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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and characterization of an obligately anaerobic, polysaccharolytic, extremely thermophilic member of the genus Spirochaeta (1991)
    Springer
    Archives of microbiology 155 (1991), S. 396-401 
    Details
    ISSN: 1432-072X
    Keywords: Spirochaeta species ; Thermophile ecology and physiology ; Obligately anaerobic spirochete ; Polysaccharolytic
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An obligately anaerobic, extremely thermophilic Spirochaeta species was isolated from a thermal spring on the edge of Green Lake on Raoul Island of the Kermadec archipelago. The strain, designated RI 19.B1 (=DSM 6192) displayed the morphological characteristics typical of Spirochaeta species: regularly coiled long thin cells consisting of a crenulated outer sheath surrounding a central coiled protoplasmic cylinder. Between the outer sheath and the protoplasmic cylinder were two longitudinal periplasmic fibrils in a 1-2-1 arrangement, each anchored by an insertion disc near one pole, whereas the other end was not anchored. The strain displayed a strictly anaerobic, chemoorganotrophic, fermentative metabolism and was able to grow on a variety of mono-, di- and polysaccharides, including cellulose. Sugar alcohols, organic and amino acids were not utilized. Growth supplements were not required, but CO2 was required to produce consistent growth. Strain RI 19.B1 had temperature, pH and salinity optima of 64–66°C, pH 6.95 and 0.4% NaCl respectively. The maximum growth temperature and salinity were 73°C and 2.5% respectively. Glucose was fermented to lactate, acetate, carbon dioxide, and hydrogen. Succinate, ethanol and formate were not detected. The strain displayed the resistance to rifampicin typical of Spirochaeta species. The mol % G+C of DNA from strain RI 19.B1 was 52%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00243461
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of an extremely thermophilic sulphur-metabolizing archaebacterium belonging to the Thermococcales (1994)
    Springer
    Archives of microbiology 162 (1994), S. 261-266 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Extreme thermophile ; Archaebacteria ; Sulphur reduction ; Hot pool ; Thermococcales
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      An extremely thermophilic, obligately anaerobic, sulphur-metabolizing archaebacterium of the order Thermococcales , previously isolated from a thermal pool at Kuirau Park, Rotorua, New Zealand, partially described, and designated isolate ANI,Thermococcales was further characterized. The isolate was a regular coccus of 0.5–2.0 mm in diameter, was strictly anaerobic, chemoorganotrophic, and fermentative. Peptone, yeast extract, or casein served as carbon and nitrogen source, and a variety of amino acids and glucose, but not organic acids, carbohydrates, or other sugars supported growth in the presence of peptone (0.1%). Major metabolic end products were H2, sulphide, acetate, isobutyrate, and isovalerate/2-methylbutyrate. Isolate ANI had a temperature optimum of 75–80°C, a pH optimum of 7.4, and a sodium chloride concentration optimum of 50 mM. No growth was observed in the absence of sodium chloride (or lithium chloride) and sulphur (or cystine or oxidized glutathione).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301848
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of an extremely thermophilic sulphur-metabolizing archaebacterium belonging to the Thermococcales (1994)
    Springer
    Archives of microbiology 162 (1994), S. 261-266 
    Details
    ISSN: 1432-072X
    Keywords: Extreme thermophile ; Archaebacteria ; Sulphur reduction ; Hot pool ; Thermococcales
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An extremely thermophilic, obligately anaerobic, sulphur-metabolizing archaebacterium of the order Thermococcales, previously isolated from a thermal pool at Kuirau Park, Rotorua, New Zealand, partially described, and designated isolate ANI, Thermococcales was further characteized. The isolate was a regular coccus of 0.5–2.0 mm in diameter, was strictly anaerobic, chemoorganotrophic, and fermentative. Peptone, yeast extract, or casein served as carbon and nitrogen source, and a variety of amino acids and glucose, but not organic acids, carbohydrates, or other sugars supported growth in the presence of peptone (0.1%). Major metabolic end products were H2, sulphide, acetate, isobutyrate, and isovalerate/2-methylbutyrate. Isolate ANI had a temperature optimum of 75–80°C, a pH optimum of 7.4, and a sodium chloride concentration optimum of 50mM. No growth was observed in the absence of sodium chloride (or lithium chloride) and sulphur (or cystine or oxidized glutathione).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301848
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  • 4
    Electronic Resource
    Electronic Resource
    Dual mechanisms of xylose uptake in the thermophilic bacterium Thermoanaerobacter thermohydrosulfuricus (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 116 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Thermoanaerobacter thermohydrosulfuricus Rt8.B1 catabolized xylose by the pentose phosphate pathway, and xylose isomerase and xylulokinase were inducible. The uptake of xylose was by two low-affinity, inducible systems. Both systems were resistant to the protonophore, tetrachlorosalicylanilide, the F1F0-ATPase inhibitor, N,N-dicyclohexylcarboiimide, and the sodium/proton antiporter, monensin. The high capacity system (100 nmol min−1 (mg protein)−1) was only expressed when the bacterium was grown with a high concentration of xylose (50 mM). It took more than 60 mM xylose to saturate the high capacity system. When T. thermohydrosulfuricus was grown with a low concentration of xylose (5 mM), xylose uptake was saturated by as little as 10 mM xylose (18 nmol min−1 (mg protein)−1). Cells grown with 50 mM xylose could not transport glucose, and high capacity xylose transport was not inhibited by glucose or non-metabolizable glucose analogues. Cells grown with 5 mM xylose transported glucose at a rapid rate (30 nmol min−1 (mg protein)−1), and low capacity xylose uptake was competitively inhibited by either glucose or 2-deoxy-glucose. Because the glucose uptake of cells grown on 5 mM xylose was competitively inhibited by xylose, it appeared that the low capacity xylose uptake system was a glucose/xylose carrier.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06712.x
