Specificity and kinetic parameters of recombinant Microdochium nivale carbohydrate oxidase

Kulys, Juozas; Tetianec, Lidija; Schneider, Palle

doi:10.1016/s1381-1177(00)00233-2

Cited by 15 publications

(16 citation statements)

References 13 publications

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“…The calculated k ox value was equal to (6.6±0.6)× 10 2 M −1 s −1 . This value is significantly less in comparison to flavin oxidases; it is 4.5× 10 5 M −1 s −1 for glucose oxidase from A. niger [21] and 1.7×10 5 M −1 s −1 for carbohydrate oxidase Microdochium nivale [19]. Low oxidation constant with dioxygen does not allow practical use of dioxygen as oxidizer even for ASDH catalyzed process.…”

Section: Kinetics Of Dehydrogenases With Artificial Electron Acceptorsmentioning

confidence: 90%

“…The kinetic curves were recorded at the wavelength of maximum of absorbance of radical cation. The concentrations of the electron acceptors were calculated using extinction coefficients of 16 mM −1 cm −1 at 530 nm for PPA +• , PPSA +• , and MPX +• [15,17,18], 7.4 mM −1 cm −1 at 462 nm for DMDHP +• [19], 9.8 mM −1 cm −1 at 604 nm for AMB +• [16], and 19.6 mM −1 cm −1 at 600 nm for DCPIP.…”

Section: Methodsmentioning

confidence: 99%

“…The analysis of the dependence of the initial rate on acceptor (A) or substrate (S) concentrations was performed by applying the ping-pong scheme [3,4,19]:…”

Section: Calculationsmentioning

confidence: 99%

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Probing Reactivity of PQQ-Dependent Carbohydrate Dehydrogenases Using Artificial Electron Acceptor

Tetianec¹,

Bratkovskaja²,

Kulys³

et al. 2010

Appl Biochem Biotechnol

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The kinetic parameters of carbohydrate oxidation catalyzed by Acinetobacter calcoaceticus pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenase (GDH) and Escherichia coli PQQ-dependent aldose sugar dehydrogenase (ASDH) were determined using various electron acceptors. The radical cations of organic compounds and 2,6-dichlorophenolindophenol are the most reactive with both enzymes in presence of glucose. The reactivity of dioxygen with ASDH is low; the bimolecular constant k (ox) = 660 M(-1) s(-1), while GDH reactivity with dioxygen is even less. The radical cation of 3-(10H-phenoxazin-10-yl)propionic acid was used as electron acceptor for reduced enzyme in the study of dehydrogenases carbohydrates specificity. Mono- and disaccharide reactivity with GDH is higher than the reactivity of oligosaccharides. For ASDH, the reactivity increased with the carbohydrate monomer number increase. The specificity of quinoproteins was compared with specificity of flavoprotein Microdochium nivale carbohydrate oxidase due to potential enzymes application for lactose oxidation.

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Section: Kinetics Of Dehydrogenases With Artificial Electron Acceptorsmentioning

confidence: 90%

Section: Methodsmentioning

confidence: 99%

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Probing Reactivity of PQQ-Dependent Carbohydrate Dehydrogenases Using Artificial Electron Acceptor

Tetianec¹,

Bratkovskaja²,

Kulys³

et al. 2010

Appl Biochem Biotechnol

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“…The kinetic enzyme reaction rate coefficients k cat was chosen from the very wide range of values [20][21][22][23] and K M were estimated from the experimental results in [24]:…”

Section: Hydrogen Ions Surface Generationmentioning

confidence: 99%

Physical Modeling of the Enzymatic Glucose-Fuelled Fuel Cells

Rubin¹,

Mor

2013

ACES

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An enzymatic glucose biofuel cell uses glucose as fuel and enzymes as biocatalyst, to transform biochemical energy into electrical energy. An analytical modelling of an enzymatic biofuel cell should be used, while developing fuel cell, to estimate its various enzymatic parameters, to obtain the highest voltage feasibly. The analytical model was developed, and the open circuit voltage (OCV) calculated by the model for various parameters of the fuel cell is in agreement with the experimental results. The OCV is interpreted by using this model, based on theoretical consideration of ions transportation in the solution. The generation and consumptions of the ions near the electrodes were defined in the model by exponential approximations, with different depletion coefficients. The model reveals that increasing the rates of hydrogen ions generation and (or) consumption by enzyme or chemical reactions leads to a higher value of OCV. The model points that the OCV is saturated with a glucose concentration and increased logarithmically with a surface enzyme concentration. Hence, a low glucose concentration is sufficient to obtain adequate OCV, on the one hand, but it can be increased by increasing electrode surface porosity, on the other hand. This model can be expanded to include time and close circuit voltage.

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“…A carbohydrate oxidase purified from Microdochium nivale (COXMn) (Kulys, Tetianec, & Schneider, 2001;Xu et al, 2001) was characterised as a flavoenzyme, which catalyses both the oxidation of glucose and other mono-and oligosaccharides by reacting with the aldehyde function at C1, and the concomitant reduction of oxygen to hydrogen peroxide. The mechanism of the C1 oxidation by oxygen is a Ping Pong mechanism (Kulys et al, 2001).…”

Section: Introductionmentioning

confidence: 99%