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Molecular Biology Reports

, Volume 46, Issue 1, pp 569–580 | Cite as

Cloning, characterization and paper pulp applications of a newly isolated DyP type peroxidase from Rhodococcus sp. T1

  • Miray Sahinkaya
  • Dilsat Nigar Colak
  • Aysegul Ozer
  • Sabriye Canakci
  • Ilhan Deniz
  • Ali Osman BelduzEmail author
Original Article
  • 185 Downloads

Abstract

A newly identified ligninolytic Rhodococcus strain (Rhodococcus sp. T1) was isolated from forestry wastes (Trabzon/Turkey). The DyP type peroxidase of Rhodococcus sp. T1 (DyPT1) was cloned, characterized and paper treated for industrial applications. Molecular weight of the protein was about 38 kDa. The kinetic parameters were 0.94 mM and 1417.53 µmol/min/mg for Km and Vmax, respectively. The enzyme was active at the temperature range of 25–65 °C and optimum temperature was 35 °C, enzyme was stable up to 6 days at room temperature. Optimum pH of the DyPT1 was 4.0 and it was stable between pH 4.0–6.0 up to 8 days at room temperature. Effects of some metal ions, Hemin, and some chemical agents on DyPT1 were determined. Hemin has implemented protective effects on the stability and the activity of the enzyme in long time periods when added into growing medium. DyPT1 was applied to eucalyptus kraft pulp for analyzing the bleaching efficiency, physical and optical tests of the manufuctared paper were carried out. Application of lignin peroxidase to kraft pulp caused a decrease of 5.2 units for kappa number and an increase from 52.05 to 64.18% in the delignification rate.

Keywords

Pulp bleaching Lignin peroxidase Rhodococcus sp. Kappa number 

Notes

Acknowledgements

This study was financially supported by Karadeniz Technical University Research Foundation (Project No: FBA-2015-5182).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

