Mycobiology

  • 제44권4호
  • /
  • Pages.260-268
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  • 2016
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  • 1229-8093(pISSN)
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  • 2092-9323(eISSN)
한국균학회 (The Korean Society of Mycology)
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Physiological Regulation of an Alkaline-Resistant Laccase Produced by Perenniporia tephropora and Efficiency in Biotreatment of Pulp Mill Effluent

  • 투고 : 2016.07.04
  • 심사 : 2016.09.19
  • 발행 : 2016.12.30
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초록

Regulation of alkaline-resistant laccase from Perenniporia tephropora KU-Alk4 was proved to be controlled by several factors. One important factor was the initial pH, which drove the fungus to produce different kinds of ligninolytic enzymes. P. tephropora KU-Alk4 could grow at pH 4.5, 7.0, and 8.0. The fungus produced laccase and MnP at pH 7.0, but only laccase at pH 8.0. The specific activity of laccase in the pH 8.0 culture was higher than that in the pH 7.0 culture. At pH 8.0, glucose was the best carbon source for laccase production but growth was better with lactose. Low concentrations of glucose at 0.1% to 1.0% enhanced laccase production, while concentrations over 1% gave contradictory results. Veratryl alcohol induced the production of laccase. A trace concentration of copper ions was required for laccase production. Biomass increased with an increasing rate of aeration of shaking flasks from 100 to 140 rpm; however, shaking at over 120 rpm decreased laccase quantity. Highest amount of laccase produced by KU-Alk4, 360 U/mL, was at pH 8.0 with 1% glucose and 0.2 mM copper sulfate, unshaken for the first 3 days, followed by addition of 0.85 mM veratryl alcohol and shaking at 120 rpm. The crude enzyme was significantly stable in alkaline pH 8.0~10.0 for 24 hr. After treating the pulp mill effluent with the KU-Alk4 system for 3 days, pH decreased from 9.6 to 6.8, with reduction of color and chemical oxygen demand at 83.2% and 81%, respectively. Laccase was detectable during the biotreatment process.

