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  • Fusion pools  (1)
  • thermotolerant  (1)
  • 1
    Electronic Resource
    Electronic Resource
    A general method for isolation of Mu d 1–8(Apr lac) operon fusions in Salmonella typhimurium LT2 from Tn10 insertion strains: chlC::Mu d 1–8 (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 221-224 
    Details
    ISSN: 1617-4623
    Keywords: Nitrate reductase ; Fusion pools ; oxrA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A general method was developed for the isolation of Salmonella thyphimurium LT2 Mu d1–8 (Apr lac) operon fusions in a gene displacing a Tn10 insertion. Random Mu d1–8 fusion pools were prepared to grow phage P22 lysates which transduced chlC::Tn10 to AprTets on fusaric acidampicillin plates. Among these AprTets potential chlC::Mu d1–8 fusions, a simple spot test identified the fusions that were closely linked to the Tn10 insertion in chlC. Out of 68 AprTets isolates 7 chlC::Mu d1–8 fusions with a nitrate-induced Lac+ phenotype were obtained. When oxrA::Tn10 was transduced into these chlC::Mu d1–8 fusions, they became Lac- even in the presence of nitrate, confirming that they were chlC::Mu d1–8 fusions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00430431
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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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