An endo-1,4-beta-glucanase from Bellamya chinensis laeta (BC-EG70a) was expressed in Pichia pastoris GS115. The molecular masses of the mature recombinant BC-EG70a enzyme (rBC-EG70a(mature)), the rBC-EG70a catalytic domain (rBC-EG70(CatD)), and the rBC-EG70a cellulose binding domain (rBC-EG70a(CBD)) were 65 kDa, 50 kDa, and 15 kDa, respectively. While the optimum pH and temperature of rBC-EG70(mature) and rBC-EG70(CatD) were pH 5.5 and 50 C, rBC-EG70(mature) was more stable within a range of pHs and temperatures compared to rBCEG70(CatD). The major hydrolysis products from cellohexaose using rBC-EG70ar, and rBC-EG70(mature) were cellobiose and cellopentaose during the early stages of the hydrolysis reaction. At lower temperature (30 degrees C), the specific activity of rBC-EG70(mature) using carboxymethyl cellulose as the substrate was 5 to 20-fold higher than those of Trichoderma reesei and T. viride cellulases. rBC-EG70(CatD) demonstrated higher activity than rBCEG70(mature) in 10%, 15%, and 20% (v/v) ethanol solutions. rBC-EG70a(CBD) showed specific adsorption toward Avicel, powder cellulose, and phosphoric acid swollen cellulose.