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horseradish peroxidase indirectly degrades anthracycline by acting on hydroqui-
none (Reszka et al. 2005 ).
Sugano et al. ( 2009 ) have reported complete decolorization of Reactive Blue 5,
which is one of the derivatives of anthraquinone, as shown in Fig. 3 by the con-
certed action of two peroxidases, one versatile peroxidase (TcVP1) and the
otherdye-decolorizing peroxidase (DyP) from Thanatephorus Cucumeris (Fig. 4 ).
The decolorization processproceeded in a sequence; initially, DyP decolorized
Reactive blue 5 to light red-brown compounds, and then TcVP1 decolorized these
colored intermediates to colorless DyP. This was the
rst description of the in vitro
complete decolorization of an anthraquinone dye and the
rst report of using adual-
enzyme system for such a purpose. This strongly supports the notion that DyP and
Fig. 4 Degradation pathway of RB5 treated with dye decolorizing peroxidase (DyP) (Sugano
et al. 2009 )
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