Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1 |
| |
Authors: | Yasushi Sugano Yuko Matsushima Katsunori Tsuchiya Hirokazu Aoki Mitsuyo Hirai Makoto Shoda |
| |
Institution: | (1) R1-30 Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, Japan |
| |
Abstract: | 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 1H- and 13C- 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. |
| |
Keywords: | Anthraquinone dye Dye-decolorizing peroxidase DyP Thanatephorus cucumeris Phthalic acid |
本文献已被 SpringerLink 等数据库收录! |
|