• Korean Journal of Food Science and Technology
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• v.28 no.5
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• pp.974-980
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• 1996

A biosensor was prepared with dual cathode electrode and immobilized enzyme membrane. A nylon net was used for the immobilization of glucose oxidase and alcohol oxidase. The immobilized enzymes were placed on the surface of the electrode which was prepared with one anode and two cathodes as an oxygen electrode. The determination of components by the biosensor was based on the consumption of dissolved oxygen. The optimum condition of this system was 0.1 M potassium phosphate buffer solution, pH 7.5 at $35^{\circ}C$. Glucose and ethanol in takju were simultaneously determined by the biosensor. Comparing with UV-spectrophotometer and gas chromatograph for cross checking, there was a good correlation between the biosensor and the conventional methods. Biosensor with dual cathode electrode required no clarification or pretreatments. It was used for simultaneous determination of glucose and ethanol during the fermentation of takju.

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

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2000.07a
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• pp.909-912
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• 2000

We synthesized polypyrrole (PPy) nanotubules by oxidative polymerization of the pyrrole monomer within the pores of a polycarbonate template. The electrochemical behavior was investigated using cyclic voltammetry. The redox potential was about -0.5 V vs. Ag/AgCl reference electrode, while the potential was about 0 V for PPy film. It is considered as the backbone grows according to the pore wall. Therefore, it is possible to be arranged regularly. That leads to improvement in the electron hopping. By electrochemical doping of glucose oxidase (GOx) on PPy nanotubules, an enzyme electrode has been fabricated. The kinetic parameter of biochemical reaction with glucose was evaluated. The formal Michaelis constant and maximum current calculated by computer were about 11.4 mmol $dm^3$ and 170.85 A respectively. Obviously, an affinity for the substrate and current response of the PPy nanotubules enzyme electrode are rather good, comparing with that of PPy film.

• KSBB Journal
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• v.13 no.3
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• pp.244-250
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• 1998

Flow-injection analysis (FIA) for on-line monitoring of glucose and acetate are described and employed in E.coli fermentation process. Glucose oxidase (GOD) for the detection of glucose is immobilized on epoxy polymer support, which is packed in a small cartirdge, and applied to a GOD-FIA system. The detection of acetate is based on the inhibition of acetate to the oxidation of sarcosine by sarcosine oxidase (SOD). SOD is also immobilized on epoxy polymer support and used for a SOD-FIA system. GOD-FIA system is characterized as well as SOD-FIA system by the investigation of the effects of pH, temperature and metabolites in samples on the peak height. GOD-FIA and SOD-FIA systems were also applied for on-line On-line measurements buy FIA measurements by FIA were in god agreement with off-line measurements.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.15 no.7
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• pp.621-626
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• 2002

In the case of immobilizing of glucose oxidase (GOx) in polypyrrole (PPy) conducting polymer using electrosynthesis, the GOx 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 GOx and the backbone of the PPy. That is mainly due to insulating property and net chain of the GOx. Since being the case, it is useless to increase in amount of GOx mere than reasonable in the synthetic solution. We improved the amount of immobilized GOx into the PPy by adding a little ethanol in the synthetic solution without any more amount of GOx in the solution. We electrochemically analyzed an improvement in the immobilizing event. For the glucose sensing, when ethanol was added by 0.1 mol $dm^{-3}$ in the synthetic solution, the Michaelis constant of the resulting enzyme electrode was about 32 mmol $dm^{-3}$ and maximum current was about $146\mu A$.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.15 no.7
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• pp.615-620
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• 2002

In the case of immobilizing of glucose oxidase into polypyrrole (PPy) using electrosynthesis, the glucose oxidise (GOx) forms a coordinate bond with the polymers backbone. However, because of intrinsic insulation and net-chain of the enzyme, the charge transfer and mass transport are obstructed during the film growth. Therefore, the film growth is dull. We synthesized enzyme electrodes by electropolymerization added some organic solvent, such as ethanol and tetrahydrofuran (THF). The formative seeds of film growth was delayed by adding ethanol. The delay was induced by radical transfer between ethanol and pyrrole monomer. The radical transfer reactions shared the contribution of dopants between electrolyte anion and GOx polyanion. This led to increase amount of immobilized the enzyme in PPy. For the UV absorption spectra of synthetic solution before synthesis and after, in the case of ethanol added, the optical density was slightly decreased for the GOx peaks. It suggests amount of GOx in the solution was decreased and amount of GOx in the film was increased.

