Ceriporiopsis subvermispora produces endoglucanase and b -glucosidase when cultivated on cellulose or wood, but biodegradation of cellulose during biopulping by C. subvermispora is low even after long periods. To resolve this discrepancy we grew C. subvermispora on Pinus taeda wood chips and purified the major b -glucosidades it produced. Kinetic parameters were determined to clear if this fungus produces enzymes capable of yielding assimilable glucose from wood. C. subvermispora was grown on Pinus taeda wood chips under solid-state fermentation. After 30 days the crude extract obtained from enzyme extraction with sodium acetate buffer 50mM, pH 5.4 was filtrated in membranes with a molecular mass exclusion limit of 100 kDa. Enzyme purification was carried out using successively Sephacryl S-300 gel filtration. The retained fraction attained 76% of b -glucosidase activity with 3.7 fold purification. Two b -glucosidases were detected with molecular mass of 110 kDa and 53 kDa. We have performed a characterization of the enzymatic properties of the b -glucosidase of 110 kDa. The optimum pH and temperature was 3.5 and 60 ^oC respectively. The K_m and V_max values were respectively 3.29 mM and 0.113 m mol  min^-1 for the hydrolysis of p-nitrophenyl-b -glucopyranoside (pNPG) and 2.63 mM and 0.103 m mol  min^-1 , towards cellobiose. b -glucosidase activity was strongly increased by Mn⁺² and Fe⁺³, while Cu⁺² severely inhibited it. The enzyme has an acid pH optimum with similar activity on pNPG and cellobiose and is thus typical b -glucosidase. Considering all this information, it seems that b -glucosidase would have limited substrate concentrations available during wood decay. Cellobiose would be formed only by occasional action of endocellulases on the end of cellulose chains or even by random degradation of cellulose by Fenton reaction.