Degradation of persistent organic pollutants (POPs) by laccases isolated from Ganoderma tsugae

CHED 1108

Jason D. Matakas, matakasj@etown.edu and Leah R. Eller, ellerl@etown.edu. Department of Chemistry & Biochemistry, Elizabethtown College, One Alpha Dr, Musser 222, Elizabethtown, PA 17022
Many persistent organic pollutants (POPs) contain aromatic rings, which contribute to the stability and persistence of the molecules. These contaminants accumulate in the environment and present hazards to local wildlife. Redox enzymes have been shown to break down some POPs and present a possible "green" method for environmental remediation. Ganoderma tsugae was collected locally in Elizabethtown, PA. G. tsugae is a wood-rotting fungus that uses the blue-copper enzyme, laccase, to oxidize the phenolic subunits in lignin. G. tusgae was cultured on potato dextrose agar (PDA), as well as malt extract broth containing peptone and cellobiose. From these liquid cultures, laccase enzymes have been isolated and purified. Time-dependent activity analyses were carried out as function of pH and growth conditions using UV-visible spectroscopy. Various aromatic compounds, halogenated and non-halogenated, were exposed to the enzyme and monitored for degradation by gas chromatography, GC-MS spectrometry, and NMR spectroscopy.