Cited by 86

The DOI matches its Crossref record.

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

Sugano, Yasushi, Matsushima, Yuko, Tsuchiya, Katsunori, Aoki, Hirokazu, Hirai, Mitsuyo, Shoda, Makoto·2009·Biodegradation

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 (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.

Overview

Integrity signals

Registry

Crossref · 10.1007/s10532-008-9234-y

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 31

  1. Alva KS, Kumar J, Marx KA, Tripathy SK (1997) Enzymatic synthesis and characterization of a novel water-soluble polyaniline: poly (2,5-diaminobenzenesulfonate). Macromolecules 30:4024–4029. doi: 10.1021/ma961544h · DOI
  2. Anliker R (1979) Ecotoxicology of dyestuffs—a joint effort by industry. Ecotoxicol Environ Saf 3:59–74. doi: 10.1016/0147-6513(79)90060-5 · DOI
  3. Banat IM, Nigam P, Singh D, Marchant R (1996) Microbial decolorization of textile-dye-containing effluents. Bioresour Technol 58:217–227. doi: 10.1016/S0960-8524(96)00113-7 · DOI · Paper page
  4. Cartoni A, Menna P, Salvatorelli E, Braghiroli D, Giampietro R, Animati F, Urabani A, Boccio PD, Minotti G (2004) Oxidative degradation of cardiotoxic anticancer anthracyclines to phthalic acids. J Biol Chem 279:5088–5099. doi: 10.1074/jbc.M306568200 · DOI
  5. Chivukula M, Spadaro JT, Renganathan V (1995) Lignin peroxidase catalized oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides. Biochemistry 34:7765–7772. doi: 10.1021/bi00023a024 · DOI
  6. Chung KT, Stevens E Jr (1993) Degradation of azo dyes by environmental microorganisms and heliminths. Environ Toxicol Chem 12:2121–2132. doi: 10.1897/1552-8618(1993)12[2121:DOADBE]2.0.CO;2 · DOI
  7. Dunford HB (1999) Heme peroxidases. Wiley-VCH, New York
  8. Fang H, Wenrong H, Yuezhong L (2004) Biodegradation mechanisms and kineteics of azo dye 4BS by a microbial consortium. Chemosphere 57:293–301. doi: 10.1016/j.chemosphere.2004.06.036 · DOI
  9. Fu Y, Viraraghavan T (2001) Fungal decolorization of dye wastewaters—a review. Bioresour Technol 79:251–262. doi: 10.1016/S0960-8524(01)00028-1 · DOI · Paper page
  10. Goszczynski S, Paszczynski A, Pasti-Grigsby MB, Crawford RL, Crawford DL (1994) New pathway for degradation of sulfonated azo dyes by microbial peroxidases of Phanerochaete chrysosporium and Streptomyces chromofuscus. J Bacteriol 176:1339–1347 · DOI
  11. Heinfling A, Martínez MJ, Martínez AT, Bergbauer M, Szewzyk U (1998) Transformation of industrial dyes by manganese peroxidases from Bjerkandera adusta and Pleurotus eryngii in a manganese-independent reaction. Appl Environ Microbiol 64:2788–2793 · DOI
  12. Itoh K, Kitade Y, Yatone C (1996) A pathway for biodegradation of anthraquinone dye, C. I. disperse red 15, by a yeast strain Pichia anomala. Bull Environ Contam Toxicol 56:413–418. doi: 10.1007/s001289900059 · DOI
  13. Itoh K, Kitade Y, Yatone C (1998) Oxidative biodegradation of an anthraquinone dye, pigment violet 12, by Coriolus versicolor. Bull Environ Contam Toxicol 60:786–790. doi: 10.1007/s001289900695 · DOI
  14. Jones P (2001) Roles of water in heme peroxidase and catalase mechanisms. J Biol Chem 276:13791–13796 · DOI
  15. Kim SJ, Shoda M (1999) Purification and characterization of a novel peroxidase from Geotricum candidum Dec 1 involved in decolorization of dyes. Appl Environ Microbiol 65:1029–1035 · DOI · Paper page
  16. Kim SJ, Ishikawa K, Hirai M, Shoda M (1995) Characteristics of a newly isolated fungus, Geotrichum candidum Dec 1, which decolorizes various dyes. J Ferment Bioeng 79:601–607. doi: 10.1016/0922-338X(95)94755-G · DOI
