Enhanced Synergistic Capability of β-Glucosidase Crude Extract Through Zeolite-Mediated Immobilization and Hydrolysis of Specific Substrates

The β-glucosidase has a crucial role in the hydrolysis of lignocellulosic biomass. Supplementing β-glucosidase in hydrolysis can reduce inhibitory effects, leading to increased glucose conversion and release. Additionally, the immobilization of β-glucosidase in zeolite can improve its stability and enable its recyclability. The β-glucosidase from the crude extract was physically adsorbed and immobilized using glutaraldehyde on synthetic and natural zeolites from the Durango region, varying pH, ionic strength, and amount of support. Adsorption of β-glucosidase on synthetic zeolite was better since it improved its stability in a pH range of 6–10 and increased its relative activity at 50 °C. Reusing the immobilized enzyme reached eight consecutive cycles with 41% residual activity using cellobiose. It worked synergistically in the hydrolysis of sodium carboxymethyl cellulose (CMC), increasing glucose release by up to 38%. The results show the immobilization capacity of the crude extracts on zeolite, thus avoiding enzymatic separation and purification and reducing costs, as well as their potential application in the hydrolysis of specific substrates for future industrial applications.