Simultaneous use of dehydrogenases and hexacyanoferrate(III) ion in electrochemical biosensors for l-lactate, d-lactate and l-glutamate ions

Montagné, Marielle; Durliat, H.; Comtat, Maurice

doi:10.1016/0003-2670(93)80081-u

Cited by 43 publications

(21 citation statements)

References 29 publications

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“…14 A number of sensor types have been developed for the measurement of Glu based on a variety of metabolic enzymes. [15][16][17][18][19][20] Attention has focused mainly on the use of l-glutamate oxidase (GluOx) that has FAD as the redox centre and molecular oxygen as a co-substrate, 21 producing hydrogen peroxide that can be detected amperometrically 19,20,[22][23][24][25][26][27][28][29][30] or spectroscopically. 31,32 The oxidative deamination catalysed by GluOx 21 can be represented by the following steps: l-Glutamate + H 2 O + GluOx/FAD ?…”

mentioning

confidence: 99%

Biosensor for Neurotransmitter L-Glutamic Acid Designed for Efficient Use of L-Glutamate Oxidase and Effective Rejection of Interference

Ryan

Lowry²,

O’Neill³

1997

Analyst

124

179

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An amperometric biosensor for l-glutamic acid (Glu) was constructed by the adsorption and dip coating of l-glutamate oxidase (GluOx, 200 U ml 21 phosphate buffer, pH 7.4) onto 60-mm radius Teflon-coated Pt wire (1 mm exposed length). The enzyme was then trapped on the surface by electropolymerisation of o-phenylenediamine that also served to block electroactive interference. This procedure afforded electrodes with similar substrate sensitivity compared with the classical approach of immobilising enzyme from a solution of monomer, and represents an approximately 10 000-fold increase in the yield of biosensors from a batch of enzyme. A number of strategies were examined to enhance the sensitivity and selectivity of the Pt/PPD/GluOx sensors operating at 0.7 V versus SCE. Pre-coating the Pt with lipid and incorporation of the protein bovine serum albumin into the polymer matrix were found to improve the performance of the electrode. The sensors had a fast response time, high sensitivity to Glu, with an LOD of about 0.3 mmol l 21 , and possessed selectivity characteristics suggesting that monitoring Glu in biological tissues in vivo may be feasible.

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mentioning

confidence: 99%

Biosensor for Neurotransmitter L-Glutamic Acid Designed for Efficient Use of L-Glutamate Oxidase and Effective Rejection of Interference

Ryan

Lowry²,

O’Neill³

1997

Analyst

124

179

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“…However, these immobilized mediators could also enable efficient electrocatalytic oxidation of interferents present in biological fluids. One way to overcome this problem is the use of electroenzymatic systems based on immobilized enzymes coupled to freely diffusing mediators such as flavins [8], ferrocene derivatives [9,10] or ferricyanide [11,12]. However, these systems are not compatible with in vivo measurements.…”

Section: Introductionmentioning

confidence: 97%

A Reagentless Biosensor for the Amperometric Determination of NADH

Cosnier¹,

Décout²,

Fontecave³

et al. 1998

Electroanalysis

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A flavin analog (1) in which the isoalloxazine ring of riboflavin is linked to a pyrrole group has been synthesized and electrochemically characterized. The enzyme flavin reductase (Fre) was successfully immobilized by copolymerization of compound 1 and the amphiphilic pyrrole ammonium derivative 2. The amperometric response of the resulting poly(1-2)-Fre electrode to NADH was based on the oxidation of the enzymically reduced flavin analog 1 at ¹0.1 V (vs. SCE). The sensitivity and detection limit of the biosensor for NADH are 13.7 mA M ¹1 cm ¹2 and 0.5 mM, respectively. The new biosensor is NADH-specific since no amperometric response was observed for repeated additions of NADPH.

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“…Alternative approaches to glutamate monitoring involve, e.g., the use of capillary biosensors combined with¯uoroscence-based detection [14], dialysis electrodes utilizing an integrated unit of dialysis sampling and electrochemical detection [25,26], enzyme reactors combined with amperometric detection [16, 27±29], thinlayer spectroelectrochemistry [30], chemiluminescence [31,32],¯u orometric detection [33], or capillary electrophoresis with laser induced¯uorescence [34]. All these methods, however, require sophisticated and expensive instruments, often a HPLC separation step, and quali®ed personnel.…”

Section: Introductionmentioning

confidence: 99%

Interference Elimination in Glutamate Monitoring with Chip Integrated Enzyme Microreactors

et al. 2001

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Simultaneous use of dehydrogenases and hexacyanoferrate(III) ion in electrochemical biosensors for l-lactate, d-lactate and l-glutamate ions

Cited by 43 publications

References 29 publications

Biosensor for Neurotransmitter L-Glutamic Acid Designed for Efficient Use of L-Glutamate Oxidase and Effective Rejection of Interference

Biosensor for Neurotransmitter L-Glutamic Acid Designed for Efficient Use of L-Glutamate Oxidase and Effective Rejection of Interference

A Reagentless Biosensor for the Amperometric Determination of NADH

Interference Elimination in Glutamate Monitoring with Chip Integrated Enzyme Microreactors

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