Differences in the secretion pattern of oxidoreductases from Bjerkandera adusta induced by a phenolic olive mill extract

Fungal Genetics and Biology

Volumn 72, Issue , 2014, Pages 99-105

  Reina, Rocío ^a   Kellner, Harald ^b   Jehmlich, Nico ^c,d   Ullrich, René ^b   García Romera, Inmaculada ^a   Aranda, Elisabet ^a   Liers, Christiane ^b  

^a CSIC   (Spain)

^b International Graduate School Zittau   (Germany)

^c UNIVERSITY MEDICINE GREIFSWALD   (Germany)

^d HELMHOLTZ CENTRE FOR ENVIRONMENTAL RESEARCH UFZ   (Germany)

Author keywords

Aryl alcohol oxidase; Dehydrogenated lignin polymer; Heme peroxidase; Olive mill residue; Secretome; White rot

Indexed keywords

ALCOHOL OXIDASE; FUNGAL ENZYME; GLUCOSE OXIDASE; LIGNIN PEROXIDASE; MANGANESE PEROXIDASE; OXIDOREDUCTASE; PEROXIDASE; PROTEIN VP1; CULTURE MEDIUM; FUNGAL PROTEIN; PLANT EXTRACT; PROTEOME;

ARTICLE; BIOTRANSFORMATION; BJERKANDERA; BJERKANDERA ADUSTA; CONTROLLED STUDY; DETOXIFICATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME PURIFICATION; ENZYME RELEASE; FAST PROTEIN LIQUID CHROMATOGRAPHY; FLOW RATE; MASS SPECTROMETRY; NONHUMAN; OLIVE; OXIDATION; PRINCIPAL COMPONENT ANALYSIS; PROTEIN CONTENT; PROTEOMICS; CHEMISTRY; CORIOLACEAE; CULTURE MEDIUM; DRUG EFFECTS; ENZYMOLOGY; GENE EXPRESSION; GENETICS; METABOLISM; OLIVE TREE; SECRETION (PROCESS);

CORIOLACEAE; CULTURE MEDIA; FUNGAL PROTEINS; GENE EXPRESSION; OLEA; OXIDOREDUCTASES; PLANT EXTRACTS; PROTEOME;

EID: 84908545441     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2014.07.009     Document Type: Article

References (50)

