The use of nanoparticles in food or pharma requires a molecular-level perceptive of how NPs interact with protein corona once exposed to a physiological environment. In this study, the conformational changes of bovine serum albumin (BSA) were investigated in detail when exposed to different concentration of titanium dioxide nanoparticle by various techniques. To analyze the effects of NPs on proteins, the interaction between bovine serum albumin and titanium dioxide nanoparticles at different concentrations were investigated. The interaction, BSA conformations, kinetics, and adsorption were analyzed by dynamic light scattering, Fourier transform infrared spectroscopy and fluorescence quenching. Dynamic light scattering analysis confirms the interaction with major changes in the size of the protein. Fluorescence quenching analysis confirms the side-on or end-on interaction of 1.1 molecules of serum albumin to titanium dioxide nanoparticles. Further, pseudo-second order kinetics was determined with equilibrium contact time of 20 min. The spectroscopic analysis suggests that there is a conformational change both at secondary and tertiary structure levels. A distortion in both α-helix and β-sheets was observed by Fourier transform infrared (FTIR) spectroscopy. Fluorescence quenching analysis confirms the interaction of a molecule of bovine serum albumin to the single TiO2 nanoparticle. Further, pseudo-second order kinetics was determined with equilibrium contact time of 20 min. The data of the present study determines the detailed evaluation of BSA adsorption on TiO2 nanoparticle along with mechanism and adsorption kinetics. © 2016 Elsevier B.V.