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Transformation of Reactive Blue 19 by a recombinant peroxidase DyP

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Abstract

Wastewater containing recalcitrant dyes causes environmental problems. A new superfamily of heme-containing peroxidases, dye-decolorizing peroxidases (DyPs), has been found to decolorize different kinds of dyes, especial anthraquinone dyes efficiently. However, the mechanism of dyes degradation by DyPs has not been fully understood and the toxicity of dye degradation intermediates by DyPs catalysis to microbes is unclear. In this study, a purified recombinant Thermobifida fusca DyP (TfuDyP) in E. coli BL21(DE3) was used to treat Reactive Blue 19 (RB19), an anthraquinone dye. The reaction intermediates analyzed by ultra performance liquid chromatography/mass spectroscopy (UPLC–MS) indicated the initial site of TfuDyP attack on RB19. In addition, it was found that both RB19 and its incomplete degradation products inhibited the growth of Bacillus subtilis. These findings provided a novel understanding of DyPs catalysis to anthraquinone dyes.

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References

  1. Husain Q (2006) Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: a review. Crit Rev Biotechnol 26:201–221

    Article  CAS  Google Scholar 

  2. Kaushik P, Malik A (2009) Fungal dye decolourization: recent advances and future potential. Environ Int 35(1):127–141

    Article  CAS  Google Scholar 

  3. Andleeb S, Atiq N, Robson GD et al (2012) An investigation of anthraquinone dye biodegradation by immobilized Aspergillus flavus in fluidized bed bioreactor. Environ Sci Pollut Res Int 19:1728–1737

    Article  CAS  Google Scholar 

  4. Augugliaro V, Litter M, Palmisano L et al (2006) The combination of heterogeneous photo catalysis with chemical and physical operations: a tool for improving the photo process performance. J Photochem Photobiol C: Photochem Rev 7:127–144

    Article  CAS  Google Scholar 

  5. Cl P, Lloyd JR, Guthrie JT (2003) The removal of colour from textile wastewater using whole bacterial cells: a review. Dyes Pigments 8:179–196

    Google Scholar 

  6. Klanovicz N, Camargo AF, Stefanski FS et al (2020) Advanced oxidation processes applied for color removal of textile effluent using a home-made peroxidase from rice bran. Bioprocess Biosyst Eng 43:261–272

    Article  CAS  Google Scholar 

  7. Salas-Veizaga DM, Morales-Belpaire I, Terrazas-Siles E (2013) Evaluation of the genotoxic potential of Reactive Black 5 solutions subjected to decolorizing treatments by three fungal strains. Ecotoxicol Environ Saf 89:125–129

    Article  CAS  Google Scholar 

  8. Pan HR, Xu XL, Wen Z et al (2017) Decolorization pathways of anthraquinone dye Disperse Blue 2BLN by Aspergillus sp. XJ-2 CGMCC12963. Bioengineered 8:630–641

    Article  CAS  Google Scholar 

  9. Osma JF, Toca-Herrera JL, Rodriguez-Couto S (2010) Transformation pathway of Remazol Brilliant Blue R by immobilised laccase. Bioresour Technol 101:8509–8514

    Article  CAS  Google Scholar 

  10. Sekuljica NZ, Prlainovic NZ, Stefanovic AB et al (2015) Decolorization of anthraquinonic dyes from textile effluent using horseradish peroxidase: optimization and kinetic study. ScientificWorld J 2015:371625

    Article  Google Scholar 

  11. Lark D, Buzzo AJDR, Andrade JAA et al (2019) Enzymatic degradation and detoxification of azo dye Congo red by a new laccase from Oudemansiella canarii. Bioresour Technol 289:121655

    Article  Google Scholar 

  12. Vignali E, Tonin F, Pollegioni L et al (2018) Characterization and use of a bacterial lignin peroxidase with an improved manganese-oxidative activity. Appl Microbiol Biotechnol 102:10579–10588

    Article  CAS  Google Scholar 

  13. Chen C, Shrestha R, Jia K et al (2015) Characterization of Dye-decolorizing peroxidase (DyP) from Thermomonospora curvata reveals unique catalytic properties of A-type DyPs. J Biol Chem 290:23447–23463

    Article  CAS  Google Scholar 

  14. Singh R, Eltis LD (2015) The multihued palette of dye-decorizing peroxidases. Arch Biochem Biophys 574:56–65

    Article  CAS  Google Scholar 

  15. Rahmanpour R, Rea D, Jamshidi S et al (2016) Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds. Arch Biochem Biophys 594:54–60

    Article  CAS  Google Scholar 

  16. Sugano Y, Matsushima Y, Tsuchiya K et al (2009) Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec1. Biodegradation 20:433–440

    Article  CAS  Google Scholar 

  17. 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

    Article  CAS  Google Scholar 

  18. Linde D, Ruiz-Dueñas FJ, Fernández-Fueyo E et al (2005) Basidiomycete DyPs: genomic diversity, structural–functional aspects, reaction mechanism and environmental significance. Arch Biochem Biophys 574:66–74

    Article  Google Scholar 

  19. Novotny D, Dias N, Kapanen A et al (2006) Comparative use of bacterial, algal and protozoan tests to study toxicity of azo- and anthraquinone dyes. Chemosphere 63:1436–1442

    Article  CAS  Google Scholar 

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Acknowledgements

This work was supported by the Program of Introducing Talents of Discipline to Universities (1112-06), the National First-class Discipline Program of Light Industry Technology and Engineering (LITE2018-27), and Top-notch Academic Programs Project of Jiangsu Higher Education Institutions (PPZY2015A056).

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Correspondence to Lei Tang.

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Pi, Q., Zhu, Z. & Tang, L. Transformation of Reactive Blue 19 by a recombinant peroxidase DyP. Bioprocess Biosyst Eng 45, 425–429 (2022). https://doi.org/10.1007/s00449-021-02660-1

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