Applications of "Wired" Peroxidase Electrodes for Peroxide Determination in Liquid Chromatography Coupled to Oxidase Immobilized Enzyme Reactors

Yang, Lixue; Janle, Elsa M.; Huang, Tian-Sen; Gitzen, James F.; Kissinger, Peter T.; Vreeke, Mark; Heller, Adam

doi:10.1021/ac00104a005

Cited by 99 publications

(52 citation statements)

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“…60 The detection limit of 1.7 mUnit GOx/mL was adequate for testing GOx expressed in S. cerevisiae culture without sample pretreatment. Controls for glucose oxidase activity assay were preformed using commercially available glucose oxidase (Biozyme; South Wales, UK).…”

Section: Electrochemical Assaymentioning

confidence: 94%

Bio micro fuel cell grand challenge final report.

Fujimoto¹,

Cornelius²,

Doughty³

et al. 2005

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Executive SummaryThis LDRD was conceived to develop a power system that could harvest the energy from carbohydrate fuels that are readily available and can be harvested from biological sources. This included the possibilities of generating power from harvested tree sap, sugars, and even mammalian blood. Since the biological host continues to produce and/or replace these fuels as part its normal biological processes, this approach enables a very long lived, power microsystem. Fuel cells were identified as the energy conversion systems most likely to take advantage of the opportunities of a continuous fuel supply, and therefore the project started from an existing foundation in traditional fuel cell operations.Six basic subtasks were identified for this project; harvesting, membrane separation, catalysis, architecture, enzymology, and power management. Harvesting targeted both harvesting from a tree using a simple spile arrangement, and harvesting through the skin of mammalian hosts using a microneedle patch. Membrane separation provided a physical separator between the anode oxidation of the fuel and the cathodic reduction of oxygen. The catalysis team targeted both the development of new, poison resistant, highly active noble metal catalysts that could readily oxidize the carbohydrate fuel without poisoning the catalysts, and also worked to develop mediator molecules to transport oxidized electrons from enzyme catalysts to anode electrode surfaces. The enzymology team developed protocols for the genetic engineering of enzymes capable of oxidizing the carbohydrates, and also looked into the requirements to immobilize these enzymes against an electrode, together with the catalysis team. The architecture team was tasked with developing a small architecture that could take in these other components and assemble them into working fuel cells running on glucose (a simple carbohydrate) and oxygen. The power management task, added after the initial program was started, focused on handling the variation in the power output from the fuel cells and in turn producing stable, electronic grade power to supply to an external circuit.At the end of the project, the best power generated from a single, 15mm x 21mm x 1mm fuel cell was about 7 mW/cm 2 running on 1 molar (M) glucose in water and oxygen at room temperature. This was achieved using a noble metal catalyst. The best enzymatic fuel cell using an anode based on glucose oxidase was able to demonstrate 5 250μW/cm 2 of power from a 50 millimolar glucose solution. In both cases, however, the lifetime was limited to a few minutes . In the noble metal case, oxidation byproducts quickly poison the catalysts. However, a system solution for in situ cleaning of the anode with little power penalty eventually extending the lifetime to about 700 hours (nearly one month) while producing about 2 mW/cm 2 . In the enzymatic case, the lifetime was limited to minutes of operation by the loss of enzyme and mediator to the flowing fuel.Significant progress was made in stabilizing the enzyme, bu...

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Section: Electrochemical Assaymentioning

confidence: 94%

Bio micro fuel cell grand challenge final report.

Fujimoto¹,

Cornelius²,

Doughty³

et al. 2005

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“…Os-polyvinylpyridine containing horseradish peroxidase (Os-gel-HRP) was obtained from Bioanalytical Systems Inc. (West Lafayette, IN). 37,38 Glutamate oxidase (GluOx) from streptomyces sp. X-119-6 was obtained from Yamasa Shoyu (Choshi, Japan).…”

Section: Chemicals and Materialsmentioning

confidence: 99%

Microfabricated On-Line Sensor for Continuous Monitoring of l-Glutamate

Niwa

Horiuchi

Kurita³

et al. 1998

ANAL. SCI.

