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Results for “OXIDASE AND PEROXIDASE”

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At least 55 records · Page 3Linked to original sources
PubMed1996

Experimental procedure for a hydrogen peroxide assay based on the peroxidase-oxidase reaction.

A low-cost assay method that is able to measure H2O2 concentrations as low as the nano-molar range is described. The assay solution contains NADH, horseradish peroxidase, and superoxide dismutase at PH 7.5. After the addition of the sample, the decrease in NADH concentration measured by spectrophotometry is proportional to the H2O2 concentration. Because of superoxide dismutation, a high amplification factor defined as moles NADH oxidised per mole H2O2 added is obtained, which allows the sensitivity limit of the method to be greatly improved. We have established the conditions under which the amplification factor can be stabilised at a high level: the best compromise is to increase both the horseradish peroxidase and superoxide dismutase concentrations. Finally, we have also shown that coupled to specific oxidases, our assay method is suitable for measuring very low concentrations of biochemicals that can be oxidized by oxygen with H2O2 production.

Computer Simulation↗
PubMed1997

Reactive liposomes encapsulating a glucose oxidase-peroxidase system with antibacterial activity.

Liposomes were prepared from phospholipid mixtures of dipalmitoylphosphatidylcholine (DPPC) and phosphatidylinositol (PI), encapsulating the enzymes glucose oxidase (GO) and GO in combination with horse radish peroxidase (HRP) by both extrusion (VET) and reverse-phase evaporation (REV). The optimum level of PI in DPPC/PI liposomes for targeting to biofilms of the oral bacterium Streptococcus gordonii has been established. The liposomes were characterised in terms of the content and activity of the encapsulated enzymes. The antibacterial activity of these 'reactive' liposomes arising from hydrogen peroxide and oxyacids in the presence of the substrates glucose and iodide ions, after targeting to the biofilms, were measured both as a function of liposome-biofilm incubation time and incubation time with the substrates. Bacterial inhibition increases with both liposome-biofilm and substrate-biofilm incubation time and with the extent of enzyme encapsulation. The reactive liposomes also display antibacterial activity in the presence of saliva. The reactive liposomes have potential value in the context of oral hygiene.

Anti-Bacterial Agents↗
PubMed2004

Real-time quantification of methanol in plants using a hybrid alcohol oxidase-peroxidase biosensor.

An amperometric biosensor immobilizing two enzymes and an electron mediator in an identical plane has been fabricated by the self-assembly technique for determination of methanol in crude plant samples. A self-assembled mixed monolayer of 4,4'-dithiodibutyric acid covalently attached two enzymes (Hansenula sp. alcohol oxidase and horseradish peroxidase) and 11-ferrocenyl-1-undecanethiol as an electron mediator on an Au electrode is exploited to produce a two-dimensional reaction matrix. The composition of the two enzymes and electron mediator molecules was optimized for detection of methanol in 0.1 M sodium phosphate buffer (pH 6.0). We successfully quantified methanol in low-purity tobacco (Nicotiana tabacum) plant extracts with the biosensor, which showed sensitivity comparable to that of gas chromatography/mass spectrometry. The redox-relay biosensor is quite simple and stable due to its covalent attachment to the Au surface, making it possible to downsize the construction. We fabricated a miniature methanol biosensor that fitted a well of a 96-well micro assay plate available for high-throughput assay. The biosensor is advantageous for the sensitive, continuous, and convenient determination of methanol.

Alcohol Oxidoreductases↗
PubMed1976

[Disadvantages of acid precipitation of proteins during the assay of blood glucose by the enzymatic glucose oxidase-peroxidase system].

In the enzymatic procedure for blood sugar by means of glucose oxidase, acid protein precipitation of blood by perchloric acid or trichloracetic acid liberated oxidizing substances, which enhanced the coloration density in oxidizing the reduced chromogen of the reaction mixture, independently of the hydrogen peroxide generated from glucose, and would give false high values of glycemia, if additional precautions had not been taken. These substances, increasing considerably with times and temperature of blood conservation, would be of peroxide nature, and would accumulate in red blood cells during their exposure to air.

Animals↗
PubMed1978

Oscillatory kinetics of the peroxidase-oxidase reaction in an open system. Experimental and theoretical studies.

1. The oscillations in the peroxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7)-catalyzed reaction between NADH and O2 are undamped when the reaction is carried out in a system open to both substrates and when 2,4-dichlorophenol and methylene blue are present in the solution. 2. The waveform of the oscillations changes when the concentration of peroxidase is varied. 3. The waveforms obtained experimentally can be simulated by a branched chain reaction model in which the branching is quadratic. 4. A correlation between the present knowledge of the reaction and the model can be made by combining well established and hypothetical reaction steps into a few reaction schemes. A selection among schemes however, is not possible at the present time. 5. Compound III participates in the reaction as an active intermediate. This is possible because dichlorophenol stimulates the break down of compound III.

Computers↗