Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1

作者：Sugano Yasushi^*; Matsushima Yuko; Tsuchiya Katsunori; Aoki Hirokazu; Hirai Mitsuyo; Shoda Makoto

来源：Biodegradation, 2009, 20(3): 433-440.

DOI：10.1007/s10532-008-9234-y

• Anthraquinone dye
• Dye-decolorizing peroxidase
• DyP
• Thanatephorus cucumeris
• Phthalic acid

The reactants produced by action of a purified unique dye-decolorizing peroxidase, DyP, on a commercial anthraquinone dye, Reactive Blue 5, were investigated using electrospray ionization mass spectrometry (ESI-MS), thin-layer chromatography (TLC), and (1)H- and (13)C- nuclear magnetic resonance (NMR). The results of ESI-MS analysis showed that phthalic acid, a Product 2 (molecular weight 472.5), and a Product 3 (molecular weight 301.5), were produced. Product 2 and Product 3 were generated by usual peroxidase reaction, whereas phthalic acid was generated by hydrolase- or oxygenase-catalyzed reaction. One potential associated product, o-aminobenzene sulfonic acid, was found to be converted to 2,2'-disulfonyl azobenzene by ESI-MS and NMR analyses. From these results, we propose, for the first time, the degradation pathway of an anthraquinone dye by the enzyme DyP.

• 出版日期2009-6