Abstract
β-glucosidase was used as catalyst for the hydrolysis of cellobiose, immobilized on different supports, including two silicas (MSNS and MCM-41) and three carbon supports (GAC, BDH and Norit). It was observed that mesoporous nanoparticles are better candidates as supports for the β-glucosidase, and that silica has a better performance, probably due to the presence of silanol groups. The MSNS showed better recovered activity compared to other supports, showing an optimum temperature at 70 0 C and an optimum pH of 5. The enzyme immobilized in MSNS showed results 80% to 98% better than those immobilized on other supports. However, for the recycling test, from the second cycle onwards, the MSNS showed a performance drop of around 40%, reaching a relative activity of 41.9% for both the fourth and the final cycle. MCM-41, on the other hand, did not show as much discrepancy in the recycling test. However, its relative activity in the first cycle was 20% of the activity achieved by MSNS, at its optimum temperature of 60 0 C. Such results indicate that the smaller particle size favours enzymatic activity. Notwithstanding, a larger available intra-pore surface area protects the enzyme from denaturation.