In this work, we study the interaction of new aluminum oxide nanoparticles produced by the acoustoplasma method with and without cavitation with blood plasma enzyme - thrombin. Using dynamic and static light scattering, we find that the interaction of thrombin with two types of nanoparticles leads to different ways of aggregation. In the case of interaction of thrombin with nanoparticles with cavitation, formed aggregates precipitate during several hours after mixing. In the case of the nanoparticles without cavitation, in the opposite, the stable aggregates are formed with a mean size of 700 nm. The total intensity of scattered light in the solution of thrombin with nanoparticles without cavitation increases 40 times one day after mixing with the maintaining of sizes. According to Rayleigh-Gans-Debye approximation, such an increase of the total intensity of scattered light may be caused by changing of either radius of particles or their concentrations, or refractive index of formed aggregates. Due to radius of particles formed remains unchanged, and to increase the concentration by 2 orders in magnitude, it is necessary the material intake (which is absent in the closed cuvette). Therefore, it is the refractive index of formed aggregates that change (Δn=0.3). Moreover, after the addition of thrombin-nanoparticle complexes to fibrinogen solution, the reaction of fibrin gel formation switched off. It testifies inactivation of thrombin under interaction with aluminum oxide nanoparticles (in opposite to the results obtained under the interaction of iron oxide nanoparticles).