• Journal of Sensor Science and Technology
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• v.15 no.1
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• pp.28-33
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• 2006

Optical-fiber sensors have been developed to determine the concentrations of glucose and lactic acid in blood samples. Fluorescence dye [tris(2,2'-biphenyridine)-ruthenium(II)-chloride (RuBPY)] was entrapped by using a silicon to the unclad tip of a glass optic fiber. Enzymes like glucose oxidase (GOD) and lactate oxidase (LOD) have been immobilized by acrylamide resin adhesive, adsorption with zeolite or covalent bonding with aminopropyl-triethoxysilan. The fiber-optic glucose/lactate sensor was then used to analyze the concentrations of glucose and lactate in blood samples. The results were compared with the results of HPLC analysis and their difference was in error by less then 5 %.

• Proceedings of the KIEE Conference
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• 2002.11a
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• pp.248-250
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• 2002

본 논문은 당뇨병의 지표물질인 glucose의 농도를 극미량의 시료를 사용하여 정량 할 수 있는 방법을 개발하기 위하여 효소 고정화 전극을 제작하였다. 전극은 실리콘 웨이퍼상에 마이크로 크기의 전극을 반도체 공정을 이용하여 제작하였고, 전기 화학적 방법으로 마이크로 전극에 전도성 고분자 Polypyrrole(PPy) 및 glucose oxidase(GOx)를 고정화한 고감도의 전기화학 전극을 개발하였다. 도전성 고분자의 전기 화학적 중합은 순환 전압 전류법으로 하였으며, 용액의 액성에 따른 효소의 표면 전하를 이용하여, 도전성 고분자를 코팅한 전극에 일정한 전압을 인가하고 GOx를 도우핑 하였다. 제작된 전극은 시간대 전류법으로 glucose의 농도에 따른 감도 측정결과 마이크로 리터의 시료에 $5{\mu}A$/decade를 얻었다. 전극의 표면분석은 Scanning electron microscopy(SEM), Energy dispersive X-ray spectroscopy(EDX)를 이용하였다.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.730-734
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• 2005

Flow injection analysis (FIA) system was developed to monitor glucose concentrations in biotechnological processes. A fiber optic oxygen sensor was used to determine consumption of oxygen concentration by reaction of immobilized glucose oxidase (GOD). The GOD was immobilized on VA-Epoxy carrier and integrated into FIA system. A calibration curve for glucose was obtained in the range of 0.5 $g/L{\sim}3.0$ g/L.

• Journal of the Korean Chemical Society
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• v.43 no.3
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• pp.264-270
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• 1999

Enzyme electrodes for amperometric measurement of glucose were prepared by immobilization of glucose oxidase on an Immobilon-AV Affinity membrane and attachement to a Pt electrodes. The electrochemical oxidation of Hz02 was monitored at +0.8V vs. Ag/AgCl. Response was linear from 0.2 mM to 20mM. The detection limit was 10m3 mM. Response time, the optimum pH and life time of enzyme immobilized membrane was 12 seconds, pH 5.5(CH3COONaJCH3COOH) and about 27 days, respectively. When the enzyme electrode was applied for the determinaion of glucose with amperometric method, other physiolosical materials have not interfered. Also, we compared the result with that from AOAC(Association of Offical Analytical Chemists) method, measuring the glucose in sweet potato. The relative error was 0.1%.