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The DNA sequence for the extracellular lignin peroxidase isozyme H2 from Phanerochaete chrysosporium, obtained from cDNA clone lambda ML-6, was synthesized by PCR and successfully expressed in Escherichia coli under control of the T7 promoter. The portion of the cDNA encoding the signal peptide, not found in the mature native enzyme, was not included. Recombinated lignin peroxidase H2 (rLiPH2) was produced in inclusion bodies in an inactive form. Active enzyme was obtained by refolding with glutathione-mediated oxidation in a medium containing urea, Ca2+, and hemin. The recombinant enzyme had spectral characteristics and kinetic properties identical to that of native enzyme isolated from P. chrysosporium. Surprisingly, rLiPH2, like the native enzyme, also exhibited some manganese peroxidase activity.
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