Skip to main content
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1994 Aug;60(8):2811–2817. doi: 10.1128/aem.60.8.2811-2817.1994

Anisaldehyde and Veratraldehyde Acting as Redox Cycling Agents for H2O2 Production by Pleurotus eryngii

Francisco Guillén 1,*, Christine S Evans 1
PMCID: PMC201727  PMID: 16349349

Abstract

The existence of a redox cycle leading to the production of hydrogen peroxide (H2O2) in the white rot fungus Pleurotus eryngii has been confirmed by incubations of 10-day-old mycelium with veratryl (3,4-dimethoxybenzyl) and anisyl (4-methoxybenzyl) compounds (alcohols, aldehydes, and acids). Veratraldehyde and anisaldehyde were reduced by aryl-alcohol dehydrogenase to their corresponding alcohols, which were oxidized by aryl-alcohol oxidase, producing H2O2. Veratric and anisic acids were incorporated into the cycle after their reduction, which was catalyzed by aryl-aldehyde dehydrogenase. With the use of different initial concentrations of either veratryl alcohol, veratraldehyde, or veratric acid (0.5 to 4.0 mM), around 94% of veratraldehyde and 3% of veratryl alcohol (compared with initial concentrations) and trace amounts of veratric acid were found when equilibrium between reductive and oxidative activities had been reached, regardless of the initial compound used. At concentrations higher than 1 mM, veratric acid was not transformed, and at 1.0 mM, it produced a negative effect on the activities of aryl-alcohol oxidase and both dehydrogenases. H2O2 levels were proportional to the initial concentrations of veratryl compounds (around 0.5%), and an equilibrium between aryl-alcohol oxidase and an unknown H2O2-reducing system kept these levels steady. On the other hand, the concomitant production of the three above-mentioned enzymes during the active growth phase of the fungus was demonstrated. Finally, the possibility that anisaldehyde is the metabolite produced by P. eryngii for the maintenance of this redox cycle is discussed.

Full text

PDF
2811

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cancel A. M., Orth A. B., Tien M. Lignin and veratryl alcohol are not inducers of the ligninolytic system of Phanerochaete chrysosporium. Appl Environ Microbiol. 1993 Sep;59(9):2909–2913. doi: 10.1128/aem.59.9.2909-2913.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. FARMER V. C., HENDERSON M. E., RUSSELL J. D. Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor. Biochem J. 1960 Feb;74:257–262. doi: 10.1042/bj0740257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. FARMER V. C., HENDERSON M. E., RUSSELL J. D. Reduction of certain aromatic acids to aldehydes and alcohols by Polystictus versicolor. Biochim Biophys Acta. 1959 Sep;35:202–211. doi: 10.1016/0006-3002(59)90349-x. [DOI] [PubMed] [Google Scholar]
  4. Faison B. D., Kirk T. K. Factors Involved in the Regulation of a Ligninase Activity in Phanerochaete chrysosporium. Appl Environ Microbiol. 1985 Feb;49(2):299–304. doi: 10.1128/aem.49.2.299-304.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fawer M. S., Stierli J., Cliffe S., Fiechter A. The characterisation of immobilised lignin peroxidase by flow injection analysis. Biochim Biophys Acta. 1991 Jan 8;1076(1):15–22. doi: 10.1016/0167-4838(91)90214-k. [DOI] [PubMed] [Google Scholar]
  6. Guillén F., Martínez A. T., Martínez M. J. Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii. Eur J Biochem. 1992 Oct 15;209(2):603–611. doi: 10.1111/j.1432-1033.1992.tb17326.x. [DOI] [PubMed] [Google Scholar]
  7. Gutiérrez A., Caramelo L., Prieto A., Martínez M. J., Martínez A. T. Anisaldehyde production and aryl-alcohol oxidase and dehydrogenase activities in ligninolytic fungi of the genus Pleurotus. Appl Environ Microbiol. 1994 Jun;60(6):1783–1788. doi: 10.1128/aem.60.6.1783-1788.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HALLIWELL G. HYDROLYSIS OF FIBROUS COTTON AND REPRECIPITATED CELLULOSE BY CELLULOLYTIC ENZYMES FROM SOIL MICRO-ORGANISMS. Biochem J. 1965 Apr;95:270–281. doi: 10.1042/bj0950270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Haemmerli S. D., Leisola M. S., Sanglard D., Fiechter A. Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase. J Biol Chem. 1986 May 25;261(15):6900–6903. [PubMed] [Google Scholar]
  10. Kappus H., Sies H. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia. 1981 Dec 15;37(12):1233–1241. doi: 10.1007/BF01948335. [DOI] [PubMed] [Google Scholar]
  11. Kersten P. J., Kirk T. K. Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium. J Bacteriol. 1987 May;169(5):2195–2201. doi: 10.1128/jb.169.5.2195-2201.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kirk T. K., Connors W. J., Zeikus J. G. Requirement for a growth substrate during lignin decomposition by two wood-rotting fungi. Appl Environ Microbiol. 1976 Jul;32(1):192–194. doi: 10.1128/aem.32.1.192-194.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kirk T. K., Farrell R. L. Enzymatic "combustion": the microbial degradation of lignin. Annu Rev Microbiol. 1987;41:465–505. doi: 10.1146/annurev.mi.41.100187.002341. [DOI] [PubMed] [Google Scholar]
  14. Kirk T. K., Mozuch M. D., Tien M. Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds. Biochem J. 1985 Mar 1;226(2):455–460. doi: 10.1042/bj2260455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Muheim A., Waldner R., Sanglard D., Reiser J., Schoemaker H. E., Leisola M. S. Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium. Eur J Biochem. 1991 Jan 30;195(2):369–375. doi: 10.1111/j.1432-1033.1991.tb15715.x. [DOI] [PubMed] [Google Scholar]
  16. Pick E., Keisari Y. A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture. J Immunol Methods. 1980;38(1-2):161–170. doi: 10.1016/0022-1759(80)90340-3. [DOI] [PubMed] [Google Scholar]
  17. Valli K., Wariishi H., Gold M. H. Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: role of veratryl alcohol in lignin biodegradation. Biochemistry. 1990 Sep 18;29(37):8535–8539. doi: 10.1021/bi00489a005. [DOI] [PubMed] [Google Scholar]
  18. de Jong E., Cazemier A. E., Field J. A., de Bont J. A. Physiological Role of Chlorinated Aryl Alcohols Biosynthesized De Novo by the White Rot Fungus Bjerkandera sp. Strain BOS55. Appl Environ Microbiol. 1994 Jan;60(1):271–277. doi: 10.1128/aem.60.1.271-277.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. de Jong E., Field J. A., Dings J. A., Wijnberg J. B., de Bont J. A. De-novo biosynthesis of chlorinated aromatics by the white-rot fungus Bjerkandera sp. BOS55. Formation of 3-chloro-anisaldehyde from glucose. FEBS Lett. 1992 Jul 6;305(3):220–224. doi: 10.1016/0014-5793(92)80672-4. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES