The highly efficient beta-1,4-glucosidase (BGL)-secreting strain, Pholiota adiposa SKU0714, was isolated and identified based on its morphological features and sequence analysis of internal transcribed spacer (ITS) rDNA. P. adiposa BGL (PaBGL), which contained a carbohydrate moiety, was purified to homogeneity from P. adiposa culture supernatants by 2-step chromatography on DEAE and Sephacryl gel filtration columns. The relative molecular weight of PaBGL was 60 kDa by SDS-PAGE or 59 kDa by size exclusion chromatography, indicating that the enzyme is a monomer. The pH and temperature optima for hydrolysis were 5.0 and 65 degrees C, respectively. PaBGL showed the highest activity towards p-nitrophenyl-beta-D-glucopyranoside (V-max = 4390 U mg protein(-1), K-m = 2.23 mol m(-3)) and cellobiose (V-max = 3460 U mg protein(-1), K-m = 5.60 mol m(-3)) ever reported. Its internal amino acid sequences showed homology with hydrolases from the glycoside hydrolase family 3 (GH3), indicating that PaBGL is a member of the GH3 family. The hydrolysis of rice straw using a commercial cellulase, Celluclast (R) 1.5L, resulted in a higher saccharification yield with the addition of PaBGL than with Novozyme 188. PaBGL may be a good candidate for applications that convert biomasses to biofuels and chemicals. (C) 2013 Elsevier Ltd. All rights reserved.