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Sensors 2003, 3(6), 166-175;

A New Laccase Biosensor For Polyphenols Determination

CECUL -Faculdade de Ciências da Universidade de Lisboa, Campo Grande, C 8 1749-016 Lisboa, Portugal
Author to whom correspondence should be addressed.
Received: 1 April 2003 / Accepted: 5 May 2003 / Published: 29 June 2003
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The relevance of polyphenols in human health is a well known fact. Prompted by that, a very intensive research has been directed to get a method to detect them, wich will improve the current ones. Laccase (p-diphenol:dioxygen oxidoreductase EC is a multi-copper oxidase, wich couples catalytic oxidation of phenolic substrates with four electron reduction of dioxygen to water [1]. A maximum catalytic response in oxigenated electrolyte was observed between 4.5 and 5.5 [2], while for pH > 6.9 the laccase was found to be inactive [3]. We prepared a biosensor with laccase immobilised on a polyether sulphone membrane, at pH 4.5, wich was applied at Universal Sensors base electrode. Reduction of the product of oxidation of several polyphenols, catalysed by laccase, was done at a potential for wich the polyphenol of interest was found to respond. Reduction of catechol was found to occur at a potential of -200mV, wich is often referred to in the literature for polyphenolic biosensors. However other polyphenols did not respond at that potential. It was observed that (+)- catechin produced a very large cathodic current when +100mV were applied to the laccase biosensor, both in aqueous acetate and 12% ethanol acetate buffer, whereas caffeic acid responded at -50mV. Other polyphenols tested were gallic acid, malvidin, quercetin, rutin, trans-resveratrol View Full-Text
Keywords: Biosensor; Laccase; Polyphenol; (+)- catechin; Caffeic acid Biosensor; Laccase; Polyphenol; (+)- catechin; Caffeic acid

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Gomes, S.A.; Rebelo, M.J. A New Laccase Biosensor For Polyphenols Determination. Sensors 2003, 3, 166-175.

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