Biochemical transformations of herbicide-derived anilines: purification and characterization of causative enzymes

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Abstract
From culture filtrate of the soil fungus Geotrichum candidum two extracellular enzymes were separated that were active in transformation of aniline. Using a concentration, salt precipitation, dialysis, and gel filtration sequence, the two enzymes, a peroxidase and an aniline oxidase, were purified 54- and 68-fold, respectively. The characteristics of the partially purified enzymes were compared and were found to be for peroxidase and for aniline oxidase, respectively, as follows: optimal pH = 4.4–5.0 and 4.8–5.4, energy of activation (Q10) = 3.0 and 1.6, apparent Km (aniline) 3.1 × 10−4 and 4.4 × 10−4 M. Km (H2O2) for peroxidase was 2.4 × 10−6, Km (O2) for aniline oxidase was 9.1 × 10−4 M. In the natural soil environment, peroxidase seems to have a greater role in pesticide residue transformation than aniline oxidas

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