• Proceedings of the KIEE Conference
• /
• 1999.11d
• /
• pp.984-986
• /
• 1999

In the case of immobilizing of glucose oxidase in organic polymer using electrosynthesis, the glucose oxidase obstructs charge transfer and mass transport during the film growth. This may lead to short chained polymer and make charge-coupling weak between the glucose oxidase and the backbone of the polymer. That is mainly due to insulating property and net chain of the glucose oxidase. Such being the case, it is useless to increase in amount of glucose oxidase more than reasonable in the synthetic solution. We establish by means of qualitative analysis that amount of immobilized glucose oxidase can be improved by adding a hole ethyl alcohol in the synthetic solution. As ethyl alcohol was added by 0.1mol $dm^{-3}$ in the synthetic solution, the faradic impedance of resultant electrode was increased about five times as much as the case of ethyl alcohol free in the solution, and mass transport was limited more than over. That is due to insulating property and net chain of the glucose oxidase. Moreover, in ultraviolet spectra of the synthetic solution, the adsorption peak at 285nm corresponding to glucose oxidase was decreased. It suggests increase in amount of immobilized glucose oxidase.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
• /
• 1999.11a
• /
• pp.147-150
• /
• 1999

In the case of immobilizing of glucose oxidase in organic polymer using electrosynthesis, the glucose oxidase obstructs charge transfer and mass transport during the film growth. This may lead to short chained polymer and/or make charge-coupling weak between the glucose oxidase and the backbone of the polymer. That is mainly due to insulating property and net chain of the glucose oxidase. Since being the case, it is useless to increase in amount of glucose oxidase more than reasonable in the synthetic solution. We establish qualitatively that amount of immobilization can be improved by adding a little ethanol in the synthetic solution. As ethanol was added by 0.1 rnol dm" in the synthetic solution, Michaelis-Menten constants of the resulting enzyme electrode decreased from 30.7 mmol $dm^{-3}$ to about 2 mmol $dm^{-3}$. That suggests increase in affinity of the enzyme electrode for glucose and in amount of the immobilized enzyme.zyme.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
• /
• v.13 no.6
• /
• pp.520-525
• /
• 2000

Glucose oxidase was immobilized in polypyrrole by electrosynthesis. The enzyme had an influence on the redox properties of a complex enzyme electrode. In the cyclic voltammograms of the enazyme electrode new peaks were appeared at the potential around 0.7V vs. Ag/AgCl in additional to the typical peaks for polypyrrole. The more immobilized the stronger the peaks became. During the cycling the pH of electrolyte solution was decreased to about 4.4 The reason for that is to be the proton released from the carboxyl in the glucose oxidase in order to keep on a charge neutrality of the oxidized enzyme. This fact suggests that the new peaks in the voltammograms are caused by the redox of glucose oxidase. In the AC impedance spectrum analysis of the electrode the diffusion of electrolyte anion was limited because of chained structure of the enzyme. The faradic impedance was large since the glucose oxidase is an insulator. Therefore when glucose oxidase is entrapped the enzyme should be limited in amount. Because the growth of the polypyrrole is accompanied both charge transfer and mass transport. For the traditional electrosynthesis that means amount of enzyme present in the electrode is limited to as much as film growable.

• Journal of Life Science
• /
• v.8 no.4
• /
• pp.416-420
• /
• 1998

Soybean sprouts peroxidase can be used for enzymatic determination of glucose. Peroxidase from soybean sprouts was purified by ammonium sulfate precipitation and DEAE Sephacel column chromatography. The glucose could be quantitatively assayed by using glucose oxidase and soybean sprouts peroxidase. The optimum pH and temperature for glucose assay were of pH 5.5 and $40^{\circ}C$, respectively. The relationship between absorbance and glucose concentration was linear. And also the relationship between absorbance and reaction time was linear. The reducing agents such as L-cysteine, dithiothreitol inhibited the glucose assay by glucose oxidase and soybean sprouts peroxidase.

• Korean Journal of Food Science and Technology
• /
• v.17 no.1
• /
• pp.37-40
• /
• 1985

The reactor performance of a coimmobilized glucose oxidase and catalase enzyme system was investigated. In the determination of efficiencies of glucose oxidase and catalase of dual, mixed and soluble systems, the dual type immobilized one was superior to either the soluble or to the mixed system. In the continuous plugflow bed reactor system of glucose oxidase and catalase, $k-d$, deactivation rare constant of glucose oxidase only and catalase/glucose oxidase = 10 were $1.12\;{\times}\;10^{-2}\;and\;2.17\;{\times}10^{-3}\;hr^{-1}$, respectively. In the effect of ${\tau}$, space time, the point of $O_2$ limitation is $5.5\;g{\cdot}hr/l$ in both catalase/glucose oxidase = 1 and 10. In the effect of $O_2$ concentration to reduce the $O_2$ diffusion limitation, it appeared that ${\tau}\;=\;8.3g{\cdot}r/l$ is the maximum point of $O_2$ concentration in both catalase/glucose oxidase = 1 and 10.

