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KMID : 0364820080440020110
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Korean Journal of Microbiology
2008 Volume.44 No. 2 p.110 ~ p.115
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Oxidation of Acridine by Laccase of Pycnoporus cinnabarinus SCH-3
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Lee Hyoun-Su
Yoon Kyoung-Ha
Han Man-Deuk
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Abstract
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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.
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KEYWORD
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3-hydroxyanthranilic acid, acridine, acridone, cinnabarinic acid, laccase, Pycnoporus cinnabarinus
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