Enzyme adsorption-induced activity changes: a quantitative study on TiO(2) model agglomerates

BACKGROUND: Activity retention upon enzyme adsorption on inorganic nanostructures depends on different system parameters such as structure and composition of the support, composition of the medium as well as enzyme loading. Qualitative and quantitative characterization work, which aims at an elucidation of the microscopic details governing enzymatic activity, requires well-defined model systems. RESULTS: Vapor phase-grown and thermally processed anatase TiO(2) nanoparticle powders were transformed into aqueous particle dispersions and characterized by dynamic light scattering and laser Doppler electrophoresis. Addition of β-galactosidase (β-gal) to these dispersions leads to complete enzyme adsorption and the generation of β-gal/TiO(2) heteroaggregates. For low enzyme loadings (~4% of the theoretical monolayer coverage) we observed a dramatic activity loss in enzymatic activity by a factor of 60–100 in comparison to that of the free enzyme in solution. Parallel ATR-IR-spectroscopic characterization of β-gal/TiO(2) heteroaggregates reveals an adsorption-induced decrease of the β-sheet content and the formation of random structures leading to the deterioration of the active site. CONCLUSIONS: The study underlines that robust qualitative and quantitative statements about enzyme adsorption and activity retention require the use of model systems such as anatase TiO(2) nanoparticle agglomerates featuring well-defined structural and compositional properties. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12951-017-0283-4) contains supplementary material, which is available to authorized users.