In this study, we immobilized pectinase preparation on porous zeolite ZSM-5 as an enzyme carrier. We realized this immobilized enzyme catalyst, pectinase preparation@ZSM-5, via a simple combined strategy involving the van der Waals adsorption of pectinase preparation followed by crosslinking of the adsorbed pectinase preparation with glutaraldehyde over ZSM-5. Conformal pectinase preparation coverage of various ZSM-5 supports was achieved for the as-prepared pectinase preparation@ZSM-5. The porous pectinase preparation@ZSM-5 catalyst exhibited ultra-efficient biocatalytic activity for hydrolyzing the beta-glycosidic bonds in the model substrate 4-nitrophenyl beta-D-glucopyranoside, with a broad operating temperature range, high thermal stability, and excellent reusability. The relative activity of pectinase preparation@ZSM-5 at a high temperature (70 degrees C) was nine times higher than that of free pectinase preparation. Using thermal inactivation kinetic analysis based on the Arrhenius law, pectinase preparation@ZSM-5 showed higher activation energy for denaturation (315 kJ mol(-1)) and a longer half-life (62 min(-1)) than free pectinase preparation. Moreover, a Michaelis-Menten enzyme kinetic analysis indicated a higher maximal reaction velocity for pectinase preparation@ZSM-5 (0.22 mu mol mg(-1) min(-1)). This enhanced reactivity was attributed to the microstructure of the immobilized pectinase preparation@ZSM-5, which offered a heterogeneous reaction system that decreased the substrate-pectinase preparation binding affinity and modulated the kinetic characteristics of the enzyme. Additionally, pectinase preparation@ZSM-5 showed the best ethanol tolerance among all the reported pectinase preparation-immobilized catalysts, and an activity 247% higher than that of free pectinase preparation at a 10% (v/v) ethanol concentration was measured. Furthermore, pectinase preparation@ZSM-5 exhibited potential for practical engineering applications, promoting the hydrolysis of beta-glycosidic bonds in baicalin to convert it into baicalein. This was achieved with a 98% conversion rate, i.e., 320% higher than that of the free enzyme.