Lignocellulosic biomass, such as wood and agricultural residues, is an attractive material for fuel ethanol production. To achieve an efficient enzymatic hydrolysis of both cellulose and hemicellulose components in the biomass, the optimization of enzyme composition including not only cellulase but also hemicellulase is important. Our goal is to develop the cellulase and hemicellulase producing-fungi that possess an enzyme composition suitable for saccharificaiton of the biomass pretreated by non-sulfuric technology. To understand cellulase and xylanase components produced by Acremonium cellulolyticus CF2612, which is a strong cellulase-producing mutant strain, the diversity of the enzymes secreted on crystalline cellulose (Solka-floc) and Birch xylan was explored by two-dimensional gel electrophoresis. Seventeen and five of the major components induced by cellulose and xylan, respectively, were analyzed by HPLC peptide mapping. The resulting peptide sequences were assigned using existing databases and a draft genome sequence of A. cellulolyticus wild type strain (unpublished data). Cellobiohydrolase I (CBH I) and CBH II were identified in the gel prepared from the Solka-floc culture with 4 spots each; those accounted for the majority of the protein spots detected in the gel. On the other hand, at least four types of deduced xylanase as well as β-xylosidase were found to express as major proteins in the xylan culture. The single xylanase and CBH I were cross-induced by both cellulose and xylan as major proteins, but no multi-spot of CBH I were observed in the gel prepared from the xylan culture.