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Title: Regulation of coal polymer degradation by fungi. Fourth quarterly progress report, May 1995--June 1995

Abstract

To test the hypothesis that coal (leonardite) Solubilization and the subsequent depolymerization of the solubilized coal macromolecules are distinct events in lignin degrading fungi. In addition to T versicolor, Phanerochaete chrysosporium, another lignin degrading fungus that also has the ability to solubilize coal, will be studied. To test the hypothesis that the processes of coal (leonardite) solubilization and coal macro molecule depolymerization in lignin degrading fungi can be regulated by altering the nutritional status of the microorganism. Coal solubilization is expected to occur in nutrient rich media whereas depolymerization of solubilized coal macromolecules is expected to occur in nutrient limited media. To determine the role of extracellular enzymes (laccases, lignin peroxidases and Mn peroxidases) that are secreted by lignin degrading fungi during coal solubilization or coal macro molecule depolymerization. To assess the role of enzymatically generated oxygen radicals, non-radical active oxygen species, veratryl alcohol radicals and Mn{sup +++} complexes in coal macro molecule depolymerization. To characterize products of coal solubilization and coal macro molecule depolymerization that are formed by T. versicolor and P. chrysosporium and their respective extracellular enzymes. Solubilization products formed using oxalic acid and other metal chelators will also be characterized and compared.

Authors:
Publication Date:
Research Org.:
Notre Dame Univ., IN (United States). Dept. of Civil Engineering and Geological Sciences
Sponsoring Org.:
USDOE, Washington, DC (United States)
OSTI Identifier:
182624
Report Number(s):
DOE/PC/94209-T4
ON: DE96005018; TRN: 96:001231
DOE Contract Number:  
FG22-94PC94209
Resource Type:
Technical Report
Resource Relation:
Other Information: PBD: 24 Jul 1995
Country of Publication:
United States
Language:
English
Subject:
01 COAL, LIGNITE, AND PEAT; 55 BIOLOGY AND MEDICINE, BASIC STUDIES; COAL; DEPOLYMERIZATION; PEROXIDASES; ENZYME ACTIVITY; PROGRESS REPORT; ENZYMES; FUNGI; PHANEROCHAETE; DISSOLUTION; BIODEGRADATION

Citation Formats

Irvine, R L. Regulation of coal polymer degradation by fungi. Fourth quarterly progress report, May 1995--June 1995. United States: N. p., 1995. Web. doi:10.2172/182624.
Irvine, R L. Regulation of coal polymer degradation by fungi. Fourth quarterly progress report, May 1995--June 1995. United States. https://doi.org/10.2172/182624
Irvine, R L. Mon . "Regulation of coal polymer degradation by fungi. Fourth quarterly progress report, May 1995--June 1995". United States. https://doi.org/10.2172/182624. https://www.osti.gov/servlets/purl/182624.
@article{osti_182624,
title = {Regulation of coal polymer degradation by fungi. Fourth quarterly progress report, May 1995--June 1995},
author = {Irvine, R L},
abstractNote = {To test the hypothesis that coal (leonardite) Solubilization and the subsequent depolymerization of the solubilized coal macromolecules are distinct events in lignin degrading fungi. In addition to T versicolor, Phanerochaete chrysosporium, another lignin degrading fungus that also has the ability to solubilize coal, will be studied. To test the hypothesis that the processes of coal (leonardite) solubilization and coal macro molecule depolymerization in lignin degrading fungi can be regulated by altering the nutritional status of the microorganism. Coal solubilization is expected to occur in nutrient rich media whereas depolymerization of solubilized coal macromolecules is expected to occur in nutrient limited media. To determine the role of extracellular enzymes (laccases, lignin peroxidases and Mn peroxidases) that are secreted by lignin degrading fungi during coal solubilization or coal macro molecule depolymerization. To assess the role of enzymatically generated oxygen radicals, non-radical active oxygen species, veratryl alcohol radicals and Mn{sup +++} complexes in coal macro molecule depolymerization. To characterize products of coal solubilization and coal macro molecule depolymerization that are formed by T. versicolor and P. chrysosporium and their respective extracellular enzymes. Solubilization products formed using oxalic acid and other metal chelators will also be characterized and compared.},
doi = {10.2172/182624},
url = {https://www.osti.gov/biblio/182624}, journal = {},
number = ,
volume = ,
place = {United States},
year = {1995},
month = {7}
}