Determination of ethanol in alcoholic drinks using an enzyme biosensor containing alcohol dehydrogenase

2010 ◽  
Author(s):  
V. Polan ◽  
K. Vytras
Keyword(s):  
Alcohol Dehydrogenase ◽  
Alcoholic Drinks ◽  
Enzyme Biosensor

scholarly journals Conductimetric Biosensor for the Detection of Uric Acid by Immobilization Uricase on Nata de Coco Membrane—Pt Electrode

2011 ◽  
Vol 6 ◽  
pp. ACI.S7346 ◽  
Author(s):  
Ani Mulyasuryani ◽  
Arie Srihardiastutie
Keyword(s):  
Uric Acid ◽  
Human Serum ◽  
Candida Utilis ◽  
Medical Laboratory ◽  
Membrane Thickness ◽  
Serum Samples ◽  
Ph Change ◽  
Pt Electrode ◽  
Enzyme Biosensor

A conductimetric enzyme biosensor for uric acid detection has been developed. The uricase, as enzyme, is isolated from Candida utilis and immobilized on a nata de coco membrane-Pt electrode. The biosensor demonstrates a linear response to urate over the concentration range 1-6 ppm and has good selectivity properties. The response is affected by the membrane thickness and pH change in the range 7.5-9.5. The response time is three minutes in aqueous solutions and in human serum samples. Application of the biosensor to the determination of uric acid in human serum gave results that compared favourably with those obtained by medical laboratory. The operational stability of the biosensor was not less than three days and the relative error is smaller than 10%.

scholarly journals Rapid Determination of Ethanol in Food by Combination of Quinone-dependent Alcohol Dehydrogenase Reaction and Self-driven Coulometry.

1995 ◽  
Vol 42 (3) ◽  
pp. 163-168
Author(s):  
Kazuyo KAJINO ◽  
Ko FURUKAWA ◽  
Hiroaki EBISUYA ◽  
Masahiro FUKAYA ◽  
Sumio AKITA ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rapid Determination ◽  
Dehydrogenase Reaction

scholarly journals Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions

2003 ◽  
Vol 68 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rate Constants ◽  
Equilibrium Constants ◽  
Kinetic Mechanism ◽  
Yeast Alcohol Dehydrogenase ◽  
Catalyzed Reactions ◽  
The Individual ◽  
Individual Rate ◽  
Catalyzed Oxidation

In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25 ?C, have been estimated. The determination of the individual rate constants was achieved by fitting the reaction progress curves to the experimental data, using the procedures of the FITSIM and KINSIM software package of Carl Frieden. This work is the first report in the literature showing the internal equilibrium constants for the isomerization of the enzyme-NAD+ complex in yeast alcohol dehydrogenase-catalyzed reactions.

Evaluation of a modified alcohol dehydrogenase assay for the determination of ethanol in blood.

1982 ◽  
Vol 28 (10) ◽  
pp. 2125-2127 ◽  
Author(s):  
A Poklis ◽  
M A Mackell
Keyword(s):  
Gas Chromatography ◽  
Reaction Time ◽  
Alcohol Dehydrogenase ◽  
Correlation Coefficients ◽  
Least Square ◽  
Standard Curve ◽  
Analytical Recovery ◽  
Sigma Chemical ◽  
Enzymic Assay

Abstract We evaluated a new alcohol dehydrogenase (EC 1.1.1.1) enzymic assay (ADH-glycine, Sigma Chemical Co.) for the determination of ethanol in blood. This assay differs from the manufacturer's previous assay (ADH-pyrophosphate) in that glycine replaces pyrophosphate as the buffer and hydrazine replaces semicarbazide as the trapping agent. The standard curve for the assay was linear over blood ethanol concentrations of 0.50-5.00 g/L. The reaction time of the assay was 10 min. At 1.00 g/L within-run and between-run CVs were 3.96% (n = 20) and 4.01% (n = 20), respectively. Mean analytical recovery of ethanol added to whole blood at 0.50-5.00 g/L was 99.7% (SD 2.6%). We performed 100 consecutive clinical and forensic determinations by the ADH-glycine assay, the ADH-pyrophosphate assay, and gas chromatography. Correlation coefficients of the results by least-square linear regression were 0.995 for ADH-pyrophosphate vs ADH-glycine, and 0.990 for gas chromatography vs ADH-glycine. The major advantage of the ADH-glycine assay over the ADH-pyrophosphate assay is the shorter reaction time, 10 min vs 30 min.

Comparison of four kits for enzymatic determination of ethanol in blood.

1976 ◽  
Vol 22 (1) ◽  
pp. 83-86 ◽  
Author(s):  
H M Redetzki ◽  
W L Dees
Keyword(s):  
Alcohol Dehydrogenase ◽  
High Alcohol ◽  
Blood Concentrations ◽  
Blood Samples ◽  
Practical Test ◽  
Advantages And Disadvantages ◽  
Enzymatic Determination

Abstract We compared results obtained with four commercially available kits for the enzymatic (alcohol dehydrogenase) determination of ethanol in blood, in a practical test in which standardized blood samples were used. Each of the kits yielded reliable results with acceptable reproducibility. A tendency to record slightly lower values in the intermediate and high alcohol range is most likely related to incomplete (inhomogeneous) deproteinization. Blood samples containing ethanol plus various concentrations of methanol and isopropanol were analyzed to evaluate the specificity of assays. Highly toxic blood concentrations of methanol (1.5 g/liter) increased apparent ethanol values only insignificantly, but even small concentrations of isopropanol (0.5 g/liter) interfered in all kits to different but substantial extents. The specific technical characteristics of the kits, their advantages and disadvantages are discussed. Costs are compared for analysis of small numbers of samples.

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