The goal of this work was the characterization, step by step, of the enzyme glucose oxidase (GOx) immobilization on silicon oxide surfaces, mainly by means of X-Ray photoelectron spectroscopy (XPS). The immobilization protocol consists of four steps: oxide activation, silanization, linker molecule deposition and GOx immobilization. The linker molecule, glutaraldehyde (GA) in this study, must be able to form a uniform layer on the sample surface in order to maximize the sites available for enzyme bonding and achieve the best enzyme deposition. Using a thin SiO2 layer grown on Si wafers and following the XPS Si2p signal of the Si substrate during the immobilization steps, we demonstrated both the glutaraldehyde layer uniformity and the possibility to use XPS to monitor thin layer uniformity. In fact, the XPS substrate signal, not shielded by the oxide, is suppressed only when a uniform layer is deposited. The …