Screening of lignin peroxidase from white-rot fungi

IRG/WP 98-10274

I Momohara

Since lignin peroxidase was first found in the ligninolytic culture of Phanerochaete chrysosporium, it has been regarded as an enzyme responsible for the lignin biodegradation and studied comprehensively. As the results of these studies its unique characteristics have been revealed. On the other hand, the features of lignin peroxidase produced by other white-rot fungi have not been studied so much. In this study, over 80 white-rot fungi were examined for their ability to produce lignin peroxidase. Five fungi produced lignin peroxidase, and they were subjected to further investigations. These lignin peroxidases showed higher activity at pH 3.5 than pH 4.5 in the oxidation of veratryl alcohol. It could oxidize guaiacol slowly. These features are similar to those from P. chrysosporium. Newly isolated lignin peroxidase were inactivated by the reaction with hydrogen peroxide. There was a difference in the rates of the inactivation by the hydrogen peroxide treatment. The rate observed in the inactvation of lignin peroxidase from P. chrysosporium was moderate.


Keywords: LIGNIN PEROXIDASE; WHITE-ROT FUNGI; VERATRYL ALCOHOL; HYDROGEN PEROXIDE; INACTIVATION

Conference: 98-06-14/19 Maastricht, The Low Countries


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