Competitive inhibition by hydrogen peroxide produced in glucose oxidation catalyzed by glucose oxidase

Bao, Jie; Furumoto, Keiji; Yoshimoto, Makoto; Fukunaga, Kimitoshi; Nakao, Katsumi

doi:10.1016/s1369-703x(02)00120-1

Cited by 84 publications

(58 citation statements)

References 7 publications

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“…Furthermore, thiophene is an undesirable medium component for many bacteria, which prevents their growth and further increases the stability of the electrode after being immersed in that solution. Moreover, in the presence of glucose the GO x was always in catalytic-action and significant amount of H 2 O 2 was produced in incubation vessel; the H 2 O 2 was forming free radicals, which in long term are highly likely to damage the GO x and in this way to reduce their enzymatic activity [42]. However, if thiophene is present in the same solution (polymerization solution) then the concentration of H 2 O 2 is reduced by involvement of this compound in polymerization reaction of thiophene.…”

Section: Stability Of Gre/go X /Ptp-modified Electrodesmentioning

confidence: 99%

Enzymatic polymerization of polythiophene by immobilized glucose oxidase

Krikstolaityte

Kuliesius

Ramanavičienė

et al. 2014

Polymer

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Section: Stability Of Gre/go X /Ptp-modified Electrodesmentioning

confidence: 99%

Enzymatic polymerization of polythiophene by immobilized glucose oxidase

Krikstolaityte

Kuliesius

Ramanavičienė

et al. 2014

Polymer

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“…31 It was reported that the stability of the GOx enzyme could be greatly improved by adding catalase enzymes to remove H2O2 quickly. 32 Thus, there is less chance of inhibiting GOx enzymes by the intermediate product in reactor I than in the other two types of reactors, because the intermediate product can be quickly converted to the final product by having HRP enzymes nearby GOx in reactor I.…”

Section: Test Of the Microreactorsmentioning

confidence: 99%

Spatial Distance Effect of Bienzymes on the Efficiency of Sequential Reactions in a Microfluidic Reactor Packed with Enzyme-immobilized Microbeads

Heo

2014

ANAL. SCI.

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Recently, microfabrication technology has opened up a new era in the applications of immobilized enzymes. Three different configurations of microfluidic reactors packed with enzyme-bearing microbeads were examined to show that the overall efficiency of coupled enzyme-catalyzed reactions depends on the spatial relationship of two enzymes immobilized on the bead surfaces. The spatial distances of glucose oxidase (GOx) and horseradish peroxidase (HRP) enzymes were controlled by using microbeads as a supporting matrix for immobilizing the two enzymes and packing them in two microfluidic chambers. A microreactor packed with microbeads coimmobilized with the two enzymes showed a better overall reaction efficiency than the other two reactors, where the two enzymes were spatially distant, under a flow condition. These results are ascribed to the reduced diffusional loss of an intermediate product in the bienzyme-coimmobilized microreactor. Furthermore, the inhibition of the GOx enzyme by H2O2, an intermediate product, can be eliminated by quickly converting H2O2 to a final non-inhibiting product in the bienzyme-coimmobilized microreactor.Keywords Microfluidic reactor, sequential enzyme reaction, enzyme immobilization

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“…The immobilization of GOD on a solid matrix prevents inactivation and increases its thermal and pH stability. Hydrogen peroxide formed during the oxidation reaction can attach the residues of GOD and decrease its catalytic activity [13][14][15]; to remove it, immobilized catalase (CAT) is usually added to the reaction mixture or is coimmobilized with GOD [15,16]. The utilization of reactions catalyzed by immobilized GOD plus catalase has increased in recent years in the fields of food processing, chemical processing, analytical practice and medicine [17].…”

mentioning

confidence: 99%

Enzymatic Oxidation and Separation of Various Saccharides with Immobilized Glucose Oxidase

Mislovičová

Pätoprstý

Vikartovská

2010

Appl Biochem Biotechnol

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Glucose oxidase from Aspergillus niger, the specific enzyme for beta-D-glucose oxidation, can also oxidize other related saccharides at very slow or negligible rates. The present study aimed to compare the kinetics of D-glucose oxidation using immobilized glucose oxidase on bead cellulose for the oxidation of related saccharides using the same biocatalyst. The significant differences were observed between the reaction rates for D-glucose and other saccharides examined. As a result, k (cat)/K (M) ratio for D-glucose was determined to be 42 times higher than D-mannose, 61.6 times higher than D-galactose, 279 times higher than D-xylose, and 254 times higher than for D-fructose and D-cellobiose. On the basis of these differences, the ability of immobilized glucose oxidase to remove D-glucose from D-cellobiose, D-glucose from D-xylose, and D-xylose from D-lyxose was examined. Immobilized catalase on Eupergit and mixed with immobilized glucose oxidase on bead cellulose or co-immobilized with glucose oxidase on bead cellulose was used for elimination of hydrogen peroxide from the reaction mixture. The accelerated elimination of D-glucose and D-xylose in the presence of co-immobilized catalase was observed. The co-immobilized glucose oxidase and catalase were able to decrease D-glucose or D-xylose content to 0-0.005% of their initial concentrations, while a minimum decrease of low oxidized saccharides D-xylose, D-cellobiose, and D-lyxose, respectively, was observed.

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Competitive inhibition by hydrogen peroxide produced in glucose oxidation catalyzed by glucose oxidase

Cited by 84 publications

References 7 publications

Enzymatic polymerization of polythiophene by immobilized glucose oxidase

Enzymatic polymerization of polythiophene by immobilized glucose oxidase

Spatial Distance Effect of Bienzymes on the Efficiency of Sequential Reactions in a Microfluidic Reactor Packed with Enzyme-immobilized Microbeads

Enzymatic Oxidation and Separation of Various Saccharides with Immobilized Glucose Oxidase

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