This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Raghukumar, C.
Right arrow Articles by Reddy, C. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Raghukumar, C.
Right arrow Articles by Reddy, C. A.
Agricola
Right arrow Articles by Raghukumar, C.
Right arrow Articles by Reddy, C. A.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, May 1999, p. 2103-2111, Vol. 65, No. 5
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Lignin-Modifying Enzymes of Flavodon flavus, a Basidiomycete Isolated from a Coastal Marine Environmentdagger

C. Raghukumar,Dagger T. M. D'Souza, R. G. Thorn,§ and C. A. Reddy*

Department of Microbiology and NSF Center for Microbial Ecology, Michigan State University, East Lansing, Michigan 48824-1101

Received 6 November 1998/Accepted 11 February 1999

A basidiomycetous fungus Flavodon flavus (Klotzsch) Ryvarden (strain 312), isolated from decaying sea grass from a coral lagoon off the west coast of India, mineralized nearly 24% of 14C-labeled synthetic lignin to 14CO2 in 24 days. When grown in low-nitrogen medium (2.4 mM N) this fungus produced three major classes of extracellular lignin-modifying enzymes (LMEs): manganese-dependent peroxidase (MNP), lignin peroxidase (LIP), and laccase. Low MNP and laccase activities were seen in high-nitrogen medium (24 mM N), but no LIP activity was seen. In media containing lignocellulosic substrates such as pine, poplar, or sugarcane bagasse as the sole source of carbon and nitrogen, relatively high MNP and moderate levels of laccases were seen, but LIP production either was not seen or was minimal. LME production was also seen in media prepared with artificial seawater. Fast protein liquid chromatography and isoelectric focusing resolved LMEs into four isozymes each of MNP and LIP, while laccase isozymes were resolved into two groups, one group containing seven isozymes (pIs 4 to 6) and the other group containing at least three isozymes (pIs < 3). The molecular masses of the different isozymes were 43 to 99 kDa for MNP, 40 and 41.5 kDa for LIP, and 43 and 99 kDa for laccase. F. flavus showed effective degradation of various dye pollutants in media prepared with or without artificial seawater. This is the first report on the production of all three major classes of LMEs by F. flavus and points to the bioremediation potential of this organism in terrestrial as well as marine environments.


* Corresponding author. Mailing address: Department of Microbiology, Michigan State University, East Lansing, MI 48824-1101. Phone: (517) 355-6499. Fax: (517) 353-8767. E-mail: reddy{at}pilot.msu.edu.

dagger NIO contribution number 2632.

Dagger Present address: National Institute of Oceanography, Dona Paula, Goa 403 004, India.

§ Present address: Department of Botany, University of Wyoming, Laramie, WY 82071-3165.


Applied and Environmental Microbiology, May 1999, p. 2103-2111, Vol. 65, No. 5
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Kamei, I., Daikoku, C., Tsutsumi, Y., Kondo, R. (2008). Saline-Dependent Regulation of Manganese Peroxidase Genes in the Hypersaline-Tolerant White Rot Fungus Phlebia sp. Strain MG-60. Appl. Environ. Microbiol. 74: 2709-2716 [Abstract] [Full Text]  
  • Borokhov, O., Rothenburger, S. (2000). Rapid Dye Decolorization Method for Screening Potential Wood Preservatives. Appl. Environ. Microbiol. 66: 5457-5459 [Abstract] [Full Text]