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  • 5
    Electronic Resource
    Electronic Resource
    Simultaneous uptake and utilisation of glucose and xylose by Clostridium thermohydrosulfuricum (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 109 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Growth studies of Clostridium thermohydrosulfuricum Rt8.B1 demonstrated that glucose and xylose were used simultaneously when supplied together at nonlimiting concentrations in pH-controlled batch culture. Under conditions of hyperbolic growth, both catabolite repression and inducer exclusion were absent. Glucose did not repress xylose metabolism (i.e. xylose permease and xylose isomerase genes were expressed in the presence of glucose and were not subject to catabolite inhibition when glucose was added to cultures growing on high concentrations of xylose). The kinetics of glucose and xylose utilisation indicated that separate systems were present for the uptake of these substrates when supplied together. Glucose utilisation was biphasic, indicating high- and low-affinity systems for glucose uptake. Xylose utilisation was directly proportional to the xylose concentration, suggesting a facilitated diffusion mechanism was operative for uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06143.x
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  • 6
    Electronic Resource
    Electronic Resource
    Acidophilic and thermophilic Bacillus strains from geothermally heated antarctic soil (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 60 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Bacteria with temperature optima of 51–54°C and pH optima of 3.5–4.5 were isolated from geothermal soil collected from Mount Erebus, Ross Island, Antarctica. The isolates were enriched on medium designed for the growth of Thermoplasma but the strains found were members of the genus Bacillus. Comparisons with other thermophilic acidophilic Bacillus species indicate that the strains most strongly resemble B. acidocaldarius although their temperature optima and substrate utilisation spectrum differ from one another. These strains join B. schlegelii as being isolated from geothermal soils present on Mt. Erebus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03486.x
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  • 7
    Electronic Resource
    Electronic Resource
    A comparison of extracellular serine proteases from four strains of Thermus aquaticus (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 43 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A comparison of extracellular proteases from New Zealand isolates of the genus Thermus demonstrated a number of minor but significant structural and functional differences. The comparison, based on molecular weights, isoelectric points, inhibitor responses, substrate specificity, pH optima and thermostability suggested that the four proteases were a closely related family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02115.x
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  • 8
    Electronic Resource
    Electronic Resource
    Inhibition of phosphofructokinases by copper(II) (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 197 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three phosphoryl donor subtypes (ATP, ADP and pyrophosphate). The sensitivities of the enzymes to Cu2+ varied greatly, with the archaeal ADP-PFK being the least and the eukaryote ATP-PFK being the most sensitive. The bacterial ATP- and pyrophosphate-dependent PFKs showed intermediate sensitivity with the exception of the Spirochaeta thermophila enzyme (pyrophosphate-dependent) which was relatively resistant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10590.x
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  • 9
    Electronic Resource
    Electronic Resource
    Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 194 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An active pyrophosphate-dependent phosphofructokinase containing a six residue polyhistidine tag has been cloned from Treponema pallidum, and characterized biochemically. The phosphofructokinase has pH optima for activity of 8.0 for both the forward and reverse reactions. The apparent Km for pyrophosphate was 0.042 mM (Vmax of 141 U mg−1 protein) and for fructose-6-phosphate, 0.529 mM. The apparent Km for the reverse reaction for fructose-1,6-diphosphate was 0.267 mM (Vmax of 42.4 U mg−1 protein). The enzyme appears to be both a dimer and non-allosteric.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb09479.x
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning, expression and characterisation of a Family B ATP-dependent phosphofructokinase activity from the hyperthermophilic crenarachaeon Aeropyrum pernix (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 202 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We have cloned a Family B sugar kinase gene from the aerobic hyperthermophilic crenarchaeon Aeropyrum pernix and have subsequently expressed the protein in Escherichia coli. The enzyme was purified with its associated histidine-tag by affinity chromatography with a nickel-nitrilotriacetic acid column followed by cation exchange chromatography and possesses a high degree of thermostable ATP-dependent phosphofructokinase activity. The enzyme has an estimated apparent Km for ATP and fructose-6-phosphate of 0.027 and 1.212 mM, respectively, that were determined in discontinuous assays at 95°C. The Family B ATP-dependent phosphofructokinase has a half-life of approximately 30 min at 95°C and is indicated to be monomeric. The implications of the presence of a Family B phosphofructokinase in the Crenarchaea are discussed with reference to the origins of the Embden–Meyerhof pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10784.x
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