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  • 1
    Electronic Resource
    Electronic Resource
    The Purification of Cellulase and Hemicellulase Components from an Extreme Thermophile by the Cloning of Enzymes into E. coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 542 (1988), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1988.tb25836.x
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  • 2
    Electronic Resource
    Electronic Resource
    Proteases from Extreme Thermophiles (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 542 (1988), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1988.tb25843.x
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  • 3
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    Berbusse, "The United States in Puerto Rico" (Book Review) (1967)
    Austin, Tex. : Periodicals Archive Online (PAO)
    Social science quarterly. 48:2 (1967:Sept.) 227 
    Details
    ISSN: 0038-4941
    Topics: Sociology
    Notes: Book Reviews
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:1217-1967-048-02-000034
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of culture conditions on the production of an extracellular proteinase byThermus sp. Rt41A (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 400-406 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Thermus sp. Rt41A produced a single extracellular proteinase, as determined by fast protein liquid chromatography and isoelectric focusing. Proteinase activity was expressed from very early in the log phase, and halted when the growth substrate was exhausted. There was no continued proteinase production in the stationary phase. Proteinase production was not stimulated by O2 limitation, not repressed by amino acid growth substrates, and its production could not be correlated to the type or oxidation state of the carbon and energy source or the growth rate on different carbon and energy sources. Growth on certain substrates, e.g. glutamate and glucose, resulted in production of high levels of proteinase, whereas others, such as acetate, resulted in low proteinase levels. Acetate repressed proteinase production in cultures growing on L-glutamate. In continuous culture on L-glutamate, acetate or pyruvate, proteinase production was highest at higher growth (dilution) rates. The kinetics of proteinase production in continuous culture on L-glutamate can be interpreted as evidence for the constitutive nature of proteinase expression byThermus sp. Rt41A. The data obtained show that the control of proteinase production is different to that postulated forThermus sp. Ok6.A1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982527
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of culture conditions on the production of an extracellular proteinase by Thermus sp. Rt41A (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 400-406 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Thermus sp. Rt41A produced a single extracellular proteinase, as determined by fast protein liquid chromatography and isoelectric focusing. Proteinase activity was expressed from very early in the log phase, and halted when the growth substrate was exhausted. There was no continued proteinase production in the stationary phase. Proteinase production was not stimulated by O2 limitation, not repressed by amino acid growth substrates, and its production could not be correlated to the type or oxidation state of the carbon and energy source or the growth rate on different carbon and energy sources. Growth on certain substrates, e.g. glutamate and glucose, resulted in production of high levels of proteinase, whereas others, such as acetate, resulted in low proteinase levels. Acetate repressed proteinase production in cultures growing on L-glutamate. In continuous culture on L-glutamate, acetate or pyruvate, proteinase production was highest at higher growth (dilution) rates. The kinetics of proteinase production in continuous culture on L-glutamate can be interpreted as evidence for the constitutive nature of proteinase expression by Thermus sp. Rt41A. The data obtained show that the control of proteinase production is different to that postulated for Thermus sp. Ok6.A1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982527
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of culture conditions on the production of an extracellular proteinase byThermus sp. Rt41A (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 400-406 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Thermus sp. Rt41A produced a single extracellular proteinase, as determined by fast protein liquid chromatography and isoelectric focusing. Proteinase activity was expressed from very early in the log phase, and halted when the growth substrate was exhausted. There was no continued proteinase production in the stationary phase. Proteinase production was not stimulated by O2 limitation, not repressed by amino acid growth substrates, and its production could not be correlated to the type or oxidation state of the carbon and energy source or the growth rate on different carbon and energy sources. Growth on certain substrates, e.g. glutamate and glucose, resulted in production of high levels of proteinase, whereas others, such as acetate, resulted in low proteinase levels. Acetate repressed proteinase production in cultures growing on L-glutamate. In continuous culture on L-glutamate, acetate or pyruvate, proteinase production was highest at higher growth (dilution) rates. The kinetics of proteinase production in continuous culture on L-glutamate can be interpreted as evidence for the constitutive nature of proteinase expression byThermus sp. Rt41A. The data obtained show that the control of proteinase production is different to that postulated forThermus sp. Ok6.A1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00939027
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  • 7
    Electronic Resource
    Electronic Resource
    Very stable enzymes from extremely thermophilic archaebacteria and eubacteria (1989)
    Springer
