Glucose oxidase, lactate oxidase, and galactose oxidase enzyme electrode based on polypyrrole with polyanion/PEG/enzyme conjugate dopant

Sung, Won Jun; Bae, You Han

doi:10.1016/j.snb.2005.04.027

Cited by 58 publications

(46 citation statements)

References 32 publications

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“…) was successfully deposited (5 min) on the modified electrode and a linear relationship between current response and glutamate concentration was observed up to 100 mM (sensitivity of 29.9 ¡ 0.8 mA mM 21 , n = 9 at 95% CI, R 2 = 0.999) and a detection limit of 250 nM. The sensitivity and detection limit were similar to those reported for GOx, indicating a similar substrate conversion rate to hydrogen peroxide.…”

supporting

confidence: 72%

“…4). Since the response signal obtained for 10 mM glucose (S) became maximal at 8 mg mL 21 or 1480 U mL 21 GOx, this enzyme level was used for all subsequent studies. The high concentration of enzyme required for signal saturation of glucose was not surprising since the Michaelis constant (K M ) for GOx from A. niger is very high (33 mM).…”

Section: Eqn (4) Thus Illustrates That the Reaction Kinetics Are Govementioning

confidence: 99%

“…The high concentration of enzyme required for signal saturation of glucose was not surprising since the Michaelis constant (K M ) for GOx from A. niger is very high (33 mM). The MWCNT concentration used to modify the GC electrode also affected the glucose Attempts to construct a Pt nano -modified GC electrode with 1 mg mL 21 SWCNTs were not successful since the response signal for 10 mM glucose was only 4 mA, i.e. 100-fold lower than with MWCNTs.…”

Section: Eqn (4) Thus Illustrates That the Reaction Kinetics Are Govementioning

confidence: 99%

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Electrochemically-assisted deposition of oxidases on platinum nanoparticle/multi-walled carbon nanotube-modified electrodes

Male

Hrapovic

Luong

2007

Analyst

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Platinum nanoparticles were electrodeposited by a multi-potential step technique onto a multiwalled carbon nanotube (MWCNT) film pre-casted on a glassy carbon (GC) or boron-doped diamond (BDD) electrode. The MWCNT network consisted of Pt nanoparticles with an average diameter of 120 nm after an optimization of 36 deposition cycles. The resulting electrochemical sensors were capable of detecting hydrogen peroxide as low as 25 nM. Five different enzymes: glucose, lactate, glutamate, amino acid and xanthine oxidases, respectively, were deposited by a constant current technique for 5-10 min to form a stable and active biolayer for the analysis of their corresponding analytes. The glucose oxidase-based biosensor was linear up to 10 mM glucose with a detection limit of 250 nM and a response time of 5 s. Similar response times and detection limits were observed with glutamate, lactate, and amino acid oxidase despite the fact that the linear ranges were noticeably narrower. The mechanism of deposition was attributed to the decrease of local pH, created by oxygen evolution and effected enzyme precipitation.

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supporting

confidence: 72%

Section: Eqn (4) Thus Illustrates That the Reaction Kinetics Are Govementioning

confidence: 99%

Section: Eqn (4) Thus Illustrates That the Reaction Kinetics Are Govementioning

confidence: 99%

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Electrochemically-assisted deposition of oxidases on platinum nanoparticle/multi-walled carbon nanotube-modified electrodes

Male

Hrapovic

Luong

2007

Analyst

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“…Additionally, higher K m constants for immobilized enzymes compared with free enzymes in solution has been reported. 4,9 This is generally attributed to steric hindrance effects and mass transfer limitations associated with immobilized enzymes vs. free enzymes in solution. The higher K m of 0.75 mM determined for Figures 1c, 2c, and 4b may also be due to increased mass transfer limitations, as for these experiments, the reactions solutions were not mixed.…”

Section: Discussionmentioning

confidence: 99%

“…To enhance biocompatibility, researchers have created polymer interfaces between the enzymes and the device surfaces. [2][3][4][5][6][7][8][9] The next generation of ''smart'' biomaterials will require the intimate coupling of advances in microfabrication and biomolecular recognition. The novelty of the approach described here is the use of patterned microdevices (conductive surface patterning) for the assembly of enzymes through an activatable ''pro-tag.''…”

Section: Introductionmentioning

confidence: 99%

Towards area‐based in vitro metabolic engineering: Assembly of Pfs enzyme onto patterned microfabricated chips

Lewandowski

Bentley

et al. 2008

Biotechnology Progress

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in Wiley InterScience (www.interscience.wiley.com).We report an approach for spatially selective assembly of an enzyme onto selected patterns of microfabricated chips. Our approach is based on electrodeposition of the aminopolysaccharide chitosan onto selected electrode patterns and covalent conjugation of a target enzyme to chitosan upon biochemical activation of a genetically fused ''pro-tag.'' We report assembly of S-adenosylhomocysteine nucleosidase (Pfs) fused with a C-terminal pentatyrosine pro-tag. Pfs is a member of the bacterial autoinducer-2 biosynthesis pathway, catalyzing the irreversible cleavage of S-adenosylhomocysteine. The assembled Pfs retains its catalytic activity and structure, as demonstrated by retained antibody recognition. Assembly is controlled by the electrode area, resulting in reproducible rates of catalytic conversion for a given area, and thus allowing for area-based manipulation of catalysis and small molecule biosynthesis. Our approach enables optimization of small molecule biosynthesis in 1-step as well as multistep enzymatic reactions, including entire metabolic pathways, and we envision a wide variety of potential applications.

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Immobilization of alcohol dehydrogenase on films prepared by the electrochemical copolymerization of pyrrole and 1‐(2‐carboxyethyl)pyrrole for ethanol sensing

Shimomura

Kubo

Iizuka

et al. 2010

J of Applied Polymer Sci

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The electrochemical copolymerization of pyrrole and 1-(2-carboxyethyl)pyrrole (Py-COOH) was carried out, and a conducting polymer film with a Py-COOH content of 5% and a conductivity of 6.6 Â 10 À4 S/cm was obtained. Alcohol dehydrogenase (ADH) was attached through amide linkage onto the surface of the conducting polymer film for the purpose of fabricating an ADH-immobilized electrode applicable to the amperometric sensing of ethanol. The quantity and activity of the immobilized ADH were determined to be 400 lg/cm 2 and 0.6 U/mg, respectively. With the ADH-immobilized electrode, amperometric ethanol sensing was attempted in the presence of nicotinamide adenine dinucleotide (a cofactor of ADH) and Meldola's blue (an electron-transferring mediator). The ADHimmobilized electrode made the current response correspond to ethanol concentration, which reached 10 lA/cm 2 at a concentration of 14 mM. The selectivity of the sensing was examined with alcohols other than ethanol. It was found that the ADH/copolymer electrode had a considerably larger current response to allyl alcohol. The selectivity was attributed to the specificity of native ADH with respect to the oxidation of alcohols.

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Glucose oxidase, lactate oxidase, and galactose oxidase enzyme electrode based on polypyrrole with polyanion/PEG/enzyme conjugate dopant

Cited by 58 publications

References 32 publications

Electrochemically-assisted deposition of oxidases on platinum nanoparticle/multi-walled carbon nanotube-modified electrodes

Electrochemically-assisted deposition of oxidases on platinum nanoparticle/multi-walled carbon nanotube-modified electrodes

Towards area‐based in vitro metabolic engineering: Assembly of Pfs enzyme onto patterned microfabricated chips

Immobilization of alcohol dehydrogenase on films prepared by the electrochemical copolymerization of pyrrole and 1‐(2‐carboxyethyl)pyrrole for ethanol sensing

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