Introduction. Recent studies show the possibility of using iron oxide nanoparticles as a food additive with certain functional and technological properties. However, when developing technologies for food products, the interaction of these particles with the main components of the food matrix, in particular, proteins, takes on special significance. The aim of the present research was to study the interaction of iron oxide nanoparticles with ovalbumin molecules.

Methods. Fourier-transform infrared and fluorescence spectroscopy were used to study interaction between iron oxide nanoparticles and ovalbumin molecules.

Results: It was found that the interaction of Iron oxide nanoparticles with ovalbumin molecules was going by the mechanism of static quenching with the formation of an intermolecular non-fluorescent complex that changes the native structure of the protein. The binding constant varied from 3.3•10⁵ to 4.8•10⁵ l mol^-1 depending on the pH value of the medium and temperature. The calculated thermodynamic parameters of binding indicate the spontaneity of the process with the predominance of the enthalpy factor. The interaction between iron nanoparticles and ovalbumin occurred mainly due to hydrogen bonds and van der Waals forces.

Conclusion: The obtained data on the mechanism of interaction of iron oxide nanoparticles with proteins should be taken into account when developing food technologies to control functional properties of products.