Preparation of enzyme electrode for D-glucose determination by immobilization of glucose oxidase on collagen membrane

1990 ◽  
Vol 55 (10) ◽  
pp. 2568-2574 ◽  
Author(s):  
Eva Vrbová ◽  
Miroslav Marek
Keyword(s):  
Glucose Oxidase ◽  
Oxygen Sensor ◽  
Immobilized Enzyme ◽  
Sensor Response ◽  
Enzyme Electrode ◽  
Collagen Membrane ◽  
Michaelis Constant ◽  
Glucose Determination ◽  
The Stability

An enzyme electrode for the determination of D-glucose was prepared by immobilization of glucose oxidase (EC 1.1.3.4.) on an activated collagen membrane using glutaraldehyde and the Ugi reaction resp. and by subsequent fixation of the membrane to an oxygen sensor of the Clark type. Two different procedures for the modification of the support, the composition of the reaction mixture and the immobilization time were examined. The electrode prepared was tested as regards the effect of pH and temperature on the magnitude of the response. The range of the linear dependence of the sensor response on substrate concentration (1.7 . 10-5 - 2.0 . 10-3), the apparent Michaelis constant of the immobilized enzyme (KM(app.) = 4.16 . 10-3 mol dm-3) and the stability of the biosensor as function of storage mode and number of assays performed with one electrode were determined. In view of the high stability and linear range of the concentration dependence the enzyme electrode is suitable for the determination of D-glucose in samples analyzed in agricultural and food laboratories.

Preparation and Utilization of a Biosensor Based on Galactose Oxidase

1992 ◽  
Vol 57 (11) ◽  
pp. 2287-2294 ◽  
Author(s):  
Eva Vrbová ◽  
Jitka Pecková ◽  
Miroslav Marek
Keyword(s):  
Oxygen Sensor ◽  
Specific Activity ◽  
Galactose Oxidase ◽  
Collagen Membrane ◽  
Michaelis Constant ◽  
Nylon Mesh ◽  
Native Collagen ◽  
The Stability ◽  
Galactose Content

An enzyme electrode for D-galactose determination was prepared by fixation of a carrier with immobilized galactose oxidase (E.C. 1.1.3.9) or coimmobilized galactose oxidase and catalase (E.C. 1.11.1.6) to a Clark-type oxygen sensor. The enzymes were immobilized either on a partially hydrolyzed nylon mesh or on a native collagen membrane using the Ugi reaction with cyclohexyl isocyanide and glutaraldehyde. The biosensors were characterized by the specific activity of the immobilized galactose oxidase, the apparent Michaelis constant KM(app.), and the stability expressed by time and a number of the performed analyses. The substrate specificity of the biosensor and the effect of pH and temperature of the reaction mixture on the response magnitude were also tested. The prepared biosensor was used for the determination of D-galactose content in samples of blood plasma and serum of patients with suspected galactosemia.

Single- and coupled-enzyme nylon-tube reactors for plasma glucose determination with glucose oxidase and aldehyde dehydrogenase.

1980 ◽  
Vol 26 (12) ◽  
pp. 1652-1655 ◽  
Author(s):  
W Hinsch ◽  
A Antonijewić ◽  
P V Sundaram
Keyword(s):  
Glucose Oxidase ◽  
Aldehyde Dehydrogenase ◽  
Plasma Glucose ◽  
Continuous Flow ◽  
Flow System ◽  
Low Cost ◽  
Immobilized Enzymes ◽  
Glucose Determination ◽  
Nylon Tube

Abstract We describe routine methods for determining glucose in plasma with use of aldehyde dehydrogenase or glucose oxidase-aldehyde dehydrogenase immobilized in a nylon tube that is integrated into a continuous-flow system. Although the coupled-enzyme nylon-tube reactors require the presence of a third enzyme, catalase, in solution, the kinetics are not so complicated as to preclude reliable routine determination of glucose at very low cost. Precision is good, and results correlate well with those by the method involving glucose oxidase in solution. More than 3000 tests may be carried out with one reactor. The immobilized enzymes are stable for several months at 4 degrees C when not in use.

Immobilized enzyme electrode for the determination of salicylate in blood serum

1986 ◽  
Vol 181 ◽  
pp. 219-225 ◽  
Author(s):  
Mohammad Ali Nabi Rahni ◽  
George G. Guilbault ◽  
G. Neto de Oliveira
Keyword(s):  
Blood Serum ◽  
Immobilized Enzyme ◽  
Enzyme Electrode

scholarly journals Dispersed Conducting Polymer Nanocomposites with Glucose Oxidase and Gold Nanoparticles for the Design of Enzymatic Glucose Biosensors

Polymers ◽  
2021 ◽  
Vol 13 (13) ◽  
pp. 2173
Author(s):  
Natalija German ◽  
Almira Ramanaviciene ◽  
Arunas Ramanavicius
Keyword(s):  
Glucose Oxidase ◽  
Conducting Polymer ◽  
Limit Of Detection ◽  
High Sensitivity ◽  
Serum Samples ◽  
Glucose Determination ◽  
Constant Potential ◽  
Good Repeatability ◽  
Graphite Rod

