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  • 1990-1994  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Glucose oxidase biosynthesis using immobilized mycelium of Aspergillus niger (1991)
    Springer
    World journal of microbiology and biotechnology 7 (1991), S. 379-384 
    Details
    ISSN: 1573-0972
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A simple method is described for the immobilization of Aspergillus niger GIV-10 which produces an extracellular glucose oxidase. A. niger conidia were immobilized on sintered glass Raschig rings, pumice stones or polyurethane foam. Mycella growing out from the spores produced extracellular glucose oxidase: the highest production was with the pumice stone carrlers. This technique facilitates the growth of the filamentous cultures in the spongy structure of a support with continuous accumulation of biomass. After 24 to 36 h, a culture liquid with 2.7 to 3.1 U of glucose oxidase/ml was obtained. This procedure also made possible repeated batch enzyme production and as many as 25 subsequent 24-h batches could be fermented by using the same carrier with only a small loss of glucose oxidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00329406
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Penicillium notatum 1 a new source of dextranase (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 315-320 
    Details
    ISSN: 1476-5535
    Keywords: Penicillium notatum 1 ; Dextranase ; Screening ; Mutagenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Two hundred and fifteen fungal strains were screened for extracellular dextranase production with a diffusion plate method. The best enzymatic activity (12–19 DU ml−1) was achieved byPenicillium notatum 1, a species for which the dextranase productivity has not yet been published. Some of the parameters affecting enzyme production have been standardized. The enzyme in crude state was relatively stable, its maximal activity was at 50°C and at pH 5.0. Conidia of the selected strain were mutagenized, and isolated mutants were tested for production of dextranase in submerged culture. The most active mutant,P. notatum 1-I-77, showed over two-times higher dextranase activity than the parentP. notatum 1
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569734
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Intensification of glucose oxidase synthesis with aspergillus niger by the way of multistage mutagenization (1990)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 10 (1990), S. 371-376 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Conidia of glucose oxidase active Aspergillus niger G 13 strain were subjected to the fourth-stage mutagenization using different combinations of mutagens in each stage (stage I - UV radiation + nitrosomethylurea, stage II - UV radiation + ethyleneimine, Stage III - acryflavine, stage IV - UV radiation + N-methyl-N′-nitrosoguanidine). In all, 400 strains which showed higher glucose oxidase activity with our own diffusion data method (were isolated out of 5208 colonies after mutagenization). Nine most active mutants were tested in the submerged culture determining the activity of glucose oxidase in the post-culture liquid which increased from 10.7 to nearly 30%.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370100412
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The controlled porous glass (CPG) with reactive epoxy groups as support for affinity chromatography. II. Modified CPG as support of substrates or coenzyme of glucose oxidase (GOD) for its purification and immobilization (1990)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 10 (1990), S. 283-292 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Controlled porosity glasses (CPG) are materials very widely employed as supports for chromatography and biotechnology. In this paper CPG with epoxy groups have been applied as carrier of FAD, glucose and 2-deoxy-D-glucose. Glucose oxidase (GOD) was highly purified on these sorbents. The purified fraction of GOD was also immobilized on the activated CPG. The presented results suggest the higher stability of immobilized form of this enzyme in relation to the native enzyme.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370100314
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    Paper (German National Licenses)
    Fulltext
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