Solid-solid heterogeneous photooxidation of egg albumin with TiO 2 was carried out under near UV-light irradiation (λ > 370 nm) and the oxidation behavior was investigated. Egg albumin was photooxidized to form CO2 without evolution of CO and organic byproducts. The activity for TiO2-catalyzed albumin photooxidation strongly depended on the albumin and TiO2 mixing conditions, indicating that the contact conditions between TiO2 and albumin were important for complete oxidation of albumin. In-situ diffuse reflectance FTIR studies revealed that the peptide bond of albumin was decomposed with the alkyl side chains and that decomposition of the peptide bond followed pseudo first-order kinetics.
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