References

  1. 1.
    Asinaa FNU, Brzonovaa I, Kozliakb E, Kubátováb A, Jia Y (2017) Microbial treatment of industrial lignin: successes, problems and challenges. Renew Sustain Energy Rev 77:1179–1205CrossRefGoogle Scholar
  2. 2.
    Viikari L, Ranva M, Kantelinen A, Sandquist J, Lınko M (1986) Biotechnology in Pulp and Paper Industry, 3rd International Conference, pp 66–69Google Scholar
  3. 3.
    Beg QK, Kapoor M, Mahajan L, Hoondal GS (2001) Microbial xylanases and their industrial applications: a review. Appl Microbiol Biotechnol 56:326–338CrossRefGoogle Scholar
  4. 4.
    Ahmad M, Roberts JN, Hardiman EM, Singh R, Eltis RD, Bugg TDH (2011) Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase. Biochemistry 50:5096–5107CrossRefGoogle Scholar
  5. 5.
    Bugg TDH, Rahmanpour R (2015) Enzymatic conversion of lignin into renewable chemicals. Curr Opin Chem Biol 29:10–17CrossRefGoogle Scholar
  6. 6.
    Rahmanpour R, Bugg TDH (2015) Characterisation of Dyp-type peroxidases from Pseudomonas fluorescens Pf-5: oxidation of Mn(II) and polymeric lignin by Dyp1B. Arch Biochem Biophys 574:93–98CrossRefGoogle Scholar
  7. 7.
    Wong DWS (2009) Structure and action mechanism of ligninolytic enzymes. Appl Biochem Biotechnol 157:174–209CrossRefGoogle Scholar
  8. 8.
    Hammel KE, Cullen DE (2008) Role of fungal peroxidases in biological ligninolysis. Curr Opin Plant Biol 11:349–355CrossRefGoogle Scholar
  9. 9.
    Kim SJ, Shoda M (1999) Purification and characterization of a novel peroxidase from Geotrichum candidum Dec1 involved in decolorization of dyes. Appl Environ Microbiol 65:1029–1035Google Scholar
  10. 10.
    Yoshida T, Sugano Y (2015) A structural and functional perspective of DyP-type peroxidase family. Arch Biochem Biophys 574:49–55CrossRefGoogle Scholar
  11. 11.
    Chen C, Shrestha R, Jia K, Gao PF, Geisbrecht BV, Bossmann SH, Shi J, Li P (2015) Characterization of dye-decolorizing peroxidase (DyP) from Thermomonospora curvata reveals unique catalytic properties of A-type DyPs. J Biol Chem 290(38):23447–23463CrossRefGoogle Scholar
  12. 12.
    Fawal N, Li Q, Savelli B, Brette M, Passaia G, Fabre M (2013) PeroxiBase: a database for large-scale evolutionary analysis of peroxidases. Nucleic Acids Res 41:441–444CrossRefGoogle Scholar
  13. 13.
    Singh R, Grigg JC, Armstrong Z, Murphy MEP, Eltis LD (2012) Distal heme pocket residues of B-type dye-decolorizing peroxidase: arginine but not aspartate is essential for peroxidase activity. J Biol Chem 287:10623–10630CrossRefGoogle Scholar
  14. 14.
    Sugano Y (2009) DyP-type peroxidases comprise a novel heme peroxidase family. Cell Mol Life Sci 66:1387–1403CrossRefGoogle Scholar
  15. 15.
    Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning—a laboratory manual, 2nd edn. Cold Spring Habour Laboratory Press, New YorkGoogle Scholar
  16. 16.
    Beffa RS, Hofer RM, Thomas M, Meins F Jr (1996) Decreased susceptibility to viral disease of [beta]-1,3-glucanase-deficient plants generated by antisense transformation. Plant Cell 8:1001–1011CrossRefGoogle Scholar
  17. 17.
    Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254CrossRefGoogle Scholar
  18. 18.
    Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227:680–685CrossRefGoogle Scholar
  19. 19.
    Mliki A, Zimmermann W (1992) Purification and characterization of an intracellular peroxidase from Streptomyces cyaneus. Appl Environ Microbiol 58(3):916–919Google Scholar
  20. 20.
    Lineweaver H. Burk D (1934) The determination of enzy me dissociation constant. J Am Chem Soc 56:658CrossRefGoogle Scholar
  21. 21.
    Ahmad M, Taylor CR, Pink D et al (2010) Development of novel assays for lignin degradation: comparative analysis of bacterial and fungal lignin degraders. Mol Biosyst 6:815–821CrossRefGoogle Scholar
  22. 22.
    Crawford DL (1978) Lignocellulose decomposition by selected streptomyces strains. Appl Environ Microbiol 35:1041–1045Google Scholar
  23. 23.
    Spiker J, Crawford D, Thiel E (1992) Oxidation of phenolic and non-phenolic substrates by the lignin peroxidase of Streptomyces viridosporus T7A. Appl Microbiol Biotechnol 37:518–523CrossRefGoogle Scholar
  24. 24.
    Davis JR et al (2013) Genome sequence of Streptomyces viridosporus strain T7A ATCC 39115, a lignin-degrading actinomycete. Genome Announc 1(4):e00416–e00413CrossRefGoogle Scholar
  25. 25.
    Zimmermann W (1990) Degradation of lignin by bacteria. J Biotechnol 13:119–130CrossRefGoogle Scholar
  26. 26.
    Ghodake GS, Kalme SD, Jadhav JP, Govindwar SP (2009) Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes. Appl Biochem Biotechnol 152(1):6–14CrossRefGoogle Scholar
  27. 27.
    Graceffa P, Jancsó A, Mabuchi K (1992) Modification of acidic residues normalizes sodium dodecyl sulfate-polyacrylamide gel electrophoresis of caldesmon and other proteins that migrate anomalously. Arch Biochem Biophys 297(1):46–51CrossRefGoogle Scholar
