• 한국식품과학회지
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• 제17권1호
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• pp.37-40
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• 1985

Glucose oxidase-catalase동시 고정화 효소계에 관한 반응을 연구하였다. 두 가지 효소를 미생물 세포벽에 동시 고정과한 제품과, glucose oxidase만 고정화 시킨 것 그리고 두가지 효소를 따로 고정화시켜 혼합한 제품의 반응성을 각각 조사한 결과 동시 고정화 제품이 가장 우수하였다. 충진식 연속 반응조에서 불활성화 상수$(K_d)$는 glucose oxidase만의 고정화 효소경우 $1.12\;{\times}\;10^{-2}\;hr^{-1}$이었고, 동시 고정화 효소의 경우 catalase/glucose oxidase=10일때 $2.17{\times}10^{-3}\;hr^{-1}$이었다. 또한 체장시간$({\tau})$이 $5.55g{\cdot}hr/l\;O_2$ 일때 catalase/glucose oxidase 1 및 10 모두 반응율이 가장 좋았고 이보다 길어지면 외부 물질 전달의 영향으로 반응율이 오히려 떨어 졌다. $O_2$의 최대 허용치는 체장시간 $8.3g{\cdot}hr/l$일때 나타났다. 본 연구 결과로 부터 glucose oxidase와 catalase 동시고정화 효소에서 생산성을 높이기 위해서는 glucose oxidase의 불활성화와 이 효소의 효율이 동시에 고려되도록 두 효소의 비율을 정해야 하는 것을 알았다.

• 한국전기전자재료학회논문지
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• 제13권6호
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• pp.520-525
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• 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.

• 대한전기학회:학술대회논문집
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• 대한전기학회 1999년도 추계학술대회 논문집 학회본부 C
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• pp.984-986
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• 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.

• 한국전기전자재료학회:학술대회논문집
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• 한국전기전자재료학회 1999년도 추계학술대회 논문집
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• pp.147-150
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• 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 Microbiology and Biotechnology
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• 제15권2호
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• pp.234-238
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• 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
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• 제1권1호
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• pp.64-70
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• 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.

• 한국식품영양과학회지
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• 제22권6호
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• pp.792-796
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• 1993

The synthesis alcohol-oxidase[EC 1.1.3.13] was investigated in the yeasts, Candida boidinii CBS 8106 and C. boidinii CBS 2428, during growth on different carbon sources. Alcohol-oxidase was undetectable in all strains submitted to the test in the mineral salts medium containing 1.0% glucose, but its production was rapidly increased when the carbon source was changed glucose to 1.0% methanol after 24hrs of incubation. When cells were grown on the various carbon sources (glucose, xylose, lactose, glycerol, galactose, saccharose, sorbose, lactic acid or acetic acid), the alcohol-oxidase activity was undetected. These carbon sources together with methanol yielded far better synthesis of alcohol-oxidase than in the case of carbon sources alone. Alcohol-oxidase was active towards alcohol of shorter alkyl-chain length than C5 and unsaturated alcohols. Its affinity for these alcohols decreased with the increasing length of the alkyl-chain. The apparent Km values for the methanol of Candida boidinii CBS 8106 and C. boidinii CBS 2428 were 1.96 and 1.21, respestively.

• KSBB Journal
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• 제9권1호
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• pp.55-62
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• 1994

Aspergillus niger 균체로부터 황산암모늄 분별침전, 이온교환 크로마토그래피, 한외여과, 소수성 크로마토그래피 과정을 거쳐 glucose oxidase( EC 1.1. 3.4)를 순수 정제하였다. 최종 정제과정인 소수성 크로마토그래퍼에 의해 소수성은 다르나 glucose oxidase의 활성을 갖는 A, B fraction이 얻어졌고, 그의 비활성도는 각각 2,191, 1,273units/mg이었다. A와 B는 분자량 78,000의 당단백질임이 확인되었으나, HPLC 겔 여과로 측정한 분자량, 최대 흡수 파장, 등전점 등에 차이를 보였다. 효소 A는 $\beta$-D-glucose를 특이적으로 산화하였고, 촉매 활성에 대한 최적 온도 는 $30^{\circ}C$, 최적 pH는 3.5이었으며, SDS에 대하여 비교적 강한 저항성을 나타내었고, 촉매 기능은 10mM $Hg^{2+}$에 의해 급격히 억제되었다. 화학 수식 실험 결과 cysteine/ cystine중의 SH기가 glucose oxidase의 활성에 관여하고 있음이 시사되었다.

• 농업과학연구
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• 제11권2호
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• pp.223-232
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• 1984

Glucose oxidase에 의(依)한 건조용(乾燥用) 난백(卵白)의 탈당반응(脫糖反應)에 미치는 영향(影響)을 구명(究明)하기 위(爲)하여 난백중(卵白中)의 glucose함량(含量) 측정법(測定法)과 효소(酵素)의 활성(活性)에 미치는 최적조건(最適條件)을 검토(檢討)하였으며 효소(酵素)의 농도(濃度), pH, 온도(溫度) 및 효소(酵素)의 공급(供給)에 의(依)한 난백(卵白)의 탈당속도(脫糖速度)와 난백(卵白)의 기포력(氣泡力)을 조사(調査)한 결과(結果)는 다음과 같다. 1. Dianisidine법(法)은 glucose $100{\mu}g$ 범위내에서의 glucose 정량법(定量法)으로 적합하다고 인정(認定)되었다. 2. Glucose oxidase활성(活性)의 glucose에 대(對)한 최적(最適)pH는 약(約) 5.0 부근이었으며, pH안정성(安定性)은 pH 4.0~5.5의 범위에서 $50^{\circ}C$로 30분(分) 처리(處理)했을 때 안정(安定)했다. 3. Glucose에 대(對)한 glucose oxidase 반응(反應)의 최적온도(最適온度)는 약(約) $20^{\circ}C$ 부근이었으며, 그 활성(活性)은 $50^{\circ}C$까지 안정(安定)하였다. 4. Glucose oxidase에 의(依)한 난백(卵白)의 탈당(脫糖)은 효소농도(酵素濃度), pH 및 산소(酸素)의 공급(供給)등에 의(依)하여 영향(影響)을 받았으며, 0.1% 효소농도(酵素濃度), pH 7.0, $26^{\circ}C$ 및 30% $H_2O_2$ 5.0ml의 반응조건(反應條件)에서 탈당(脫糖)은 10시간(時間)이 소요되었다. 5. 공시(供試) 난백(卵白)의 기포력(氣泡力)은 90.0ml(control)에서 103.4ml(trypsin+glucose oxidase)의 범위였으며, 단백질분해효소(蛋白質分解酵素)로 처리(處理)했을 때 대조구(對照區)에 비(比)해 기포안정성(氣泡安定性)이 낮았다.

• Mycobiology
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• 제39권1호
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• pp.64-66
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• 2011

Most fungi possess several hydrogen peroxide-generating enzymes, glucose oxidase and pyranose oxidase. Pyranose oxidase can use glucose as its substrate to generate hydrogen peroxide. White rot fungi, which degrade diverse recalcitrant compounds, contain lignin-degrading enzymes, and lignin peroxidase and manganese peroxidase require hydrogen peroxide for their enzymatic reactions. In this study, we isolated a cDNA fragment of pyranose oxidase from Phlebia tremellosa using PCR and examined its expression under the degradation conditions of diethylphthalate (DEP). Pyranose oxidase expression was enhanced up to 30% by the addition of DEP, and this result supports the possible involvement of pyranose oxidase in the degradation of recalcitrant compounds.