A comparison was made of the hydrolysis of microcrystalline cellulose Avicel using the cellulolytic complex of the ascomycete Morchella conica and a commercial cellulase. An enzyme concentration of 1 U AVase mg-1 substrate gave the best results during the hydrolytic processes. At 24 h, the M. conica enzyme complex achieved 35.5% and the commercial cellulase 31.2% saccharification, with glucose 84.2% and 52% of the total reducing sugars liberated, respectively. The specific rates of hydrolyses were 0.77 and 0.14 h-1 for reducing sugars and 0.54 and 0.12 h-1 for glucose formation with M. conica and the commercial cellulase, respectively. At 96 h, the degree of saccharification reached 46% for M. conica and 49% for the commercial cellulase, with glucose 76.5% and 65.9% of the total reducing sugars liberated, respectively. Both the complexes were quite stable with a residual activity of 62% CMCase and 47% AVase for M. conica, and 74% CMCase and 57% AVase for the commercial cellulase at 96 h of hydrolysis. The qualitative analysis of the hydrolysis products by TLC indicated, for M. conica, an earlier appearance of cellobiose, which was quickly hydrolyzed to glucose.