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  • 1
    Electronic Resource
    Electronic Resource
    Increased thermal stability of glucose dehydrogenase by cross-linking chemical modification (1999)
    Springer
    Biotechnology letters 21 (1999), S. 199-202 
    Details
    ISSN: 1573-6776
    Keywords: thermal stabilization ; glucose dehydrogenase ; cross-linking chemical modification ; amperometric glucose sensor ; storage stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A hetero-oligomeric glucose dehydrogenase (GDH) from a moderate thermophilic bacterium, SM4 was cross-linked with glutaraldehyde (GA) and it now showed only one optimum temperature for reaction at around 65 °C, which approximately follows the Arrhenius equation. The native enzyme had shown optima at both 45 °C and 75 °C. In addition to the alteration of the optimum temperature for reaction, GA cross-linked GDH retained more than 90% of its initial activity even after 30 min of incubation at 65 °C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005455911753
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Construction and characterization of a linked-dimeric pyrroloquinoline quinone glucose dehydrogenase (1999)
    Springer
    Biotechnology letters 21 (1999), S. 707-710 
    Details
    ISSN: 1573-6776
    Keywords: biosensor ; glucose dehydrogenase ; protein engineering ; pyrroloquinoline quinone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Using the structural gene of a homo dimeric enzyme, the water-soluble pyrroloquinoline quinone glucose dehydrogenase (PQQGDH-B), a gene consisting of two identical subunits linked together by a DNA segment coding linker peptide region was constructed. Using the constructed gene, a linked-dimeric PQQGDH-B was produced in Escherichia coli as the active soluble enzyme. Linked-dimeric PQQGDH-B showed a larger increase in thermal stability than the native dimeric enzyme. During incubation over 45 °C, the residual activity of linked-dimeric PQQGDH-B was more than twice that of the native dimeric enzyme. The potential application of linked-dimeric PQQGDH-B for glucose enzyme sensor is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005518610946
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    The production of soluble pyrroloquinoline quinone glucose dehydrogenase by Klebsiella pneumoniae, the alternative host of PQQ enzymes (2000)
    Springer
    Biotechnology letters 22 (2000), S. 1343-1347 
    Details
    ISSN: 1573-6776
    Keywords: glucose dehydrogenase ; Klebsiella pneumoniae ; pyrroloquinoline quinone ; recombinant production
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Klebsiella pneumoniae, which produces PQQ and is available for use with a conventional expression vector system, was selected as the host strain for soluble PQQ glucose dehydrogenase (PQQGDH-B) production. The recombinant K. pneumoniaeexpressed PQQGDH-B in its holo-form at about 18 000 U l−1, equal to that achieved in recombinant Escherichia coli. The signal sequence of recombinant PQQGDH-B produced by K. pneumoniaewas correctly processed. K. pneumoniaecan become an alternative host microorganism not only for PQQGDH-B production but also for recombinant PQQ enzymes production.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005615400089
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    Paper (German National Licenses)
    Fulltext
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