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  • Springer  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Azo dye decolorization with a mutant Escherichia coli strain (2000)
    Springer
    Biotechnology letters 22 (2000), S. 807-812 
    Details
    ISSN: 1573-6776
    Keywords: azo dye ; decolorization ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A recombinant Escherichia coli strain (E. coli NO3) containing genomic DNA fragments from azo-reducing wild-type Pseudomonas luteola strain decolorized a reactive azo dye (C.I. Reactive Red 22) at approx. 17 mg dye h−1 g cell. The ability to decolorize the azo dye probably did not originate from the plasmid DNA. Acclimation in azo-dye-containing media gave a nearly 10% increase in the decolorization rate of E. coli NO3. Growth with 1.25 g glucose l−1 completely stopped the decolorization activity. When the decolorization metabolites from E. coli NO3 were analyzed by HPLC and MS, the results suggested that decolorization of the azo dye may be due to cleavage of the azo bond.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005624707777
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Optimum ratio of d-carbamoylase to d-hydantoinase for maximizing d-p-hydroxyphenylglycine productivity (2000)
    Springer
    Biotechnology letters 22 (2000), S. 99-103 
    Details
    ISSN: 1573-6776
    Keywords: bio-conversion ; carbamoylase ; hydantoinase ; hydroxyphenylglycine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract By use of PCR, the genes encoding d-carbamoylase and d-hydantoinase, responsible for the synthesis of d-p-hydroxyphenylglycine (d-HPG), were cloned separately from Agrobacterium radiobacter NRRL B11291 into Escherichia coli. d-HPG production was carried out with a mixed population consisting of various proportions of two recombinants producing individual enzymes. As a result, with a total amount of 192 mg dry cell, the optimal productivity of d-HPG (ca. 4.5 g h−1 l−1) was obtained when the ratio of d-carbamoylase to d-hydantoinase ranged between 1 and 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005689202685
    Location Call Number Limitation Availability
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    Paper (German National Licenses)
    Fulltext
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