Published Date
Biosensors and Bioelectronics
15 November 2005, Vol.21(5):742–748, doi:10.1016/j.bios.2005.01.008
Abstract
Three amperometric enzyme electrodes have been constructed by adsorbing anionic royal palm tree peroxidase (RPTP), anionic sweet potato peroxidase (SPP), or cationic horseradish peroxidase (HRP-C) on spectroscopic graphite electrodes. The resulting H2O2-sensitive biosensors were characterized both in a flow injection system and in batch mode to evaluate their main bioelectrochemical parameters, such as pH dependency, Imax, , detection limit, linear range, operational and storage stability. The obtained results showed a distinctly different behavior for the plant peroxidase electrodes, demonstrating uniquely superior characteristics of the RPTP-based sensors. The broader linear range observed for the RPTP-based biosensor is explained by a high stability of this enzyme in presence of H2O2. The higher storage and operational stability of RPTP-based biosensor as well as its capability to measure hydrogen peroxide under acidic conditions connect with an extremely high thermal and pH-stability of RPTP.
Keywords
Peroxidase
Biosensors
Palm tree
Horseradish
Sweet potato
Hydrogen peroxide
For further details log on website :
http://www.sciencedirect.com/science/article/pii/S0956566305000230
Biosensors and Bioelectronics
15 November 2005, Vol.21(5):742–748, doi:10.1016/j.bios.2005.01.008
Received 28 October 2004. Revised 11 January 2005. Accepted 12 January 2005. Available online 3 February 2005.
Abstract
Three amperometric enzyme electrodes have been constructed by adsorbing anionic royal palm tree peroxidase (RPTP), anionic sweet potato peroxidase (SPP), or cationic horseradish peroxidase (HRP-C) on spectroscopic graphite electrodes. The resulting H2O2-sensitive biosensors were characterized both in a flow injection system and in batch mode to evaluate their main bioelectrochemical parameters, such as pH dependency, Imax, , detection limit, linear range, operational and storage stability. The obtained results showed a distinctly different behavior for the plant peroxidase electrodes, demonstrating uniquely superior characteristics of the RPTP-based sensors. The broader linear range observed for the RPTP-based biosensor is explained by a high stability of this enzyme in presence of H2O2. The higher storage and operational stability of RPTP-based biosensor as well as its capability to measure hydrogen peroxide under acidic conditions connect with an extremely high thermal and pH-stability of RPTP.
Keywords
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Copyright © 2005 Elsevier B.V. All rights reserved.
For further details log on website :
http://www.sciencedirect.com/science/article/pii/S0956566305000230
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