• Journal of Microbiology and Biotechnology
• /
• v.15 no.2
• /
• pp.234-238
• /
• 2005

Glucose oxidase was immobilized on the carboxylated multi-wall carbon nanotubes (MWNT-COOHs) in the presence of a coulping reagent, 1-ethy1-3-(3-dimethylaminopropy1) carbodiimide. Significant amounts of glucose oxidase were also immobilized on MWNT-COOHs without the coupling reagent. Various conditions for the immobilization of glucose oxidase were optimized. Optimal pH for the maximal activity of the immobilized glucose oxidase shifted to 7 from the optimal pH of 6 for the maximal activity of free enzyme due to the carboxy1 groups on the surface of MWNT-COOHs. An electrode of graphite rod with a diameter of 6 mm was fabricated using the immobilized glucose oxidase. The cyclic voltammetry study of the enzyme electrode revealed that the oxidation of glucose and subsequent transfer of electrons from the oxidation of glucose to the electrode were possible by the immobilized glucose oxidase without a mediator, implying that the enzyme electrode can be utilized for the development of biofuel cells.

• Advances in Traditional Medicine
• /
• v.1 no.1
• /
• pp.64-70
• /
• 2000

Effects of Rhizoma gastrodiae on glucose oxidase-induced neurotoxicity was investigated in cultured newborn mouse spinal dorsal root ganglion(DRG) neurons that were treated in the media with or without glucose oxidase. In addition, the protective effect of Rhizoma gastrodiae extract against glucose oxidase-induced neurotoxicity was examined. Cytotoxic values were expressed as a percentage of number of living cells by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. In this paper, exposure of neurons to glucose oxidase resulted in a significant call death in a dose- and time-dependent manners in DRG neuron cultures. The decrease in cell viability induced by the glucose oxidase was blocked by Rhizoma gastrodiae extract. These results indicate that the neuroprotective effect of Rhizoma gastrodiae extract against glucose oxidase-induced neurotoxicity may result from a prevention or attenuation of oxidative damage induced by glucose oxidase.

• Microbiology and Biotechnology Letters
• /
• v.15 no.6
• /
• pp.402-407
• /
• 1987

Glucose oxidase from Aspergillus niger KUF-04 was purified homogeneously by the procedure of seven steps including crystallization. The ball-like crystalline enzyme was obtained from the 23-fold purified enzyme solution. The glucose oxidase was found to be composed of two identical subunits and the molecular weight of the enzyme and its subunit were estimated to be about 210, 000 and 110, 000 by HPLC and SDS-acrylamide gel electrophoresis, respectively.

• Korean Journal of Microbiology
• /
• v.27 no.4
• /
• pp.430-435
• /
• 1989

Dextranase and glucose-osidase was investigated as an anti-plaque agent and a component of dentifrice. In vitro synthesis of the water-insoluble glucan was decreased with increasing amount of dextranase and glucose-oxidase. Dextranase was effective on the decrease of viable S. mutans, and the formation of plaque decreased. But it is not effective on the degradatio of plaque. As a research for addition of enzyme to the dentifrice components, we formulated the Model Dentifrice for stabilization of enzyme. At the Model Dentifrice, we confirmed the stability of enzyme by evalution of activity for a long time.

• Korean Journal of Agricultural Science
• /
• v.11 no.2
• /
• pp.223-232
• /
• 1984

The influences of some factors involved in removing glucose from egg white by the glucose oxidase system be fore drying were investigated. And the properties between foams prepared from raw and enzyme-treat ed egg white was compared. The results obtained we re summarized as follows; 1. The dianisidine method was found to be suitable for the measurement of egg white glucose in the range up to 100ug/ml. 2. The optimal pH of glucose oxidase activity on glucose was found to be a bout 5.0, and thats activity was most stable in the pH range of about 4.0~5.0 when that enzyme was treat ed for 30 minute at $50^{\circ}C$. 3. The optimal temperature for glucose oxidase reaction on glucose was found to be about $20^{\circ}C$, and that enzyme activity was s table up to $50^{\circ}C$. 4. The removing rate of glucose from egg white with glucose oxidase was influenced by the enzyme concentration, pH and oxygen addition, and the react ion time of the desugarization was about 10 hour sunder the conditions of 0.5% hydrogen peroxide, pH 7.0 and $26^{\circ}C$. 5. All of the each egg white treated with glucose oxidase, glucose oxidase+pancreatin, glucose oxidase+trypsin showed highly foaming ability than that of natural egg white(control), but thats foam stability, on the contrary, was reversed.