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참고문헌

  1. Barr DP, Aust SD. Mechanisms white rot fungi use to degrade pollutants. Environ Sci Technol 1994;28:78A-87A. https://doi.org/10.1021/es00051a724
  2. Hadibarata T, Kristanti RA. Potential of a white-rot fungus Pleurotus eryngii F032 for degradation and transformation of fluorene. Fungal Biol 2014;118:222-7. https://doi.org/10.1016/j.funbio.2013.11.013
  3. Freitas AC, Ferreira F, Costa AM, Pereira R, Antunes SC, Goncalves F, Rocha-Santos TA, Diniz MS, Castro L, Peres I, et al. Biological treatment of the effluent from a bleached kraft pulp mill using basidiomycete and zygomycete fungi. Sci Total Environ 2009;407:3282-9. https://doi.org/10.1016/j.scitotenv.2009.01.054
  4. Chandra R, Singh R. Decolourisation and detoxification of rayon grade pulp paper mill effluent by mixed bacterial culture isolated from pulp paper mill effluent polluted site. Biochem Eng J 2012;61:49-58. https://doi.org/10.1016/j.bej.2011.12.004
  5. Elisashvili V, Kachlishvili E. Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes. J Biotechnol 2009;144:37-42. https://doi.org/10.1016/j.jbiotec.2009.06.020
  6. Manavalan T, Manavalan A, Thangavelu KP, Heese K. Characterization of optimized production, purification and application of laccase from Ganoderma lucidum. Biochem Eng J 2013;70:106-14. https://doi.org/10.1016/j.bej.2012.10.007
  7. Teerapatsakul C, Abe N, Bucke C, Kongkathip N, Jareonkitmongkol S, Chitradon L. Novel laccases of Ganoderma sp. KU-Alk4, regulated by different glucose concentration in alkaline media. World J Microbiol Biotechnol 2007;23:1559-67. https://doi.org/10.1007/s11274-007-9401-z
  8. Teerapatsakul C, Bucke C, Parra R, Keshavarz T, Chitradon L. Dye decolorisation by laccase entrapped in copper alginate. World J Microbiol Biotechnol 2008;24:1367-74. https://doi.org/10.1007/s11274-007-9617-y
  9. Teerapatsakul C, Parra R, Bucke C, Chitradon L. Improvement of laccase production from Ganoderma sp. KU-Alk4 by medium engineering. World J Microbiol Biotechnol 2007;23:1519-27. https://doi.org/10.1007/s11274-007-9396-5
  10. Zheng Z, Schwartz S, Wagner L, Miller W. A greedy algorithm for aligning DNA sequences. J Comput Biol 2000;7:203-14. https://doi.org/10.1089/10665270050081478
  11. Hall TA. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 1999;41:95-8.
  12. Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 2007;24:1596-9. https://doi.org/10.1093/molbev/msm092
  13. Tien M, Kirk TK. Lignin peroxidase of Phanerochaete chrysosporium. Methods Enzymol 1988;161:238-49.
  14. Kondo R, Kurashiki K, Sakai K. In vitro bleaching of hardwood kraft pulp by extracellular enzymes excreted from white rot fungi in a cultivation system using a membrane filter. Appl Environ Microbiol 1994;60:921-6.
  15. Zhao CL, Cui BK. A new species of Perenniporia (Polyporales, Basidiomycota) described from southern China based on morphological and molecular characters. Mycol Prog 2012;11:555-60. https://doi.org/10.1007/s11557-011-0770-1
  16. Ardon O, Kerem Z, Hadar Y. Enhancement of laccase activity in liquid cultures of the ligninolytic fungus Pleurotus ostreatus by cotton stalk extract. J Biotechnol 1996;51:201-7. https://doi.org/10.1016/S0168-1656(96)01597-0
  17. Sethuraman A, Akin DE, Eriksson KE. Production of ligninolytic enzymes and synthetic lignin mineralization by the bird's nest fungus Cyathus stercoreus. Appl Microbiol Biotechnol 1999;52:689-97. https://doi.org/10.1007/s002530051580
  18. Sripuan T, Aoki K, Yamamoto K, Tongkao D, Kumagai H. Purification and characterization of thermostable ${\alpha}$-galactosidase from Ganoderma lucidum. Biosci Biotechnol Biochem 2003;67:1485-91. https://doi.org/10.1271/bbb.67.1485
  19. Galhaup C, Goller S, Peterbauer CK, Strauss J, Haltrich D. Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. Microbiology 2002;148(Pt 7):2159-69. https://doi.org/10.1099/00221287-148-7-2159
  20. Ronne H. Glucose repression in fungi. Trends Genet 1995;11:12-7. https://doi.org/10.1016/S0168-9525(00)88980-5
  21. Arora DS, Gill PK. Effect of various media and supplements on laccase production by some white rot fungi. Bioresour Technol 2001;77:89-91. https://doi.org/10.1016/S0960-8524(00)00114-0
  22. Galhaup C, Haltrich D. Enhanced formation of laccase activity by the white-rot fungus Trametes pubescens in the presence of copper. Appl Microbiol Biotechnol 2001;56:225-32. https://doi.org/10.1007/s002530100636
  23. Revankar MS, Lele SS. Enhanced production of laccase using a new isolate of white rot fungus WR-1. Process Biochem 2006;41:581-8. https://doi.org/10.1016/j.procbio.2005.07.019
  24. Miasoedova NM, Chernykh AM, Psurtseva NV, Belova NV, Golovleva LA. New efficient producers of fungal laccases. Appl Biochem Microbiol 2008;44:73-7. https://doi.org/10.1134/S0003683808010122
  25. Palmieri G, Giardina P, Bianco C, Fontanella B, Sannia G. Copper induction of laccase isoenzymes in the ligninolytic fungus Pleurotus ostreatus. Appl Environ Microbiol 2000;66:920-4. https://doi.org/10.1128/AEM.66.3.920-924.2000
  26. Baldrian P. Interactions of heavy metals with white-rot fungi. Enzyme Microb Technol 2003;32:78-91. https://doi.org/10.1016/S0141-0229(02)00245-4
  27. Collins PJ, Dobson A. Regulation of laccase gene transcription in Trametes versicolor. Appl Environ Microbiol 1997;63:3444-50.
  28. Ben Younes S, Mechichi T, Sayadi S. Purification and characterization of the laccase secreted by the white rot fungus Perenniporia tephropora and its role in the decolourization of synthetic dyes. J Appl Microbiol 2006;102:1033-42.
  29. Songulashvili G, Jimenez-Tobon G, Jaspers C, Penninckx MJ. High production of laccase by Ganoderma lucidum 447 in submerged cultivation on ethanol production residue supplemented with $Cu^{2+}$. Mycosphere 2011;2:507-13.
  30. Hess J, Leitner C, Galhaup C, Kulbe KD, Hinterstoisser B, Steinwender M, Haltrich D. Enhanced formation of extracellular laccase activity by the white-rot fungus Trametes multicolor. Appl Biochem Biotechnol 2002;98-100:229-41. https://doi.org/10.1385/ABAB:98-100:1-9:229
  31. Raj A, Kumar S, Haq I, Singh SK. Bioremediation and toxicity reduction in pulp and paper mill effluent by newly isolated ligninolytic Paenibacillus sp. Ecol Eng 2014;71:355-62. https://doi.org/10.1016/j.ecoleng.2014.07.002
  32. Singh P, Thakur IS. Removal of colour and detoxification of pulp and paper mill effluent by microorganisms in two step bioreactor. J Sci Ind Res 2004;63:944-8.
  33. Bugg TD, Ahmad M, Hardiman EM, Rahmanpour R. Pathways for degradation of lignin in bacteria and fungi. Nat Prod Rep 2011;28:1883-96. https://doi.org/10.1039/c1np00042j
  34. D'Annibale A, Stazi SR, Vinciguerra V, Di Mattia E, Sermanni GG. Characterization of immobilized laccase from Lentinula edodes and its use in olive-mill wastewater treatment. Process Biochem 1999;34:697-706. https://doi.org/10.1016/S0032-9592(98)00144-7
  35. Manzanares P, Fajardo S, Martin C. Production of ligninolytic activities when treating paper pulp effluents by Trametes versicolor. J Biotechnol 1995;43:125-32. https://doi.org/10.1016/0168-1656(95)00125-8