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Titolo:
Enzyme electrode with enhanced specificity using outer polymeric membrane doped with substrate selective ditopic carrier
Autore:
Kim, JS; Pike, JD; Coucouvanis, D; Meyerhoff, ME;
Indirizzi:
Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA Univ Michigan Ann ArborMI USA 48109 , Dept Chem, Ann Arbor, MI 48109 USA Gyeongsang Natl Univ, Dept Chem, Chinju 660701, South Korea Gyeongsang Natl Univ Chinju South Korea 660701 hinju 660701, South Korea
Titolo Testata:
ELECTROANALYSIS
fascicolo: 16, volume: 12, anno: 2000,
pagine: 1258 - 1262
SICI:
1040-0397(200011)12:16<1258:EEWESU>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
SALICYLALDIMINE COMPLEXES; AMPEROMETRIC BIOSENSORS; LIQUID-MEMBRANE; TRANSPORT; GLUCOSE; BACTERIAL; TISSUE;
Keywords:
enzyme electrode; amino acid oxidase; substrate selective transport; ditopic carrier;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Meyerhoff, ME Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 nn Arbor, MI 48109 USA
Citazione:
J.S. Kim et al., "Enzyme electrode with enhanced specificity using outer polymeric membrane doped with substrate selective ditopic carrier", ELECTROANAL, 12(16), 2000, pp. 1258-1262

Abstract

A new method for enhancing the specificity of enzyme electrodes in which the immobilized enzymatic layer is a relatively nonselective biocatalyst is reported. The approach is based on the use of an outer polymeric membrane doped with a substrate selective carrier that transports the target analyte selectively into the underlying enzyme layer. As an initial model for this concept, an amperometric enzyme electrode with enhanced selectivity for tryptophan is described. The sensor is prepared by coating a layer of L-amino acid oxidase (AAO) on the surface of a platinum working electrode and then covering this layer with an outer hydrophobic plasticized polyurethane (PU)film containing the ditopic carrier, manganese(III)-4,5-di(3,5-di-t-butylsalicylideneimine)benzo-18-crown-6 tetraphenylborate (Mn(III)tBuSalph-B 18C6(BPh4). Tryptophan is transported selectively from sample solution by the carrier into the L-amino acid oxidase layer, yielding production of hydrogenperoxide that can be detected amperometrically at the platinum electrode at 650 mV (vs. Ag/AgCl reference electrode). The resulting enzyme electrode is shown to exhibit a dramatic increase in selectivity for tryptophan when compared to the amino acid response of an analogous enzyme electrode prepared with a nonselective outer dialysis membrane. Independent measurements ofthe PU-carrier membrane's substrate permselectivity using a diffusion cellcorrelate with the amperometric enzyme electrode results. The practical limitations of this approach for preparing enzyme electrodes (i.e., slower response times and reduced substrate fluxes) are discussed and potential solutions to these problems are proposed.

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Documento generato il 28/09/20 alle ore 15:18:39