This is a proposal to investigate an innovative and novel biodegradation system that may be applicable to difficult-to-degrade chemicals or complex mixtures of chemicals. The system is based upon extracellular enzymes that catalyze free radical reactions that evolved to degrade lignin, natures most recalcitrant chemical. Lignin is an insoluble, non-stereoselective, complex heteropolymer. We propose that a system that evolved to degrade lignin should be useful for the biodegradation of a wide variety of very recalcitrant, man-made chemicals. The ultimate objective is to reduce the amount and toxicity of environmental pollutants. The system should be adapted to both aqueous and solid matrices and it may be that availability of the chemical may not be as critical as with other systems. Also, the fungus should have a major competitive advantage if the systems are based upon lignocellulose nutrients. We propose to use a white rot fungus to biologically reduce the risk associated with environmental pollutants in hazardous waste sites or hazardous waste streams. It is a highly integrated yet interdisciplinary program where various areas of expertise are brought to bear on critical subjects of interest to all of the individual investigators. The program will be coordinated with other projects to test the system for the bioremediation of TNT and PCP contaminated soil and HMX contaminated water. The program will be part of and support the Toxicology Degree Program of the Center for Environmental Toxicology. It is expected that several students will pursue a joint Toxicology/Molecular Biology degree. The program will involve faculty in Chemistry and Biochemistry, Biology and Environmental Engineering at Utah State University, and Molecular and Cell Biology at Pennsylvania State University and Chemistry and Biochemistry at Notre Dame. The research will include molecular biology, recombinant DNA technology, enzyme engineering, enzymology, biodegradation studies, factors involved in fungal competition and bioreactor design and engineering.

Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Hazardous Substances Basic Research Grants Program (NIEHS) (P42)
Project #
5P42ES004922-05
Application #
3104511
Study Section
Special Emphasis Panel (SRC (S2))
Project Start
1988-12-07
Project End
1995-03-31
Budget Start
1993-04-01
Budget End
1994-03-31
Support Year
5
Fiscal Year
1993
Total Cost
Indirect Cost
Name
Utah State University
Department
Type
Other Domestic Higher Education
DUNS #
City
Logan
State
UT
Country
United States
Zip Code
84322
Kwon, S I; Anderson, A J (2001) Catalase activities of Phanerochaete chrysosporium are not coordinately produced with ligninolytic metabolism: catalases from a white-rot fungus. Curr Microbiol 42:8-11
Sutherland, G R; Zapanta, L S; Tien, M et al. (1997) Role of calcium in maintaining the heme environment of manganese peroxidase. Biochemistry 36:3654-62
Tatarko, M; Bumpus, J A (1997) Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium. Arch Biochem Biophys 339:200-9
Nie, G; Aust, S D (1997) Effect of calcium on the reversible thermal inactivation of lignin peroxidase. Arch Biochem Biophys 337:225-31
He, B; Sinclair, R; Copeland, B R et al. (1996) The structure-function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase. Biochemistry 35:2413-20
Goodwin, D C; Aust, S D; Grover, T A (1996) Free radicals produced during the oxidation of hydrazines by hypochlorous acid. Chem Res Toxicol 9:1333-9
Whitwam, R; Tien, M (1996) Heterologous expression and reconstitution of fungal Mn peroxidase. Arch Biochem Biophys 333:439-46
Khindaria, A; Yamazaki, I; Aust, S D (1996) Stabilization of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 35:6418-24
Khindaria, A; Aust, S D (1996) EPR detection and characterization of lignin peroxidase porphyrin pi-cation radical. Biochemistry 35:13107-11
Koduri, R S; Whitwam, R E; Barr, D et al. (1996) Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium. Arch Biochem Biophys 326:261-5

Showing the most recent 10 out of 83 publications