  17. McMullan G, Meehan C, Conneely A, Kirby N, Robinson T, Nigam P, Banat IM, Marchant R, Smyth WF (2001) Microbial decolourisation and degradation of textile dyes. Appl Microbiol Biotechnol 56:81–87. doi: 10.1007/s002530000587 · DOI
  18. Ollikka P, Alhonmaki K, Leppanen VM, Glumoff T, Raijola T, Suominen I (1993) Decolorization of azotriphenyl methane, heterocyclic, and polymeric dyes by lignin peroxidase isozymes from Phanerochaete chrysosporium. Appl Environ Microbiol 59:4010–4016 · DOI
  19. Pasti MB, Crawford DL (1991) Relationship between the abilities of streptomycetes to decolorize three anthron-type dyes and to degrade lignocellulose. Can J Microbiol 37:902–907 · DOI
  20. Reszka KJ, Wagner BA, Burns CP, Britigan BE (2005) Effects of peroxidase substrates on the amplex red/peroxidase assay: antioxidant properties of anthracycline. Anal Biochem 342:327–337. doi: 10.1016/j.ab.2005.04.017 · DOI
  21. Scheibner M, Hülsdau B, Zelena K, Nimtz M, de Boer L, Berger RG, Zorn H (2008) Novel peroxidases of Marasmius acorodonius degrade β-carotene. Appl Microbiol Biotechnol 77:1241–1250. doi: 10.1007/s00253-007-1261-9 · DOI
  22. Stolz A (2001) Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol 56:69–80. doi: 10.1007/s002530100686 · DOI · Paper page
  23. Sturm A, Schierhorn A, Lindenstrauss U, Lilie H, Brüser T (2006) YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins. J Biol Chem 281:13972–13978. doi: 10.1074/jbc.M511891200 · DOI
  24. Sugano Y, Sasaki K, Shoda M (1999) cDNA cloning and genetic analysis of a novel decolorizing enzyme, peroxidase gene dyp from Geotrichum candidum Dec 1. J Biosci Bioeng 87:411–417. doi: 10.1016/S1389-1723(99)80087-5 · DOI
  25. Sugano Y, Nakano R, Sasaki K, Shoda M (2000) Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1. Appl Environ Microbiol 66:1754–1758. doi: 10.1128/AEM.66.4.1754-1758.2000 · DOI
  26. Sugano Y, Matsushima Y, Shoda M (2006) Complete decolorization of the anthraquinone dye Reactive Blue 5 by the concerted action of two peroxidases from Thanatephorus cucumeris Dec 1. Appl Microbiol Biotechnol 73:862–871. doi: 10.1007/s00253-006-0545-9 · DOI
  27. Sugano Y, Muramatsu R, Ichiyanagi A, Sato T, Shoda M (2007) DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: Asp171 replaces the distal histidine of classical peroxidases. J Biol Chem 282:36652–36658. doi: 10.1074/jbc.M706996200 · DOI
  28. Vyas BR, Molitoris HP (1995) Involvement of an extracellular H2O2-dependent ligninolytic activity of the white rot fungus Pleurotus ostreatus in the decolorization of remazol brilliant blue R. Appl Environ Microbiol 61:3919–3927 · DOI
  29. Young L, Yu J (1997) Ligninase-catalysed decolorization of synthetic dyes. Water Res 31:1187–1193. doi: 10.1016/S0043-1354(96)00380-6 · DOI
  30. Zubieta C, Joseph R, Krishna SS, McMullan D, Kapoor M, Axelrod HL, Miller MD, Abdubek P, Acosta C, Astakhova T, other 37 authors (2007a) Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins 69:234–243. doi: 10.1002/prot.21673 · DOI
  31. Zubieta C, Krishna SS, Kapoor M, Kozbial P, McMullan D, Axelrod HL, Miller MD, Abdubek P, Ambing E, Astakhova T, other 34 authors (2007b) Crystal structures of two novel dye-decolorizing peroxidases reveal a β-barrel fold with a conserved heme-binding motif. Proteins 69:223–233. doi: 10.1002/prot.21550 · DOI

Cited by

Sorted by citations

Metadata

Authors
Sugano, Y., Matsushima, Y., Tsuchiya, K., Aoki, H., Hirai, M., & Shoda, M.
Venue
Biodegradation
Published
2008-11-15
Volume
20
Issue
3
Pages
433-440
ISSN
  • 0923-9820
  • 1572-9729
Cited by
86
References
0
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review