A Bioelectrocatalysis Method for the Kinetic Measurement of Thermal Inactivation of a Redox Enzyme, Bilirubin Oxidase

Ikeda, Tokuji; Tatsumi, Hirosuke; Katano, Hajime; Wanibuchi, Mizue; Hibi, Takao; Kajino, Toshitaka

doi:10.2116/analsci.24.237

Cited by 30 publications

(24 citation statements)

References 17 publications

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“…In contrast to the case, PA1 may act like a protective colloid to increase the hydrophilicity and to prevent the aggregation of the enzyme. Also, in our previous study, 11 a large positive activation entropy of inactivation of BOD was obtained from the temperature dependence of ki. The stabilizing effect of the polyammonium may be attributed to decreasing the local disorder or to the desolvation of hydrating water molecules during inactivation.…”

Section: Stabilizing Effect Of Pa1 On Bod In Aqueous Solutionsmentioning

confidence: 94%

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Application of Poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as Enzyme Stabilizer for Bilirubin Oxidase Immobilized Electrode

et al. 2009

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It has been shown that polyammonium cations comprising quaternary ammonium and hydrophilic groups such as amide and hydroxyl groups stabilize a redox enzyme bilirubin oxidase (BOD). The BOD catalyzes the reaction: 4[Fe(CN)6] 4-+ 4H + + O2 → 4[Fe(CN)6] 3-+ 2H2O, and has been a promising enzyme for use as a cathode catalyst in biofuel cells. In this study, the stabilizing effect of poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene] (PA1) on BOD has been investigated. The sample solution containing BOD and the PA1 salt was kept at a given temperature, and the loss of the enzymatic activity was detected after given stored times. The activity decreased exponentially with stored time so that the first-order rate-constant of inactivation was determined. The inactivation rate-constant lowered with increasing the concentration of the PA1 salt, suggesting that BOD was stabilized by the association with the PA1 cation. The PA1 cation may act like a protective colloid or decrease the local disorder of BOD by its wrapping. A membrane-covered electrode containing BOD, PA1, and [Fe(CN)6] 4-/3-in the internal solution phase was examined in air-saturated aqueous solution. The electrode gave a well-defined current-potential curve with a steady state limiting current due to the PA1-[Fe(CN)6] 4-/3-polyion complex-mediated bioelectrocatalytic current for the reduction of O2. The decreasing of the steady state limiting current became slower in the presence of the PA1 salt, indicating again the stabilizing effect of PA1 cation on BOD.

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Section: Stabilizing Effect Of Pa1 On Bod In Aqueous Solutionsmentioning

confidence: 94%

“…The relative activity decreased exponentially with ts, suggesting a first-order kinetics of the inactivation. 11 We assume the following simple mechanism of inactivation:…”

Section: Stabilizing Effect Of Pa1 On Bod In Aqueous Solutionsmentioning

confidence: 99%

Application of Poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as Enzyme Stabilizer for Bilirubin Oxidase Immobilized Electrode

et al. 2009

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“…The effect can be studied by a bioelectroanalysis method in which the inactivation process is followed by the enzymatic bioelectrocatalytic current. 14,15 Unlike the conventional spectrophotometric enzyme assay, this method can measure the enzyme activity in solution continually and directly, so that the rate constants and kinetic parameters for the thermal inactivation of enzymes can be determined advantageously. Using the bioelectroanalysis method, εPL has been found to be a superior stabilizer for glucose oxidase (GOD).…”

Section: Introductionmentioning

confidence: 99%

Analytical Methods for the Detection and Purification of ε-Poly-L-lysine for Studying Biopolymer Synthetases, and Bioelectroanalysis Methods for Its Functional Evaluation

et al. 2014

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“…8,9 BOD has proven to be a promising enzyme for use as a cathode catalyst in biofuel cells, 10,11 and its stability in solutions has been also studied electrochemically. [12][13][14] Like other multicopper enzymes, BOD from Trachyderma tsunodae (T.t. BOD) is inhibited by some anions such as N3 -, SCN -, F -, Cl -, and Br -ions.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of an Electrochemical Method for the Analysis of Enzymatic Inhibition Reactions

Uematsu

Katano

2013

ANAL. SCI.

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A Bioelectrocatalysis Method for the Kinetic Measurement of Thermal Inactivation of a Redox Enzyme, Bilirubin Oxidase

Cited by 30 publications

References 17 publications

Application of Poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as Enzyme Stabilizer for Bilirubin Oxidase Immobilized Electrode

Application of Poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as Enzyme Stabilizer for Bilirubin Oxidase Immobilized Electrode

Analytical Methods for the Detection and Purification of ε-Poly-L-lysine for Studying Biopolymer Synthetases, and Bioelectroanalysis Methods for Its Functional Evaluation

Evaluation of an Electrochemical Method for the Analysis of Enzymatic Inhibition Reactions

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