A versatile peroxidase, purified from a novel strain of Bjerkandera sp. (B33/3), was tested for its reactivity on a lignin fraction obtained from straw pulping. The effects of such processing parameters as reaction time, pH, and lignin:enzyme ratio were evaluated. Gel filtration chromatography was employed to characterise the molecular mass distribution of the lignin fragments produced by the enzyme-mediated reaction. Our results have shown that such a versatile peroxidase can directly bring about transformations of lignin, even in the absence of external mediators.