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Appl Environ Microbiol. 1985 May; 49(5): 1040-1045
Copyright © 1985, American Society for Microbiology. All Rights Reserved.

Transformation of Halogen-, Alkyl-, and Alkoxy-Substituted Anilines by a Laccase of Trametes versicolor{dagger}

Thomas Hoff, Shu-Yen Liu and Jean-Marc Bollag*

Laboratory of Soil Microbiology, Department of Agronomy, The Pennsylvania State University, University Park, Pennsylvania 16802

ABSTRACT

The laccase of the fungus Trametes versicolor was able to polymerize various halogen-, alkyl-, and alkoxy-substituted anilines, showing substrate specificity similar to that of horseradish peroxidase, whereas the laccase of Rhizoctonia praticola was active only with p-methoxyaniline. The substrate specificities of the enzymes were determined by using gas chromatography to measure the decrease in substrate concentration during incubation. With p-chloroaniline as the substrate, the peroxidase and the Trametes laccase showed maximum activity near pH 4.2. The transformation of this substrate gave rise to a number of oligomers, ranging from dimers to pentamers, as determined by mass spectrometry. The product profiles obtained by high-pressure liquid chromatography were similar for the two enzymes. A chemical reaction was observed between p-chloroaniline and an enzymatically formed dimer, resulting in the formation of a trimer. All three enzymes oxidized p-methoxyaniline to 2-amino-5-p-anisidinobenzoquinone di-p-methoxyphenylimine, but only the T. versicolor laccase and the peroxidase caused the formation of a pentamer (2,5-di-p-anisidinobenzoquinone di-p-methoxyphenylimine). Our results demonstrate that in addition to horseradish peroxidase, a T. versicolor laccase can also polymerize aniline derivatives.

FOOTNOTES

* Corresponding author.

{dagger} Pennsylvania Agricultural Experiment Station Journal Series no. 7066.

Appl Environ Microbiol. 1985 May; 49(5): 1040-1045
Copyright © 1985, American Society for Microbiology. All Rights Reserved.



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