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Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79

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Abstract

A manganese peroxidase (MnP) isoenzyme from Panus tigrinus CBS 577.79 was produced in a benchtop stirred-tank reactor and purified to apparent homogeneity. The purification scheme involving ultrafiltration, affinity chromatography on concanavalin–A Sepharose, and gel filtration led to a purified MnP, termed “MnP II,” with a specific activity of 288 IU mg−1 protein and a final yield of 22%. The enzyme turned out to be a monomeric protein with molecular mass of 50.5 kDa, pI of 4.07, and an extent of N-glycosylation of about 5.3% of the high-mannose type. The temperature and pH optima for the formation of malonate manganic chelates were 45 °C and 5.5, respectively. MnP II proved to be poorly thermostable at 50 and 60 °C, with half-lives of 11 min and 105 s, respectively. K m values for H2O2 and Mn2+ were 16 and 124 μM, respectively. Although MnP II was able to oxidize veratryl alcohol and to catalyze the Mn2+-independent oxidation of several phenols, it cannot be assigned to the versatile peroxidase family. As opposed to versatile peroxidase oxidation, veratryl alcohol oxidation required the simultaneous presence of H2O2 and Mn2+; in addition, low turnover numbers and K m values higher than 300 μM characterized the Mn2+-independent oxidation of substituted phenols. Kinetic properties and the substrate specificity of the enzyme markedly differed from those reported for MnP isoenzymes produced by the reference strain P. tigrinus 8/18. To our knowledge, this study reports for the first time a thorough electrochemical characterization of a MnP from this fungus.

