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  • Anaerobiosis  (1)
  • thermotolerant  (1)
  • 1
    Electronic Resource
    Electronic Resource
    ack::Mu d1-8 (Apr lac) operon fusions of Salmonella typhimurium LT2 (1988)
    Springer
    Molecular genetics and genomics 211 (1988), S. 183-185 
    Details
    ISSN: 1617-4623
    Keywords: Acetate kinase ; Phosphotransacetylase ; Anaerobiosis ; Mu d1-8 fusions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Several ack::Mu d1-8 insertions were isolated from Salmonella typhimurium on MacConkey-glucose-trimethylamine oxide medium. They could not produce gas from glucose in the absence of exogeneous formate. Two of the mutants expressed β-galactosidase activity and were shown to be ack::Mu d1-8 fusions by genetic analysis. These insertions were characterized and located on the genetic map at the ack locus by co-transduction with zei::Tn10. The gene order zei::Tn10-ack-pta was established. The direction of transcription of ack was clockwise on the genetic map. Expression of the lac operon in ack::Mu d1-8 was increased twofold by anaerobiosis. Addition of formate, pyruvate, and acetate did not affect the anaerobic expression of the lac operon in ack::Mu d1-8.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00338411
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and properties of β-amylase from Bacillus circulans S31 (1994)
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 597-598 
    Details
    ISSN: 1573-0972
    Keywords: Amylases ; Bacillus ; enzyme ; maltose ; starch ; thermotolerant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A thermotolerant β-amylase was purified from Bacillus circulans S31 isolated from soil in Hong Kong. The purified enzyme has an M r of 64 kDa and was stable at 50°C and pH 7.0 for 30 min. Its K m for starch was 0.9 mg/ml with a V max of 0.3 mg/min. It was not activated by any metal ion although sulphydrys reagents were inhibitory.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00367677
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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