Study of catalase electrode for organic peroxides assays.
The catalytic activity of immobilized catalase (EC 1.11.1.6) for two model peroxide compounds (dibenzoyl peroxide and 3-chloroperoxibenzoic acid) in a non-aqueous medium was used to prepare an organic-phase enzyme electrode (OPEE). The enzyme was immobilized within a polymeric film on spectrographic graphite. The amperometric signal of the enzyme electrode in substrate solutions was found to be due to the reduction of oxygen generated in the enzyme layer. The electrode response is proportional to peroxide concentrations up to about 40 microM within the potential range from -450 to -650 mV (vs. Ag/AgCl), and the response time is at most 90 s. The enzyme electrode retains about 35% of its initial activity after a 3-week storage at room temperature.
Horozova
Elena
E
Department of Physical Chemistry, University of Plovdiv, 24, Tsar Assen St., Plovdiv 4000, Bulgaria. harozova@argon.acad.bg
Dimcheva
Nina
N
Jordanova
Zinaida
Z
D001585:Benzoyl Peroxide / Q000032:analysis; D015374:Biosensing Techniques / Q000379:methods*; D002374:Catalase / Q000378:metabolism*; D002723:Chlorobenzoates / Q000032:analysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D010408:Penicillium chrysogenum / Q000201:enzymology*; D010545:Peroxides / Q000032:analysis*; D013379:Substrate Specificity; D013696:Temperature
D002723:Chlorobenzoates; D004800:Enzymes, Immobilized; D010545:Peroxides; D002374:Catalase; C000433:3-chloroperbenzoic acid; D001585:Benzoyl Peroxide