Titanium dioxide photocatalyzed oxidation of proteins in biocontaminated waters.
The TiO2 photocatalyzed oxidation of the proteins serum albumin, ovalbumin and gamma globulin, is reported. All the amino acids were susceptible to photocatalytic oxidation. However, some were especially vulnerable. Tyrosine was particularly sensitive, as was the semiaromatic histidine, although to a lesser extent. The lack of an activating group on the aromatic ring in Phe, renders the system less amenable to degradation. The photocatalytic degradation of the aliphatic amino acids Gly and Asp, was particularly slow, like in the Fenton oxidation where production of glycine was observed during the cleavage of collagen induced by hydroxyl radicals. Intermediate degradation rate was noticed in Ser, Arg, Val, Cys and Phe.
Muszkat
L
L
Department of Chemical Agroecology, Institute of Plant Protection, ARO, Volcani Center, Bet-Dagan, Israel. alex.muszkat@weizmann.ac.il
Feigelson
L
L
Bir
L
L
Muszkat
K A
KA
D000596:Amino Acids / Q000378:metabolism; D002384:Catalysis; D007700:Kinetics; D010047:Ovalbumin / Q000378:metabolism*; D010084:Oxidation-Reduction; D017319:Photosensitizing Agents / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D014025:Titanium / Q000378:metabolism*; D014874:Water Pollutants, Chemical / Q000378:metabolism*; D005719:gamma-Globulins / Q000378:metabolism*
D000596:Amino Acids; D017319:Photosensitizing Agents; D014874:Water Pollutants, Chemical; D005719:gamma-Globulins; C009495:titanium dioxide; D012710:Serum Albumin, Bovine; D010047:Ovalbumin; D014025:Titanium