    Applied microbiology and biotechnology 31 (1989), S. 556-561 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Thirty-six thermophilic archaebacteria and nine extremely thermophilic eubacteria have been screened on solid media for extracellular amylase, protease, hemicellulase (xylanase), cellulase, pectinase and lipase activities. Extracellular enzymes were detected in 14 archaebacteria belonging to three different orders. Twelve of these were able to degrade starch and casein and the two Thermofilum strains were able to degrade starch, xylan and carboxymethylcellulose. Three of the eubacteria could degrade only starch. The other six (including four Thermotoga strains) all had activity against starch, xylan and carboxymethylcellulose, and one also had activity against casein. Some of the amylolytic archaebacteria released α-glucosidase, β-glucosidase, amylase and transglucosylase activities into liquid media containing starch or maltose. Thermotoga strain FjSS3B.1 released amylase, xylanase, cellulase and β-glucosidase activities into the medium when grown in the presence of substrates. When the partially purified enzymes from Thermotoga and some of the archaebacteria were compared with known thermostable enzymes the majority were found to be the most thermostable of their type. The β-glucosidase, xylanase and cellulase from Thermotoga and two α-glucosidases, a β-glucosidase, an amylase and a pullulanase from archaebacteria all have half-lives of at least 15 min at 105°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270794
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  • 8
    Electronic Resource
    Electronic Resource
    The phylogenetic position of the Thermococcus isolate AN1 based on 16S rRNA gene sequence analysis: a proposal that AN1 represents a new species, Thermococcus zilligii sp. nov. (1997)
    Springer
    Archives of microbiology 168 (1997), S. 245-248 
    Details
    ISSN: 1432-072X
    Keywords: Key words Thermophile ; Thermococcus ; Pyrococcus ; 16S rRNA ; Archaea ; Euryarchaeota ; Extremophile ; Phylogeny ; Taxonomy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 16S rRNA gene from the Thermococcus New Zealand isolate AN1 was cloned and sequenced. Analysis of the gene revealed the presence of signature sequences, indicating that strain AN1 represents a new species of the genus Thermococcus. Since the isolate AN1 differed from other thermococci in both its lower optimal NaCl concentration and generally lower optimal temperature for growth, in its unusual lipid membrane composition, and in its sensitivity to antibiotics, we propose that strain AN1 represents a new species of Thermococcus. The proposed name is Thermococcus zilligii, and the type strain is DSM 2770.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050495
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation of an extremely thermophilic chemoorganotrophic anaerobe similar to Dictyoglomus thermophilum from new zealand hot springs (1987)
    Springer
    Archives of microbiology 147 (1987), S. 21-24 
    Details
    ISSN: 1432-072X
    Keywords: Dictyoglomus ; Fervidothrix ; Description ; Rotund bodies ; Extremely thermophilic ; Obligate anaerobe ; Fermentation products ; Physiology ; Distribution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strain similar to Dictyoglomus thermophilum, isolated from a New Zealand hot spring, is described. This strictly anaerobic, Gram-negative, non-motile and nonsporulating bacterium usually exists as long thin filaments of 5 to 25 μm by 0.35 to 0.45 μm. Rotund bodies are commonly observed. Thin sections of the cells revealed a two-layered cell wall. The optimum temperature and pH for growth was 70°C and 7.0 and 7.5 respectively. No growth was observed at 40°C and 85°C or at pH 4.5 to pH 9.0. The organism fermented glucose, maltose, mannose, xylose, lactose, cellobiose, galactose and sucrose and produced acetate as the major end-product with significant amounts of lactate, H2 and CO2 and only traces of ethanol. The doubling time on glucose was 10 h. The DNA base composition was 29.5% guanine plus cytosine as determined by the thermal denaturation method. Growth was inhibited by penicillin, tetracycline and chloramphenicol indicating that the organism was a eubacterium. These features are in common with the newly described species Dictyoglomus thermophilum to which the New Zealand isolate belongs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492899
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  • 10
    Electronic Resource
    Electronic Resource
    Phosphofructokinase activities within the order Spirochaetales and the characterisation of the pyrophosphate-dependent phosphofructokinase from Spirochaeta thermophila (1999)
    Springer
    Archives of microbiology 172 (1999), S. 401-406 
    Details
    ISSN: 1432-072X
    Keywords: Key words Spirochetes ; Phosphofructokinase ; Treponema ; Leptospira ; Spirochaeta ; Glycolysis ; ¶Pyrophosphate ; Thermophile
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The subtype of phosphofructokinase activity, either ATP-, ADP- or pyrophosphate-dependent, present in members of three genera from the Spirochaetales was investigated. The individual species/strains examined included Spirochaeta alkalica, S. asiatica, S. halophila, S. isovalerica, S. litoralis, S. zuelzerae, S. thermophila, two thermophilic spirochetes, Treponema bryantii, T. denticola, ¶T. pectinovorum, Leptospira biflexa and L. interrogans. All of the Spirochaeta strains, regardless of their phenotype, possessed primarily a pyrophosphate-dependent phosphofructokinase. In contrast, T. bryantii, T. denticola and L. biflexa had predominantly an ATP-dependent activity, whereas no activity was detected in T. pectinovorum or ¶L. interrogans. The results suggest that pyrophosphate-dependent phosphofructokinase activity may be a reliable phenotypic marker for the genus Spirochaeta and that there are potentially interesting differences in how the catabolism of saccharides is controlled among members of genera within the Spirochaetales. The pyrophosphate-dependent phosphofructokinase from S. thermophila strain RI 19.B1 was purified (303-fold) to homogeneity and biochemically characterised. The S. thermophila enzyme displayed hyperbolic kinetics with respect to both the forward and reverse cosubstrates and was not significantly affected by traditional activators or inhibitors of phosphofructokinase. The biochemical characterisation represents the first spirochete phosphofructokinase to be described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050777
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