Mediated amperometric determination of xylose and glucose with an immobilized aldose dehydrogenase electrode

Maria Smolander (Corresponding Author), Hanna Livio, Lea Räsänen

Research output: Contribution to journalArticleScientificpeer-review

35 Citations (Scopus)

Abstract

An enzyme electrode was constructed for amperometric determination of xylose and glucose. The electrode is based on the PQQ-dependent membrane-bound aldose dehydrogenase (ALDH) from Gluconobacter oxydans. ALDH was covalently immobilized on a graphite electrode. Immobilized dimethylferrocene, soluble ferrocene carboxylic acid and phenazine metho-sulphate were used as electron transfer mediators. When xylose was measured electrochemically using an electrode modified with ALDH and dimethyl-ferrocene, the linear measurement range extended to 100 mM. For glucose measurement the linear measurement range was about one-tenth of that for xylose. The electrode showed fairly good stability: 50% of the original electrode response was still obtained after 5 days of intermittent use. The effect of possible leakage of adsorbed mediator was determined by measuring the response of an electrode with soluble mediator as a function of time. The reproducibility of the electrode was good, the standard deviation of the electrode response in ten measurements with the same electrode being only 2.7%.

Original languageEnglish
Pages (from-to)637-643
Number of pages7
JournalBiosensors & Bioelectronics
Volume7
Issue number9
DOIs
Publication statusPublished - 1992
MoE publication typeA1 Journal article-refereed

Fingerprint

Xylose
Glucose
Oxidoreductases
Electrodes
Gluconobacter oxydans
Enzyme electrodes
Graphite electrodes
xylose-glucose
Graphite
Carboxylic acids
Biosensing Techniques
Sulfates
Membranes
Electrons

Keywords

  • biosensor
  • enzyme electrode
  • PQQ-dependent dehydrogenase
  • D-xylose
  • D-glucose

Cite this

@article{f44b48146466481e8efefa49dea8f35c,
title = "Mediated amperometric determination of xylose and glucose with an immobilized aldose dehydrogenase electrode",
abstract = "An enzyme electrode was constructed for amperometric determination of xylose and glucose. The electrode is based on the PQQ-dependent membrane-bound aldose dehydrogenase (ALDH) from Gluconobacter oxydans. ALDH was covalently immobilized on a graphite electrode. Immobilized dimethylferrocene, soluble ferrocene carboxylic acid and phenazine metho-sulphate were used as electron transfer mediators. When xylose was measured electrochemically using an electrode modified with ALDH and dimethyl-ferrocene, the linear measurement range extended to 100 mM. For glucose measurement the linear measurement range was about one-tenth of that for xylose. The electrode showed fairly good stability: 50{\%} of the original electrode response was still obtained after 5 days of intermittent use. The effect of possible leakage of adsorbed mediator was determined by measuring the response of an electrode with soluble mediator as a function of time. The reproducibility of the electrode was good, the standard deviation of the electrode response in ten measurements with the same electrode being only 2.7{\%}.",
keywords = "biosensor, enzyme electrode, PQQ-dependent dehydrogenase, D-xylose, D-glucose",
author = "Maria Smolander and Hanna Livio and Lea R{\"a}s{\"a}nen",
year = "1992",
doi = "10.1016/0956-5663(92)85021-2",
language = "English",
volume = "7",
pages = "637--643",
journal = "Biosensors & Bioelectronics",
issn = "0956-5663",
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}

Mediated amperometric determination of xylose and glucose with an immobilized aldose dehydrogenase electrode. / Smolander, Maria (Corresponding Author); Livio, Hanna; Räsänen, Lea.

In: Biosensors & Bioelectronics, Vol. 7, No. 9, 1992, p. 637-643.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Mediated amperometric determination of xylose and glucose with an immobilized aldose dehydrogenase electrode

AU - Smolander, Maria

AU - Livio, Hanna

AU - Räsänen, Lea

PY - 1992

Y1 - 1992

N2 - An enzyme electrode was constructed for amperometric determination of xylose and glucose. The electrode is based on the PQQ-dependent membrane-bound aldose dehydrogenase (ALDH) from Gluconobacter oxydans. ALDH was covalently immobilized on a graphite electrode. Immobilized dimethylferrocene, soluble ferrocene carboxylic acid and phenazine metho-sulphate were used as electron transfer mediators. When xylose was measured electrochemically using an electrode modified with ALDH and dimethyl-ferrocene, the linear measurement range extended to 100 mM. For glucose measurement the linear measurement range was about one-tenth of that for xylose. The electrode showed fairly good stability: 50% of the original electrode response was still obtained after 5 days of intermittent use. The effect of possible leakage of adsorbed mediator was determined by measuring the response of an electrode with soluble mediator as a function of time. The reproducibility of the electrode was good, the standard deviation of the electrode response in ten measurements with the same electrode being only 2.7%.

AB - An enzyme electrode was constructed for amperometric determination of xylose and glucose. The electrode is based on the PQQ-dependent membrane-bound aldose dehydrogenase (ALDH) from Gluconobacter oxydans. ALDH was covalently immobilized on a graphite electrode. Immobilized dimethylferrocene, soluble ferrocene carboxylic acid and phenazine metho-sulphate were used as electron transfer mediators. When xylose was measured electrochemically using an electrode modified with ALDH and dimethyl-ferrocene, the linear measurement range extended to 100 mM. For glucose measurement the linear measurement range was about one-tenth of that for xylose. The electrode showed fairly good stability: 50% of the original electrode response was still obtained after 5 days of intermittent use. The effect of possible leakage of adsorbed mediator was determined by measuring the response of an electrode with soluble mediator as a function of time. The reproducibility of the electrode was good, the standard deviation of the electrode response in ten measurements with the same electrode being only 2.7%.

KW - biosensor

KW - enzyme electrode

KW - PQQ-dependent dehydrogenase

KW - D-xylose

KW - D-glucose

U2 - 10.1016/0956-5663(92)85021-2

DO - 10.1016/0956-5663(92)85021-2

M3 - Article

VL - 7

SP - 637

EP - 643

JO - Biosensors & Bioelectronics

JF - Biosensors & Bioelectronics

SN - 0956-5663

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