beta-D-Glucopyranosidase (betaG, EC 3.2.1.21) has been isolated from some collateral activities, alpha-L-arabinofuranosidase (Ara, EC 3.2.1.55), alpha-L-rhamnopyranosidase (Rha, EC 3.2.1.40), and o-acetylesterase (Est, EC 3.1.1.53), using a commercial enzyme preparation and a simple method economically sustainable for the food industry. The procedure comprises precipitation of extraneous substances by adding ethanol and CaCl2. ultrafiltration, and adsorption, first on bentonite and then on chitosan. The results obtained were the complete isolation of betaG from the above-mentioned activities, a drastic reduction in extraneous compounds, such as brown substances and polysaccharides, and a slight increase in purification.