1. Aranda E., et al. Contribution of hydrolytic enzymes produced by saprophytic fungi to the decrease in plant toxicity caused by water-soluble substances in olive mill dry residue. Appl. Microbiol. Biotechnol. 2004, 64:132-135.
2. Aranda E., et al. Phenolic removal of olive-mill dry residues by laccase activity of white-rot fungi and its impact on tomato plant growth. Int. Biodeter. Biodegr. 2006, 58:176-179.
3. Binder M., et al. Phylogenetic and phylogenomic overview of the polyporales. Mycologia 2013, 105:1350-1375.
4. Camarero S., et al. Description of a versatile peroxidase involved in natural degradation of lignin that has both Mn-peroxidase and lignin-peroxidase substrate binding sites. J. Biol. Chem. 1999, 274:10324-10330.
5. Carabajal M., et al. The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase. J. Biotechnol. 2013, 168:15-23.
6. Colpa D., et al. DyP-type peroxidases: a promising and versatile class of enzymes. J. Ind. Microbiol. Biotechnol. 2014, 41:1-7.
7. Cordova J., et al. Lipase production by solid state fermentation of olive cake and sugar cane bagasse. J. Mol. Catal. - B Enzym. 1998, 5:75-78.
8. Delmas S., et al. Uncovering the genome-wide transcriptional responses of the filamentous fungus Aspergillus niger to lignocellulose using RNA sequencing. PLoS Genet. 2012, 8.
9. Díaz R., et al. Biochemical and molecular characterization of Coriolopsis rigida laccases involved in transformation of the solid waste from olive oil production. Appl. Microbiol. Biotechnol. 2010, 88:133-142.
10. García-Sánchez M., et al. Defence response of tomato seedlings to oxidative stress induced by phenolic compounds from dry olive mill residue. Chemosphere 2012, 89:708-716.
11. Girard V., et al. Secretomes: the fungal strike force. Proteomics 2013, 13:597-608.
12. Hammel K.E., et al. Reactive oxygen species as agents of wood decay by fungi. Enzyme Microb. Technol. 2002, 30:445-453.
13. Hatakka A. Lignin-modifying enzymes from selected white-rot fungi: production and role from in lignin degradation. FEMS Microbiol. Rev. 1994, 13:125-135.
14. Hofrichter M., et al. New and classic families of secreted fungal heme peroxidases. Appl. Microbiol. Biotechnol. 2010, 87:871-897.
15. Hölker U., et al. Biotechnological advantages of laboratory-scale solid-state fermentation with fungi. Appl. Microbiol. Biotechnol. 2004, 64:175-186.
16. Kaal E.E.J., et al. Stimulation of ligninolytic peroxidase activity by nitrogen nutrients in the white rot fungus Bjerkandera sp. strain BOS55. Appl. Environ. Microbiol. 1993, 59:4031-4036.
17. Kapich A.N., et al. Oxidizability of unsaturated fatty acids and of a non-phenolic lignin structure in the manganese peroxidase-dependent lipid peroxidation system. Enzyme Microb. Technol. 2010, 46:136-140.
18. Kapich A.N., et al. Comparative evaluation of manganese peroxidase-and Mn (III)-initiated peroxidation of C18 unsaturated fatty acids by different methods. Enzyme Microb. Technol. 2011, 49:25-29.
19. Kersten P., Cullen D. Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium. Fungal Genet. Biol. 2007, 44:77-87.
20. Kuhad R.C., et al. Microbial cellulases and their industrial applications. Enzyme Res. 2011.
21. Laufenberg G., et al. Transformation of vegetable waste into value added products: (A) the upgrading concept; (B) practical implementations. Bioresource Technol. 2003, 87:167-198.
22. Liers C., et al. Patterns of lignin degradation and oxidative enzyme secretion by different wood- and litter-colonizing basidiomycetes and ascomycetes grown on beech-wood. FEMS Microbiol. Ecol. 2011, 78:91-102.
23. Liers C., et al. Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases. J. Mol. Cat. B-Enzym. 2013, 103:41-46.
24. Martínez Á T., et al. Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin. I. Microbiol. 2005, 8:195-204.
25. Martínez Á T., et al. Enzymatic delignification of plant cell wall: from nature to mill. Curr. Opin. Biotechnol. 2009, 20:348-357.
26. Martinez D., et al. Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion. Proc. Natl. Acad. Sci. USA 2009, 106:1954-1959.
27. Marx I.J., et al. Comparative secretome analysis of Trichoderma asperellum S4F8 and Trichoderma reesei Rut C30 during solid-state fermentation on sugarcane bagasse. Biotechnol. Biofuels 2013, 6.
28. Morin E., et al. Genome sequence of the button mushroom Agaricus bisporus reveals mechanisms governing adaptation to a humic-rich ecological niche. Proc. Natl. Acad. Sci. USA 2012, 109:17501-17506.
29. Muheim A., et al. An extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta. Enzyme Microb. Technol. 1990, 12:204-209.
30. Orth A.B., et al. Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi. Appl. Environ. Microbiol. 1993, 59:4017-4023.
31. Pandey A. Solid-state fermentation. Biochem. Eng. J. 2003, 13:81-84.
32. Rampitsch C., et al. Comparative secretome analysis of Fusarium graminearum and two of its non-pathogenic mutants upon deoxynivalenol induction in vitro. Proteomics 2013, 13:1913-1921.
33. Reina R., et al. Solid state fermentation of olive mill residues by wood- and dung-dwelling Agaricomycetes: effects on peroxidase production, biomass development and phenol phytotoxicity. Chemosphere 2013, 93:1406-1412.
34. Ruiz-Dueñas F.J., et al. Lignin-degrading peroxidases in Polyporales: an evolutionary survey based on 10 sequenced genomes. Mycologia 2013, 105:1428-1444.
35. Salgado J.M., et al. Integrated use of residues from olive mill and winery for lipase production by solid state fermentation with Aspergillus sp. Appl. Biochem. Biotechnol. 2013, 10.1007/s12010-013-0613-4.
36. Salvachua D., et al. Differential proteomic analysis of the secretome of Irpex lacteus and other white-rot fungi during wheat straw pretreatment. Biotechnol. Biofuels 2013, 6:115.
37. Sampedro I., et al. Organic matter transformation and detoxification in dry olive mill residue by the saprophytic fungus Paecilomyces farinosus. Process Biochem. 2009, 44:216-225.
38. Siles J.A., et al. Short-term dynamics of culturable bacteria in a soil amended with biotransformed dry olive residue. Syst. Appl. Microbiol. 2013, 37:113-120.
39. 13C NMR spectroscopic characterisation of six dimeric arylglycerol-ß-aryl ether model compounds representative of syringyl and p-hydroxyphenyl structures in lignins. On the aldol reaction in ß-ether preparation. Holzforschung 1995, 49:325-331.
40. Ten Have R., Teunissen P.J.M. Oxidative mechanisms involved in lignin degradation by white-rot fungi. Chem. Rev. 2001, 101:3397-3413.
41. Vizcaíno J.A., et al. ProteomeXchange provides globally coordinated proteomics data submission and dissemination. Nat. Biotechnol. 2014, 30:223-226.
42. Wariishi H., et al. Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: kinetic mechanism and role of chelators. J. Biol. Chem. 1992, 267:23688-23695.
43. Wold S., et al. Principal component analysis. Chemom. Intell. Lab. Syst. 1987, 2:37-52.
44. Wong D.W. Feruloyl esterase. Appl. Biochem. Biotechnol. 2006, 133:87-112.
45. Wymelenberg A.V., et al. The Phanerochaete chrysosporium secretome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium. J. Biotechnol. 2005, 118:17-34.
46. Wymelenberg A.V., et al. Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identification of peptides in ligninolytic cultures reveal complex mixtures of secreted proteins. Fungal Genet. Biol. 2006, 43:343-356.
47. Wymelenberg A.V., et al. Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium. Appl. Environ. Microbiol. 2006, 72:4871-4877.
48. Wymelenberg A.V., et al. Transcriptome and secretome analyses of Phanerochaete chrysosporium reveal complex patterns of gene expression. Appl. Environ. Microbiol. 2009, 75:4058-4068.
49. Wymelenberg A.V., et al. Comparative transcriptome and secretome analysis of wood decay fungi Postia placenta and Phanerochaete chrysosporium. Appl. Environ. Microbiol. 2010, 76:3599-3610.
50. Zybailov B., et al. Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae. J. Proteome Res. 2006, 5:2339-2347.