Glucose oxidase catalyses the reduction of O2 to H2O2 in the presence of irradiated TiO2 and isopropyl alcohol.
Catalytic amounts of glucose oxidase from Aspergillus niger (GO) are active in the reduction of O2 to H2O2 in the presence of irradiated suspensions of TiO2 and isopropyl alcohol as electron donor. An explanation of this behaviour is given on the basis of the ability of the enzyme to capture electrons from the photoexcited TiO2 instead of its natural substrate, glucose. This process has a marked positive effect on both the oxidation of isopropyl alcohol to acetone and the formation of radical intermediates, which have been detected, for the first time, by EPR-spin trapping investigation.
Ganadu
Maria L
ML
Dipartimento di Chimica, Università di Sassari, Via Vienna 2, 07100 Sassari, Italy. billia@ssmain.uniss.it
Andreotti
Leonardo
L
Vitali
Irene
I
Maldotti
Andrea
A
Molinari
Alessandra
A
Mura
Giovanni M
GM
D019840:2-Propanol / Q000737:chemistry*; D001230:Aspergillus / Q000201:enzymology; D002384:Catalysis; D004578:Electron Spin Resonance Spectroscopy; D005949:Glucose Oxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000138:chemical synthesis*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D010777:Photochemistry / Q000379:methods*; D017319:Photosensitizing Agents / Q000737:chemistry*; D019097:Spin Trapping; D013997:Time Factors; D014025:Titanium / Q000737:chemistry*
D017319:Photosensitizing Agents; C009495:titanium dioxide; D006861:Hydrogen Peroxide; D014025:Titanium; D005949:Glucose Oxidase; D019840:2-Propanol; D010100:Oxygen