A 4.1-kb fragment of chromosomal DNA from the lignocellulose-decomposing actinomyceteStreptomyces viridosporusT7A was previously found to encode a lignin peroxidase gene. However, when cloned intoEscherichia coliin pBSKS+, peroxidase activity was not expressed. When cloned in pIJ702 inStreptomyces lividans, the gene was expressed in a peroxidase positive background, owing to the production byS. lividansof its own extracellular peroxidases. To circumvent these problems, the DNA was cloned into the commercial expression vector pIC9 for extracellular expression in the yeastPichia pastoris. Yeast transformants, however, expressed two activities, extracellular peroxidase and an extracellular endoglucanase. The enzymes were not expressed by the yeast cells alone or by yeast cells with pIC9 without the insert. Expression of the enzymes by only those transformants expressing the 4.1-kb DNA was confirmed by Western blot analyses, by nondenaturing activity gel staining, and by spectrophotometric enzyme assays of extracellular culture filtrates. Activity gel staining showed that the two activities resided in different proteins and the peroxidase expressed was similar to ALip-P3, one of the isoenzymes of lignin peroxidase of theS. viridosporusT7A wildtype. Other evidence indicated that in the transformants, the peroxidase and endoglucanase genes in the 4.1-kb insert were controlled by the methanol-inducible AOX1 yeast promoter in pIC9, since their expression was induced by methanol. In the best transformants, extracellular production of peroxidase by recombinantP. pastoriscultures was significantly higher than typically observed inS. viridosporus. The results also indicate that lignocellulose catabolism genes may be clustered on theS. viridosporuschromosome.Key words: lignocellulose, degradation,Streptomyces, peroxidase, endoglucanase, cloning, pIC9,Pichia pastoris.