• Korean Journal of Microbiology
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• v.44 no.2
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• pp.110-115
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• 2008

Acridine was not a substrate for fungal laccase but it was oxidized to acridone in the culture medium of P. cinnabarinus SCH-3. During the cultivation of P. cinnabarinus SCH-3, Laccase was the predominant extracellular phenoloxidase, and 3-hydroxyanthranilic acid (3-HAA) was produced in the early culture. Cinnabarinic acid (CA) was observed to accumulate in the culture medium. When P. cinnabarinus was grown in the culture medium containing acridine, acridine was oxidized to acridone. But when the laccase purified from the culture medium of P. cinnabarinus directly reacted with acridine in sodium tartrate buffer (pH 3.0), The oxidation of acridine did not happen. In contrast, when 3-HAA was added to the buffer that was mixed with laccase and acridine, the acridine was oxidized to acridone. While in vitro studies, the CA was formed from 3-HAA in the presence of purified laccase. The results suggest that the acridine should be oxidized to the acridone through the mediation of 3-HAA by the laccase in the culture medium of P. cinnabarinus SCH-3.