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...

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Bibliographic Details
Published in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2002-12, Vol.58 (2), p.181-187
Main Authors: Horozova, Elena, Dimcheva, Nina, Jordanova, Zinaida
Format: Article
Language:English
Subjects:
Benzoyl Peroxide - analysis
Biosensing Techniques - methods
Catalase - metabolism
Chlorobenzoates - analysis
Enzymes, Immobilized - metabolism
Graphite
Immobilized catalase
Kinetics
Nafion
Organic-phase enzyme electrode
Penicillium chrysogenum - enzymology
Peroxides - analysis
Substrate Specificity
Temperature
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Summary: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 μM 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.
ISSN:1567-5394
1878-562X
DOI:10.1016/S1567-5394(02)00153-6