Quinoprotein glucose dehydrogenase modified carbon paste electrode for the detection of phenolic compounds

Wollenberger, Ulla; Neumann, Bettina

doi:10.1002/elan.1140090503

Cited by 31 publications

(26 citation statements)

References 36 publications

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“…Glassy carbon electrodes, which were modified by glucose oxidase [4], glucose dehydrogenase [7,17] or laccase [17] have shown good sensitivity in the relevant range with lower detection limits between 1 and 20 nmol/L. Alternatively, a carbon paste electrode incorporating glucose dehydrogenase was developed with similar sensing characteristics [18]. However, a problem is still the reproducible fabrication of such sensors and the relatively slow response rate.…”

Section: Introductionmentioning

confidence: 98%

Recycling Systems Based on Screen-Printed Electrodes

Lisdat

Wollenberger

et al. 1998

Electroanalysis

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Screen-printed enzyme electrodes sensitive to catecholamines were developed. The bioelectrocatalytic recycling systems investigated exploited the combination of laccase catalyzed catecholamine oxidation with the electrochemical reduction of the formed quinoic product or, alternatively, electrochemical oxidation of the catecholamine followed by quinoprotein glucose dehydrogenase (GDH) catalyzed reduction. Both systems allowed quantitation of nanomolar concentrations. The lower detection limit for dopamine was 50 nmol/L and 2 nmol/L for the laccase or GDH based system, respectively. The conditions for attaining the highest sensitivity were optimized. Relatively large oxygen fluctuations in solution can be tolerated without disturbing sensor performance. Good long-term stability can be provided for sensor operation and storage.

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Section: Introductionmentioning

confidence: 98%

Recycling Systems Based on Screen-Printed Electrodes

Lisdat

Wollenberger

et al. 1998

Electroanalysis

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“…Furthermore, covalent immobilization could make the redox cycle of the substrate to take place on the surface very closely and minimize the diffusional resistance of the substrate. Comparatively, response times of some reported sensors for HQ are 5s, 90s and 7.5 min for laccase, 19 GDH 21 and GOD 22 immobilized sensor, respectively.…”

Section: Resultsmentioning

confidence: 95%

“…22 The long-term stability of the sensor is 60 days for HQ with retaining 80% of initial activity. Wasa et al reported that T. versicolor laccase immobilized Epoxy-RVC sensor retained about 65% of initial activities after repetitive use for 2 months, 19 Wollenberger et al reported that response of GDH modified carbon paste electrode dropped by 50% after 10 days 21 and Lindgren et al reported that half the response remained after storage in 4 o C for 1 week for CDH sensor. 23 The very fast response and the durable long-term stability are the principal advantages of the laccase covalently immobilized sensor.…”

Section: Resultsmentioning

confidence: 99%

“…for biosensor method, although the instrumental analysis is accurate, specific and sensitive it often requires delicate and timeconsuming sample pretreatment prior to the analysis and requires utilization of heavy equipment, therefore, they are inappropriate for massive screening. 12,18 In reported biosensor methods, for detection of HQ enzymes such as laccase (T. versicolor), 19,20 glucose dehydrogenase (GDH, A. calcoaceticus), 21 glucose oxidase (GOD, Aspergillus) 22 and cellobiose dehydrogenase (CDH, P. chrysosporium), 23 etc. were used, and for detection of HGA enzymes such as laccase (T. versicolor), 19 homogentisate dioxygenase (A. nidulans), 12 etc.…”

Section: Introductionmentioning

confidence: 99%

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Amperometric Detection of Hydroquinone and Homogentisic Acid with Laccase Immobilized Platinum Electrode

Quan¹,

Shin²

2004

Bulletin of the Korean Chemical Society

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DeniLiteTM laccase immobilized platinum electrode was used for amperometric detection of hydroquinone (HQ) and homogentisic acid (HGA) by means of substrate recycling. In case of HQ, the obtained sensitivity is 280 nA/µM with linear range of 0.2-35 µM (r 2 = 0.998) and detection limit (S/N = 3) of 50 nM. This high sensitivity can be attributed to chemical amplification due to the cycling of the substrate caused by enzymatic oxidation and following electrochemical regeneration. In case of HGA, the obtained sensitivity is 53 nA/µM with linear range of 1-50 µM (r 2 = 0.999) and detection limit of 0.3 µM. The response times (t 90% ) are about 2 seconds for the two substrates and the long-term stability is 60 days for HQ and around 40-50 days for HGA with retaining 80% of initial activities. The very fast response and the durable long-term stability are the principal advantages of this sensor. pH studies show that optimal pH of the sensor for HQ is 6.0 and that for HGA is 4.5-5.0. This shift of optimal pH towards acidic range for HGA can be attributed to the balance between enzyme activity and accessibility of the substrate to the active site of the enzyme.

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“…It is known that quinoprotein ADHs can be used for biotechnological applications, e.g., as biosensors or for the stereoselective oxidation of chiral alcohols (14,17,28,39,51). The broad substrate spectrum makes them useful for the production of different pure enantiomers (44).…”

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Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

2001

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The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparent k cat /K m and K i values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k cat /K m value of 788 ؋ 10 4 M ؊1 s ؊1 . The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo (tfaA) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases.

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Quinoprotein glucose dehydrogenase modified carbon paste electrode for the detection of phenolic compounds

Cited by 31 publications

References 36 publications

Recycling Systems Based on Screen-Printed Electrodes

Recycling Systems Based on Screen-Printed Electrodes

Amperometric Detection of Hydroquinone and Homogentisic Acid with Laccase Immobilized Platinum Electrode

Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

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