Biosensors for the determination of glucose concentration have a great significance in clinical diagnosis, and in the food and pharmaceutics industries. In this research, short-chain polyaniline (PANI) and polypyrrole (Ppy)-based nanocomposites with glucose oxidase (GOx) and 6 nm diameter AuNPs (AuNPs(6 nm)) were deposited on the graphite rod (GR) electrode followed by the immobilization of GOx. Optimal conditions for the modification of GR electrodes by conducting polymer-based nanocomposites and GOx were elaborated. The electrodes were investigated by cyclic voltammetry and constant potential amperometry in the presence of the redox mediator phenazine methosulfate (PMS). The improved enzymatic biosensors based on GR/PANI-AuNPs(6 nm)-GOx/GOx and GR/Ppy-AuNPs(6 nm)-GOx/GOx electrodes were characterized by high sensitivity (65.4 and 55.4 μA mM−1 cm−2), low limit of detection (0.070 and 0.071 mmol L−1), wide linear range (up to 16.5 mmol L−1), good repeatability (RSD 4.67 and 5.89%), and appropriate stability (half-life period (τ1/2) was 22 and 17 days, respectively). The excellent anti-interference ability to ascorbic and uric acids and successful practical application for glucose determination in serum samples was presented for GR/PANI-AuNPs(6 nm)-GOx/GOx electrode.

A New and Rapid Method for the Determination of Glucose by Measurement of Rate of Oxygen Consumption

1968 ◽  
Vol 14 (2) ◽  
pp. 116-131 ◽  
Author(s):  
Arnold Henry Kadish ◽  
Robert L Litle ◽  
James C Sternberg
Keyword(s):  
Hydrogen Peroxide ◽  
Oxygen Consumption ◽  
Glucose Oxidase ◽  
Oxygen Sensor ◽  
Direct Measure ◽  
Peroxide Formation ◽  
Glucose Levels ◽  
Rate Of Oxygen Consumption ◽  
Hydrogen Peroxide Formation

Abstract Glucose levels in serum, plasma, and urine are determined rapidly and conveniently by a new glucose oxidase method employing a polarographic oxygen sensor with a circuit modified to record the rate of oxygen consumption. The maximum apparent rate of oxygen consumption relative to the rate obtained with a glucose standard provides a direct measure of the glucose level in the sample; results are obtainable within 20 sec. after sample (100 µl.) addition and within 3 min. after a blood sample is withdrawn from a patient. Interferences associated with prior colorimetric glucose oxidase methods are avoided by measuring oxygen consumption instead of hydrogen peroxide formation. The method is described and results are presented showing a standard deviation of less than 1.5% on replicate determinations and a bias of 1% with respect to data obtained on the same samples by the automated ferricyanide method.

Determination of penicillin using an immobilized enzyme electrode, an undergraduate experiment

1984 ◽  
Vol 61 (7) ◽  
pp. 638 ◽  
Author(s):  
Theodore E. Mifflin ◽  
Kirk M. Andriano ◽  
Wayne B. Robbins
Keyword(s):  
Immobilized Enzyme ◽  
Enzyme Electrode

Amperometric Enzyme Electrodes for Substrates of Immobilized Pyranose Oxidase

1994 ◽  
Vol 59 (5) ◽  
pp. 1226-1234 ◽  
Author(s):  
Marek Petřivalský ◽  
Petr Skládal ◽  
Lumír Macholán ◽  
Jindřich Volc
Keyword(s):  
Immobilized Enzyme ◽  
Graphite Electrode ◽  
Sensor Response ◽  
Concentration Region ◽  
Covalent Bonds ◽  
Low Concentrations ◽  
Optimum Ph ◽  
Pyranose Oxidase ◽  
Linear Concentration

Two kinds of biosensors for the determination of pyranose oxidase substrates were developed, based on the detection of evolving hydrogen peroxide on a platinum or platinized graphite electrode at +650 or +400 mV, respectively. The membranes consisted of enzyme immobilized by covalent bonds on nylon net and were stable for 8 months of dry storage at 4 °C. In addition to D-glucose, low concentrations of D-xylose, D-galactose and L-sorbose can also be measured with the biosensor. The shift of the optimum pH of the immobilized enzyme to the alkaline region (8.0 - 9.5) is convenient for the borate buffer medium which extends the linear concentration region of the biosensor to 15 mmol l-1 for D-galactose, 30 mmol l-1 for D-xylose and 30 mmol l-1 for maltose. L-Sorbose provides no response up to a concentration of 10 mmol l-1 in 0.05 M borate and up to a concentration of 30 mmol l-1 in 0.2 M borate at pH 9.2. Interfering D-glucose was eliminated up to 2.5 mmol l-1 by means of an enzyme pre-membrane with immobilized hexokinase. The effect of ascorbate was eliminated, up to 75 mmol l-1, by using a cellulose acetate electrostatic barrier. D-Galactose, however, decreases the sensor response to D-glucose.

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