Keratin Protein Modified Anatase TiO2 Nanoparticle Characterizations of Protein Functionalized Surface
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Abstract
Anatase titanium dioxide (TiO2) nanoparticle surface is modified with Keratin, a protein from swine wool. The protein structure and the modified surface of the TiO2 nanoparticle is investigated. The structure and bonding of the adsorbed protein on TiO2 surface were investigated by Fourier-transform infrared spectroscopy (FT-IR). The surface morphology of hybrid nanocomposite was observed by Field Emission Scanning Electron Microscopy (FESEM). Chemical bonding between protein and titanium dioxide was further investigated by X-ray Photoelectron Spectroscopy (XPS). Electrochemical cyclic voltammetry (CV) was used to characterize the electrochemical behaviour the protein modified TiO2. The protein structure conformation and chemical bonding interaction with TiO2 surface critically depend on the protein concentration. The protein is likely adsorbed via the interactions between the methyl, carbonyl, and amines group on the side chains of random coil secondary structure with the anatase TiO2 surface. The protein has strong bonding to TiO2 surface as evidently observed XPS for an environment bonding change in binding energy and component at O1s Ti2p and N1s region. The electrochemical behaviour of keratin protein modulated anatase TiO2 hybrid material shows significant influence by protein structure and/or protein concentration at the surface.
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