Two beta-xylosidases [EC 3.2.1.37], beta-Xyl I (molecular mass 180 kDa, pi 4.7) and beta-Xyl II (molecular mass 190 kDa, pI 3.5), derived from Aspergillus pulverulentus were separated and purified by successive chromatographies and their characterization and transxylosylation were studied. beta-Xyl I and beta-Xyl II were stable at temperatures up to 50 degrees C and from pH 1.5 to 6.5 and 2.5 to 7.0, respectively, while their highest activities were in the pH ranges 2.5-3.5 and 4.0-5.0 at 60 degrees C. Although both enzymes were strongly inhibited by N-bromosuccinimide, the inhibitory effect of HgCl2 was not significant on either. The two enzymes exhibited different resistances against AgNO3, glucono 1,5-lactone and nojirimycin. They were shown to have broad acceptor specificity in transferring the xylosyl residue of xylooligosaccharides to various alcohol and phenolic compound accepters. In the presence of 25% or more 2-propanol, the synthesis of the transfer product, 2-propyl beta-xyloside, was closely consistent with the theoretical yield.