A new assay for lignin-type peroxidases employing the dye azure B

Author:

Archibald F S1

Affiliation:

1. Pulp and Paper Research Institute of Canada, Pointe Claire, Quebec.

Abstract

The discovery in 1983 of fungal "ligninases" capable of catalyzing the peroxidation of nonphenolic aromatic lignin components has been seen as a major advance in understanding how certain basidiomycete fungi can completely degrade lignin. The ability of these lignin-type peroxidases to covert millimolar concentrations of veratryl alcohol to veratraldehyde, indicated by a change in the A310 of veratraldehyde, has become the standard assay for routine quantitation of LP activity. A new assay based on the oxidation of micromolar concentrations of the dye Azure B is presented. Although it is as simple and rapid as the veratryl alcohol assay, it appears to overcome some of the shortcomings of that assay. In particular, interference from UV- and short-wavelength visible-light-absorbing materials is greatly reduced and assay specificity is improved.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference40 articles.

1. Ecotoxicology of dyestuffs-a joint effort by industry;Anliker R.;Ecotoxicol. Environ. Saf.,1979

2. Lignin peroxidases are not important in the biological bleaching and delignification of kraft brownstock by Trametes versicolor;Archibald F.;Appl. Environ. Microbiol.,1992

3. Archibald F. The role of fungus-fiber contact in the biobleaching of kraft brownstock by Trametes (Coriolus) versicolor. Holzforschung in press.

4. .Archibald F. Unpublished data.

5. Decolorization of kraft bleachery effluent chromophores by Coriolus (Trametes) versicolor;Archibald F.;Enzyme Microb. Technol.,1990

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