concentrations inhibited the enzyme reaction. These results were discussed with those from other sources and found to be unique for Zymomonas mobilis.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 173 (2000), S. 49-57 
    ISSN: 1432-072X
    Keywords: Key words Arsenate reduction ; Sulfate reduction ; Desulfovibrio sp. ; Desulfomicrobium sp. ; Arsenate ¶reductase ; Cytochrome c ; Arsenate resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two sulfate-reducing bacteria, which also reduce arsenate, were isolated; both organisms oxidized lactate incompletely to acetate. When using lactate as the electron donor, one of these organisms, Desulfomicrobium strain Ben-RB, rapidly reduced (doubling time = 8 h) 5.1 mM arsenate at the same time it reduced sulfate (9.6 mM). Sulfate reduction was not inhibited by the presence of arsenate. Arsenate could act as the terminal electron acceptor in minimal medium (doubling time = 9 h) in the absence of sulfate. Arsenate was reduced by a membrane-bound enzyme that is either a c-type cytochrome or is associated with such a cytochrome; benzyl-viologen-dependent arsenate reductase activity was greater in cells grown with arsenate/sulfate than in cells grown with sulfate only. The second organism, Desulfovibrio strain Ben-RA, also grew (doubling time = 8 h) while reducing arsenate (3.1 mM) and sulfate (8.3 mM) concomitantly. No evidence was found, however, that this organism is able to grow using arsenate as the terminal electron acceptor. Instead, it appears that arsenate reduction by the Desulfovibrio strain Ben-RA is catalyzed by an arsenate reductase that is encoded by a chromosomally-borne gene shown to be homologous to the arsC gene of the Escherichia coli plasmid, R773 ars system.
    Type of Medium: Electronic Resource
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