A kinetic study of soluble glucose oxidase using a rotating-disc electrode

Stroe-Biezen, S. A. M. van; Janssen, Andrea P.M.; Janssen, L. J. J.

doi:10.1016/0302-4598(94)87032-2

Cited by 11 publications

(11 citation statements)

References 3 publications

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“…In the case of an immobilized enzyme product, inhibition could occur and the equilibrium constants would change. A study on glucose oxidase kinetics showed that 10 mM glucolactone produced little inhibition [45]. Inhibition by H 2 O 2 was observed when the concentration was changed from 0 to 0.75 mM.…”

Section: Mathematical Model Of the Amperometric Response Of God/ppd Imentioning

confidence: 93%

Improved platinization conditions produce a 60-fold increase in sensitivity of amperometric biosensors using glucose oxidase immobilized in poly-o-phenylenediamine

Corcuera

Cavalieri

Powers

2005

Journal of Electroanalytical Chemistry

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Section: Mathematical Model Of the Amperometric Response Of God/ppd Imentioning

confidence: 93%

Improved platinization conditions produce a 60-fold increase in sensitivity of amperometric biosensors using glucose oxidase immobilized in poly-o-phenylenediamine

Corcuera

Cavalieri

Powers

2005

Journal of Electroanalytical Chemistry

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“…Red stars indicate the absence of kinetic data. Abbreviations (and associated references for corresponding data) are as follows: Lac, laccase(380)(381)(382)(383); POD, peroxidase(380,(384)(385)(386)(387)(388); CDH, cellobiose dehydrogenase(102,(128)(129)(130)(389)(390)(391)(392); GOX, glucose oxidase(167,(393)(394)(395)(396)(397)(398); AAO, aryl alcohol oxidase(166,399,400); GDH, glucose dehydrogenase(401,402); AAQO, aryl alcohol quinone oxidoreductase(403); PDH, pyranose dehydrogenase(404)(405)(406)(407); AOX, alcohol oxidase(177,(408)(409)(410); P2O, pyranose 2-oxidase(181,(411)(412)(413); VAO, vanillyl alcohol oxidase(186,187); GLOX, glyoxal oxidase(170,<...>…”

mentioning

confidence: 99%

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

Bissaro

Várnai

Røhr

et al. 2018

Microbiol Mol Biol Rev

233

246

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SUMMARYBiomass constitutes an appealing alternative to fossil resources for the production of materials and energy. The abundance and attractiveness of vegetal biomass come along with challenges pertaining to the intricacy of its structure, evolved during billions of years to face and resist abiotic and biotic attacks. To achieve the daunting goal of plant cell wall decomposition, microorganisms have developed many (enzymatic) strategies, from which we seek inspiration to develop biotechnological processes. A major breakthrough in the field has been the discovery of enzymes today known as lytic polysaccharide monooxygenases (LPMOs), which, by catalyzing the oxidative cleavage of recalcitrant polysaccharides, allow canonical hydrolytic enzymes to depolymerize the biomass more efficiently. Very recently, it has been shown that LPMOs are not classical monooxygenases in that they can also use hydrogen peroxide (H2O2) as an oxidant. This discovery calls for a revision of our understanding of how lignocellulolytic enzymes are connected since H2O2is produced and used by several of them. The first part of this review is dedicated to the LPMO paradigm, describing knowns, unknowns, and uncertainties. We then present different lignocellulolytic redox systems, enzymatic or not, that depend on fluxes of reactive oxygen species (ROS). Based on an assessment of these putatively interconnected systems, we suggest that fine-tuning of H2O2levels and proximity between sites of H2O2production and consumption are important for fungal biomass conversion. In the last part of this review, we discuss how our evolving understanding of redox processes involved in biomass depolymerization may translate into industrial applications.

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“…4B also shows that signals after standard addition time 2400 s (39.0 mM glucose) cannot reach a steady state. The uncertainties associated with the measurement stability include applied voltage, operating temperature, stirring speed, and the product (D-glucono-d-lactone) inhibition [27] for glucose oxidase. Although the control of applied voltage, operating temperature, and stirring speed is good during the measurement, the applied voltage can be varied by those factors mentioned in the CV measurement at high glucose concentration.…”

Section: Batch Mode Electrode Performancementioning

confidence: 99%

On-line flow injection analysis using gold particle modified carbon electrode amperometric detection for real-time determination of glucose in immobilized enzyme hydrolysate of waste bamboo chopsticks

Cheng

Chang

Pijanowska

2012

Journal of Electroanalytical Chemistry

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A kinetic study of soluble glucose oxidase using a rotating-disc electrode

Cited by 11 publications

References 3 publications

Improved platinization conditions produce a 60-fold increase in sensitivity of amperometric biosensors using glucose oxidase immobilized in poly-o-phenylenediamine

Improved platinization conditions produce a 60-fold increase in sensitivity of amperometric biosensors using glucose oxidase immobilized in poly-o-phenylenediamine

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass

On-line flow injection analysis using gold particle modified carbon electrode amperometric detection for real-time determination of glucose in immobilized enzyme hydrolysate of waste bamboo chopsticks

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