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Various methods have been developed for measuring the in vivo and in vitro concentrations of L-glutamate, since glutamate plays an important role in synaptic efficacy, including the long-term potentiation (LTP) 1,2 and long-term depression (LTD) 3,4 of excitatory neurotransmission. It is also reported to be a factor in several diseases including ischemia and nerve cell death.5,6 A number of methods have already been proposed for measuring L-glutamate, including chromatographic technique 7 and capillary electrophoresis. 8,9 However, these methods require time for derivatization and column separation.Recently, many groups have been focusing on the development of amperometric enzyme sensors using glutamate dehydrogenase and glutamate oxidase. The latter enzyme has more often been used to fabricate glutamate sensors because a glutamate dehydrogenase sensor requires the addition of NAD + . 10-12 Therefore, glutamate oxidase has been more often used to fabricate electrochemical sensors for detecting the neurotransmitter, L-glutamate. [13][14][15][16][17][18][19][20][21][22][23][24] Carbon fiber or metal wire microelectrodes modified with glutamate oxidase have been employed for measuring L-glutamate in the brain and in cultured rat brain tissue. [13][14][15][16] It has been reported that L-glutamate increases as the result of KCl and electrical stimulations. The advantages of the enzyme-modifed electrodes are their fast response and their ability to measure a small localized area.By contrast, on-line L-glutamate sensors have been developed. These consist of a syringe pump, a microdialysis (MD) sampling probe, an enzymatic reactor and an electrode in a flow cell. [17][18][19][20][21][22] On-line sensors are particularly useful for measuring in vivo L-glutamate, since they are very stable. This is because the flow measurement is very reproducibile and the MD membrane eliminates high molecular weight interferents such as proteins. The reported detection limits of online L-glutamate sensors are from 10 nM to 0.5 µM, which are lower than those of microelectrode-based sensors. However, the on-line sensor response is slower than that of the microelectrode sensors and it has a large sampling probe (usually 1 -3 mm long and a few hundred µm in diameter). There have been a few reports on the use of on-line sensors for measuring cultured nerve cells. However, their slow response and large sampling probe size limits their spatial and temporal resolutions in spite of their high sensitivity and long term stability. 21,22 We reported an on-line L-glutamate sensor for measuring dissociated nerve cell cultures. 23 The sensor consists of a glass capillary for sampling combined with an electrochemical thin layer flow cell. Since the sampling probe is much smaller than the MD probe, we can achieve better spatial resolution. We observed the transient release of L-glutamate by stimulating the inhibitory neurotransmitter, γ-aminobutyric acid (GABA), using this sensor. 24 However, the relatively large volume of the sensor means that there ...

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“…Glucose oxidase, lactate oxidase, and acetylcholine esterase/choline oxidase IMERs were used in these systems for their respective substrates. Details of the performance of the peroxidase electrode in these LC-IMER systems have been discussed elsewhere [8]. Although the peroxidase detector-oxidase IMER approach is not as simple as the direct determination of oxidase substrates with oxidase modified amperometric detectors, it has the potential advantage loading a much greater active catalyst in a rugged format.…”

Section: Application Of Peroxidase Electrode In Lc Systems With Post-mentioning

confidence: 99%

“…There have been many publications on the development of oxidase modified amperometric flow cells for flow injection analysis. Relatively fewer such developments, however, have been incorporated in detectors for LC [8][9] or microdialysis [4-71, which are of great practical importance.…”

Section: Introductionmentioning

confidence: 99%

Determination of oxidase enzyme substrates using cross‐flow thin‐layer amperometry

Yang

Kissinger

1996

Electroanalysis

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Thin-layer cross-flow amperometric dete:ctors with enzyme modified working electrodes were developed for the determination of oxidase substrates in flowing streams. The enzymse was covalently immobilized in an osmium redox polymer film on the electrode surface. Electrodes modified with glucose oxidase or lactate oxidase were prepared for the continuous monitoring of glucose or lactate. A peroxidase electrode coupled with oxidase enzyme reactors w,as also explored for the determination of glucose, lactate, and acetylcholine/choline in continuous monitoring systems or following liquid chromatography. The effects of interferences, oxygen, mass transfer limiting membrane, and perfusate composition on electrode performance are discussed.

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Applications of "Wired" Peroxidase Electrodes for Peroxide Determination in Liquid Chromatography Coupled to Oxidase Immobilized Enzyme Reactors

Cited by 99 publications

References 0 publications

Bio micro fuel cell grand challenge final report.

Bio micro fuel cell grand challenge final report.

Microfabricated On-Line Sensor for Continuous Monitoring of l-Glutamate

Determination of oxidase enzyme substrates using cross‐flow thin‐layer amperometry

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