Purification and Characterization of an Intracellular NADH: Quinone Reductase from Trametes versicolor
2007
Lee, S.S. (Kangwon National University, Chuncheon, Republic of Korea) | Moon, D.S. (Kangwon National University, Chuncheon, Republic of Korea) | Choi, H.T. (Kangwon National University, Chuncheon, Republic of Korea) | Song, H.G. (Kangwon National University, Chuncheon, Republic of Korea), E-mail: [email protected]
Intracellular NADH:quinone reductase involved in degradation of aromatic compounds including lignin was purified and characterized from white rot fungus Trametes versicolor. The activity of quinone reductase was maximal after 3 days of incubation in fungal culture, and the enzyme was purified to homogeneity using ion-exchange, hydrophobic interaction, and gel filtration chromatographies. The purified enzyme has a molecular mass of 41 kDa as determined by SDS-PAGE, and exhibits a broad temperature optimum between 20-40℃, with a pH optimum of 6.0.
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