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Change in turnover capacity of crude recombinant dye-decolorizing peroxidase (rDyP) in batch and fed-batch decolorization of Remazol Brilliant Blue R

Shakeri, M., Shoda, M.·2007·Applied Microbiology and Biotechnology

Abstract

Decolorization of the representative anthraquinone dye, Remazol Brilliant Blue R (RBBR) was assessed to determine the practical potential of crude recombinant dye-decolorizing peroxidase generated by Aspergillus oryzae (rDyP) in term of turnover capacity of rDyP. The turnover capacity, defined as the milligram of RBBR decolorized per unit of rDyP inactivated over the catalytic life time of rDyP, was quantified under condition by H(2)O(2) -mediated rDyP inactivation. In batch culture, equimolar batch addition of H(2)O(2) and RBBR yielded complete decolorization of RBBR by rDyP, with a turnover capacity of 4.75. In stepwise fed-batch addition of H(2)O(2), the turnover capacity increased to 5.76, and by increasing dye concentration, it reached 14.3. When H(2)O(2) was added in continuous fed-batch to minimize rDyP inactivation and 1.6 mM dye was added in stepwise fed-batch mode, the turnover capacity increased to 20.4. At this turnover capacity, 1 l of crude rDyP solution containing 5,000 U could decolorize up to 102 g RBBR in 650 min.

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Crossref · 10.1007/s00253-007-1042-5

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  • Diffusional limitations of substrate and/or product in-between the cell compartments can be avoided as well as any other actions besides enzymatic.

    “Also, diffusional limitations of substrate and/or product in-between the cell compartments can be avoided as well as any other actions besides enzymatic 105-107 .”
  • Recombinant DyP was used to treat Reactive Blue 19 in a single batch system and also in a step fed batch reactor to assess a cyclic operation, leading to a very high decolorisation performance, regardless the soluble nature of the enzyme.

    “For example, recombinant DyP was used to treat Reactive Blue 19 in a single batch system and also in a step fed batch reactor 107 to assess a cyclic operation, leading to a very high decolorisation performance, regardless the soluble nature of the enzyme.”

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Metadata

Authors
Shakeri, M., & Shoda, M.
Venue
Applied Microbiology and Biotechnology
Published
2007-06-14
Volume
76
Issue
4
Pages
919-926
ISSN
  • 0175-7598
  • 1432-0614
Cited by
14
References
0
Language
en

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