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Hydration and confinement effects on horse heart myoglobin adsorption in mesoporous $TiO_{2}$
Tijdschriftbijdrage - Tijdschriftartikel
Despite the intensive research on protein adsorption in mesoporous materials, the effect of (de)hydration and confinement on the adsorbed proteins stability and activity is poorly understood. In this paper, we study the effect of differences in structural features (pore size) and drying time on the adsorption and structural stability of horse heart myoglobin (hhMb) on mesoporous titanium dioxide. Infrared spectroscopy (DRIFT) and thermal analysis (TGA) coupled to a quadrupole mass spectrometer (TGAMS) were used to evaluate the impact of the confinement in different pores and hydration on the myoglobin secondary structure. Electron paramagnetic spectroscopy (EPR) was applied to identify the changes in the heme and its close surrounding. The peroxidase-like activity of myoglobin toward 2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) in the presence of hydrogen peroxide allowed us to detect changes in the protein activity after adsorption in pores with different sizes and drying for different periods of time. The results show a clear effect of the pore size and drying time on the secondary structure of hhMb, which is confirmed by differences induced in the catalytic activity of the adsorbed proteins. Therefore, we recommend evaluating the effect of both hydration and confinement in future applications involving biomolecule adsorption in porous matrices.
Tijdschrift: The journal of physical chemistry: C : nanomaterials and interfaces
ISSN: 1932-7447
Volume: 122
Pagina's: 23393 - 23404
Jaar van publicatie:2018
Trefwoorden:A1 Journal article
BOF-keylabel:ja
BOF-publication weight:3
CSS-citation score:1
Authors from:Higher Education
Toegankelijkheid:Open