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A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily

van Bloois, Edwin, Torres Pazmiño, Daniel E., Winter, Remko T., Fraaije, Marco W.·2010·Applied Microbiology and Biotechnology
DOI 10.1007/s00253-009-2369-xPMC PMC2854361
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  • Although their action mechanism resembles that of other peroxidases, anthraquinone dye degradation by DyPs is not yet fully mapped.

    “Although their action mechanism resembles that of other peroxidases, anthraquinone dye degradation is not yet fully mapped 129-134 .”

    From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [129]

    The Introduction describes peroxide-driven oxidation as a general peroxidase reaction, and the Discussion says understanding of DyP enzymes is limited. But the paper does not specifically say that the mechanism of anthraquinone dye degradation remains unmapped; it also emphasizes that DyPs have distinct reaction characteristics from other peroxidase superfamilies. The indexed passages provide section labels but no page numbers. (LLM, conf=0.83)

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Research works printed but not linked: 46

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Metadata

Authors
van Bloois, E., Torres Pazmiño, D. E., Winter, R. T., & Fraaije, M. W.
Venue
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2009-12-05
Volume
86
Issue
5
Pages
1419-1430
ISSN
  • 0175-7598
  • 1432-0614
DOI
10.1007/s00253-009-2369-x
PMC
PMC2854361
Cited by
180
References
0
Language
en

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