Protein adsorption on dental zirconia (ZrO) surfaces plays a crucial role in plaque formation, tissue healing, and bone osseointegration. This study investigated and compared the adsorption behavior of three salivary antimicrobial proteins-peroxidase, lactoferrin, and lysozyme-on a ZrO sensor and an Au sensor using a quartz crystal microbalance (QCM) operating at 27 MHz. Protein adsorption was determined from frequency decreases, and the apparent reaction rate constant () was calculated by fitting frequency-time curves to a kinetic model. The amount of lactoferrin adsorbed on the ZrO sensor was significantly higher than that of peroxidase and lysozyme ( < 0.05). Significantly smaller amounts of peroxidase and lysozyme were adsorbed onto the ZrO sensor than the Au sensor ( < 0.05). The for lysozyme on the Au sensor was significantly higher than those for lactoferrin on sensors and for peroxidase on the Au sensor ( < 0.05). Differences in salivary antimicrobial protein adsorption between Au and ZrO surfaces were influenced, in part, by electrostatic interactions between the proteins and the material surface.