  28. 28.
    English AM, Tsaprailis G (1995) Catalytic structure–function relationships in heme peroxidases. Adv Inorg Chem 43:79–125CrossRefGoogle Scholar
  29. 29.
    Santos A, Mendes S, Brissos V, Martins LO (2014) New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications. Appl Microbiol Biotechnol 98:2053–2065CrossRefGoogle Scholar
  30. 30.
    Colpa DI, Fraaije MW, van Bloois E (2013) DyP-type peroxidases: a promising and versatile class of enzymes. J Ind Microbiol Biotechnol 41:1–7CrossRefGoogle Scholar
  31. 31.
    Sun Y, Fenster M, Yu A, Berry RM, Argyropoulos DS (1998) The effect of metal ions on the reaction of hydrogen peroxide with Kraft lignin model compounds. Can J Chem 77:667–675CrossRefGoogle Scholar
  32. 32.
    Ogola HJO, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, Shibata H, Sawa Y (2009) Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. App. Environ Microbiol 75(23):7509–7518CrossRefGoogle Scholar
  33. 33.
    Li J, Liu C, Li B, Yuan H, Yang J, Zheng B (2012) Identification and molecular characterization of a novel DyP-type peroxidase from Pseudomonas aeruginosa PKE117. Appl Biochem Biotechnol 166:774–785CrossRefGoogle Scholar
  34. 34.
    Bajpai P (1999) Application of enzymes in the pulp and paper industry. Biotechnol Prog 15:147–157CrossRefGoogle Scholar
  35. 35.
    Antonopoulos VT, Hernandez M, Arias ME, Mavrakos E, Ball AS (2001) The use of extracellular enzyme from Streptomyces albusi ATCC 3005 for the bleaching of eucalyptus kraft pulp. Appl Microbiol Biotechnol 57(1–2):92–97Google Scholar
  36. 36.
    De Carvalho ME, Monteiro MC, Bon EPS, Santanna GL (1998) Production and characterization of phanerochaete chrysosporium lignin peroxidases for pulp bleaching. Appl Biochem Biotechnol 70–72:955–966CrossRefGoogle Scholar
  37. 37.
    Eugenio ME, Hernández M, Moya R, Martín-Sampedro R, Villar JC, Arias ME (2011) Evaluation of a new laccase produced by Streptomyces ipomoea on biobleaching and ageing of kraft pulps. Bioresources 6:3231–3241Google Scholar
  38. 38.
    Lin X, Han S, Zhang N, Hu H, Zheng S, Ye Y, Lin Y (2013) Bleach boosting effect of xylanase A from Bacillus halodurans C-125 in ECF bleaching of wheat straw pulp. Enzyme Microb Technol 52:91–98CrossRefGoogle Scholar
  39. 39.
    Kim DH, Paik KH (2000) Effect of xylanase pre- and post-treatment on oxygen bleaching of Oak kraft pulp. J Indus Eng Chem 6(3):194–200Google Scholar
  40. 40.
    Saleem M, Tabassum MR, Yasmin R, Imran M (2009) Potential of xylanase from thermophilic Bacillus sp. XTR-10 in biobleaching of wood kraft pulp. Biodeterior Biodegrad 63:1119–1124CrossRefGoogle Scholar
  41. 41.
    Bissoon S, Christov L, Singh S (2002) Bleach boosting effects of purified xylanase from Thermomyces lanuginosus SSBP on bagasse pulp. Pro Biochem 38:567–572CrossRefGoogle Scholar
  42. 42.
    Comlekcioglu U, Tutus A, Cicekler M, Gunes M, Aygan A (2014) Application of recombinant xylanase from Orpinomyces sp. in elemental chlorine-free bleaching of kraft pulps. Rom Biotechnol Lett 19:8941–8950Google Scholar
  43. 43.
    Sharma P, Sood C, Singh G, Capalash N (2015) An eco-friendly process for biobleaching of eucalypts kraft pulp with xylanase producing Bacillus halodurans. J Clean Prod 87:966–970CrossRefGoogle Scholar
  44. 44.
    Sondhi S, Sharma P, George N, Chauhan PS, Puri N, Gupta N (2015) An extracellular thermo-alkali-stable laccase from Bacillus tequilensis SN4, with a potential to biobleach softwood pulp. 3 Biotech 5:175–185CrossRefGoogle Scholar
  45. 45.
    Singh G, Ahuja N, Batish M, Capalash N, Sharma P (2008) Biobleaching of wheat straw-rich soda pulp with alkalophilic laccase from gamma-proteobacterium JB: optimization of process parameters using response surface methodology. Bioresour Technol 99:7472–7479CrossRefGoogle Scholar
  46. 46.
    Faison BDT, Kirk K, Farrell RL (1986) Role of veratryl alcohol in regulating ligninase activity in Phanerochaete chrysosporium. AppI Environ Microbiol 52:251–254Google Scholar
  47. 47.
    Arbeloa M, De Leseuc J, Goma G, Pommier JC (1992) An evaluation of the potential of lignin peroxidases to improve pulps. Tappi J 75:215–221Google Scholar

Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  • Miray Sahinkaya
    • 1
  • Dilsat Nigar Colak
    • 2
  • Aysegul Ozer
    • 1
  • Sabriye Canakci
    • 1
  • Ilhan Deniz
    • 3
  • Ali Osman Belduz
    • 1
    Email author
  1. 1.Department of Biology, Faculty of SciencesKaradeniz Technical UniversityTrabzonTurkey
  2. 2.Department of Forestry, Vocational School of DereliGiresun UniversityGiresunTurkey
  3. 3.Department of Forest Industrial Engineering, Faculty of ForestryKaradeniz Technical UniversityTrabzonTurkey

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