LAUSR

Abstract The purpose of this work is to improve the method for immobilizing Trichoderma reesei enzyme on various supports, namely, SBA-15, TUD-1, and MCM-48, and to study its hydrolysis efficiency. Among the studied supports, SBA-15 showed 100% adsorption. This work examined the effects of temperature, pH, and amount of the support on the enzyme immobilization. The optimal conditions for cellulose hydrolysis were at pH = 3.8 and 45 °C for 3 days using 1.2 g of the enzyme immobilized on SBA-15 (IM-SBA-15), yielding about 90% sugar. Depth profiles of X-ray photoelectron and Infrared spectroscopies (XPS and IR, respectively) illustrated that the enzyme was attracted to the support surface by electrostatic force between carbonyl of the amide group and hydroxyl group of the support. Remarkably, IM-SBA-15 resulted in a much better yield of monomeric sugar (90%) in a weak-acid condition while only 65% monomeric sugar yield was obtained using the free enzyme.