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References

  1. López C, Moreira MT, Feijoo G, Lema JM (2008) Biotechnol Prog 20:74–81

    Article  Google Scholar 

  2. Moreira MT, Feijoo G, Canaval J, Lema JM (2003) Wood Sci Technol 37:117–123

    Article  CAS  Google Scholar 

  3. Hofrichter M (2002) Enzyme Microb Technol 30:454–466

    Article  CAS  Google Scholar 

  4. Waarishi H, Akileswaran L, Gold MH (1988) Biochemistry 27:5365–5370

    Article  Google Scholar 

  5. Waarishi H, Valli K, Gold MH (1992) J Biol Chem 267:23688–23695

    Google Scholar 

  6. D’Annibale A, Crestini C, Di Mattia E, Giovannozzi Sermanni G (1996) J Biotechnol 48:231–239

    Article  Google Scholar 

  7. Forrester IT, Grabsky AC, Mishra C, Burgess RR, Leatham GF (1988) Biochem Biophys Res Commun 157:992–999

    Article  CAS  PubMed  Google Scholar 

  8. Fenice M, Giovannozzi Sermanni G, Federici F, D’Annibale A (2003) J Biotechnol 100:77–85

    Article  CAS  PubMed  Google Scholar 

  9. Quaratino D, Fenice M, Federici F, D’Annibale A (2006) J Chem Technol Biotechnol 81:832–840

    Article  CAS  Google Scholar 

  10. Quaratino D, D’Annibale A, Federici F, Cereti CF, Rossini F (2007) Chemosphere 66:1627–1633

    Article  CAS  PubMed  Google Scholar 

  11. D’Annibale A, Ricci M, Quaratino D, Federici F, Fenice M (2004) Res Microbiol 155:596–603

    Article  PubMed  Google Scholar 

  12. Leontievsky AA, Myasoedova NM, Golovleva LA (1994) J Biotechnol 32:299–307

    Article  CAS  Google Scholar 

  13. Maltseva OV, Niku-Paavola ML, Leontievsky AA, Myasoedova NM, Golovleva LA (1991) Biotechnol Appl Biochem 13:291–302

    CAS  Google Scholar 

  14. Golovleva LA, Leontievsky AA, Maltseva OV, Myasoedova NM (1993) J Biotechnol 30:71–77

    Article  CAS  Google Scholar 

  15. Lisov AV, Leontievsky AA, Golovleva LA (2003) Biochemistry (Mosc) 68:1027–1035

    Article  CAS  Google Scholar 

  16. Lisov AV, Leontievsky AA, Golovleva LA, Evans CS (2004) J Mol Catal B Enzym 31:1–8

    Article  CAS  Google Scholar 

  17. Lisov AV, Leontievsky AA, Golovleva LA (2005) Biochemistry (Mosc) 70:467–472

    Article  CAS  Google Scholar 

  18. Neuhoff V, Arold N, Taube D, Ehrhardt W (1988) Electrophoresis 9:255–262

    Article  CAS  PubMed  Google Scholar 

  19. Kuan IC, Johnson K, Tien M (1993) J Biol Chem 268:20064–20070

    CAS  PubMed  Google Scholar 

  20. Schlosser D, Höfer C (2002) Appl Environ Microbiol 68:3514–3521

    Article  CAS  PubMed  Google Scholar 

  21. Bard AJ, Faulkner LR (eds) (2002) Electrochemical method, 2nd edn. Wiley, New York

    Google Scholar 

  22. Presnova G, Grigorenko V, Egorov A, Ruzgas T, Lindgren A, Gorton L, Börchers T (2000) Faraday Discuss 116:281–289

    Article  CAS  PubMed  Google Scholar 

  23. Nassar A-EF, Zhang Z, Hu N, Rusling JF, Kumosinski TF (1997) J Phys Chem B 101:2224–2231

    Article  CAS  Google Scholar 

  24. Léger C, Bertrand P (2008) Chem Rev 108:2379–2438

    Article  PubMed  Google Scholar 

  25. Aitken MD, Irvine RL (1990) Arch Biochem Biophys 276:405–414

    Article  CAS  PubMed  Google Scholar 

  26. Hirai H, Sugiura M, Kawai S, Nishida T (2006) FEMS Microbiol Lett 246:19–24

    Article  Google Scholar 

  27. Ruiz-Dueñas FJ, Camarero S, Pérez-Boada M, Martínez MJ, Martínez AT (2001) Biochem Soc Trans 29:116–122

    Article  PubMed  Google Scholar 

  28. Ruiz-Dueñas FJ, Morales M, García E, Miki Y, Martínez MJ, Martínez AT (2009) J Exp Bot 60:441–452

    Article  PubMed  Google Scholar 

  29. Martìnez MJ, Ruiz-Duenas FJ, Guillèn F, Martinez AT (1996) Eur J Biochem 237:424–432

    Article  PubMed  Google Scholar 

  30. Giardina P, Palmieri G, Fontanella B, Rivieccio V, Sannia G (2000) Arch Biochem Biophys 376:171–179

    Article  CAS  PubMed  Google Scholar 

  31. Gelpke MDS, Youngs HL, Gold MH (2000) Eur J Biochem 267:7038–7045

    Article  CAS  PubMed  Google Scholar 

  32. Heinfling A, Ruiz-Dueñas FJ, Martínez MJ, Bergbauer M, Szewzyk U, Martínez AT (1998) FEBS Lett 428:141–146

    Article  CAS  PubMed  Google Scholar 

  33. Camarero S, Sarkar S, Ruiz-Dueñas FJ, Martínez MJ, Martínez AT (1999) J Biol Chem 274:10324–10330

    Article  CAS  PubMed  Google Scholar 

  34. Pérez-Boada M, Ruiz-Dueñas FJ, Pogni R, Basosi R, Choinowski T, Martínez MJ, Piontek K, Martínez AT (2005) J Mol Biol 354:385–402

    Article  PubMed  Google Scholar 

  35. Mc Eldoon JP, Pokora AR, Dordick JS (1995) Enzyme Microb Technol 17:359–365

    Article  CAS  Google Scholar 

  36. Armstrong FA (2002) J Chem Soc Dalton Trans 661–671

  37. Krishtalik LI (2000) Biochim Biophys Acta 1458:6–13

    Article  CAS  PubMed  Google Scholar 

  38. Hirst J (2006) Biochim Biophys Acta 1757:225–239

    Article  CAS  PubMed  Google Scholar 

  39. Ferapontova EE, Castillo J, Gorton L (2006) Biochim Biophys Acta 1760:1343–1354

    CAS  PubMed  Google Scholar 

  40. Santucci R, Bongiovanni C, Marini S, Del Conte R, Tien M, Banci L, Coletta M (2000) Biochem J 349:85–90

    Article  CAS  PubMed  Google Scholar 

  41. Oyadomari M, Shinohara H, Johjima T, Wariishi H, Tanaka H (2003) J Mol Catal B Enzym 21:291–297

    Article  CAS  Google Scholar 

  42. Munteanu F-D, Ruiz-Dueñas FJ, Martínez MJ, Cavaco-Paulo A (2005) J Electroanal Chem 580:35–40

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was carried out with the financial support of “Sapienza” University of Rome and of the European Commission under contract number 017350 (BioMedNano).

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Authors and Affiliations

  1. Dipartimento di Agrobiologia and Agrochimica, Università degli Studi della Tuscia, Via San Camillo de Lellis snc, 01100, Viterbo, Italy

    Maurizio Petruccioli, Daniele Quaratino, Stefano Covino, Federico Federici & Alessandro D’Annibale

  2. Dipartimento di Chimica e Tecnologie del Farmaco, Università La Sapienza, Rome, Italy

    Marco Frasconi, Gabriele Favero & Franco Mazzei

  3. Consorzio Interuniversitario della Chimica per l’Ambiente, Venice, Italy

    Daniele Quaratino

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  1. Maurizio Petruccioli
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  2. Marco Frasconi
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Correspondence to Alessandro D’Annibale.

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Petruccioli, M., Frasconi, M., Quaratino, D. et al. Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79. J Biol Inorg Chem 14, 1153–1163 (2009). https://doi.org/10.1007/s00775-009-0559-8

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  • DOI: https://doi.org/10.1007/s00775-009-0559-8

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