This work presents the functionalization of ceramic membranes with novel modifiers to enhance the immobilization efficiency and catalytic performance of Candida antarctica lipase B (CALB).Three newly synthesized urea-based silane modifiers - Si-C3H6-U-CH2CH3, Si-C3H6-U-CH2NH2, and Si-C3H6-U-NHCH3, were grafted onto Al2O3 powders and ZrO2 planar ceramic membranes and compared with a com. alkylsilane (Si-C8H17).Comprehensive physicochem. characterization confirmed successful grafting with high efficiency (up to 98 %), tunable surface hydrophobicity, and nanometric control over grafted layer thickness (1.11-1.44 nm).Enzyme immobilization was performed via phys. adsorption, and performance was evaluated using a model enantioselective transesterification of (R,S)-1-phenylethanol.Among the tested surfaces, Si-C3H6-U-CH2CH3 demonstrated the highest lipase loading (0.41 mg) and superior catalytic activity (initial conversion rate: 104 μmol h-1), significantly outperforming the com. modifier (Si-C8H17).Enhanced activity correlated with increased surface hydrophobicity, facilitating the lipase′s open conformation and active site accessibility.The membranes also displayed distinct zeta potential profiles and adhesion characteristics, indicating that terminal functional groups play a crucial role in enzyme affinity and surface interaction.Reusability studies revealed that the Si-C3H6-U-CH2CH3-functionalized membranes retained 81 % of their initial activity after two cycles, though activity declined to 31 % after five cycles - likely owing to enzyme desorption from the membrane surface.These findings highlight the interplay between surface chem., enzyme interaction, and catalytic performance, offering a pathway for tailoring membrane supports for biocatalytic applications.This work provides a valuable insight into designing next-generation enzyme-functionalized membranes for sustainable chem. processes, bioconversion, and pharmaceutical synthesis, where high efficiency, stability, and reusability are paramount.