• KSBB Journal
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• v.21 no.6 s.101
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• pp.456-460
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• 2006

We investigated the activity and stability of alcohol oxidase from Hansenula sp., Pichia pastoris, and Candida boidinii under the electric stimulation. The activity and stability of alcohol oxidase depended on electric output voltage, electric stimulation time. This inactivation of the enzyme under electric stimulation could be recovered by stabilizing additives such as sugars, surfactants and hydrogels. These alcohol oxidase was more stable in trehalose, Triton X-100, Brji solution and alcohol oxidase from Hansenula is more stable than that from P. pastoris, and C. boidinii. The stabilizing of enzymes against electric stimulation showed a great potential use of enzymes in biotechnology and medical engineering fields.

• The Korean Journal of Food And Nutrition
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• v.18 no.1
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• pp.4-10
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• 2005

Periodate-oxidized soluble starch increased pH stability of Aspergillus awamori a-glucosidase. After incubation for two hours, the enzyme in the absence of oxidized soluble starch was stable in the range of pH 3-7 at 40℃, pH 3-6 at 50℃ and the enzyme in the presence of oxidized soluble starch was stable in the range of pH 3-9 at 40℃, pH 3-8 at 50℃. At 60℃, the enzyme was stable in pH 3-6 regardless of the presence or absence of IO₄-oxidized soluble starch, but when IO₄-oxidized soluble starch existed in pH 5-6, remained activity of the enzyme increased 20% more than when it didn't exist. The enzyme modified with IO₄-oxidized soluble starch remained 70% of activity in pH 9, but native enzyme didn't remain, showing the increase of stability due to modification. In thermal stability, modified enzyme remained 12% at 50℃ and 7% at 80℃. But native enzyme remained 8% at 50℃ and didn't remain at more than 70℃. The result of HPLC analysis revealed the subunit of the enzyme at under pH 2 or over pH 9 was separated or the enzyme was denatured and conjugated. Protein structure of native enzyme was denatured by acidic and basic pH but was stable in the presence of IO₄-oxidized soluble starch.

• Journal of Life Science
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• v.17 no.7 s.87
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• pp.990-995
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• 2007

We tested the effect of sodium tungstate, which disturbs the molybdenum cofactor formation, on the activities of aldehyde oxidase(AO) and the growth of maize(Zea mays) primary roots. As reported in other plants, sodium tungstate inhibited AO also in the maize root concentration-dependently. The inhibitory effect of sodium tungstate was observed only when the inhibitor was applied to the living plants. Application of tungstate to the extracted protein did not show any effect. Western analysis revealed slightly decreased level of AO protein in the presence of tungstate, indicating a positive feedback of gene regulation by the product. We also tested the effects of tungstate on the root growth. The elongation of primary root and the development of lateral roots, which are sensitive to the absolute level of auxin, were decreased in the presence of sodium tungstate. However, the gravitropic curvature of the primary root, which is dependent on the relative amount of auxin at both sides, was unaffected. These data suggested the decrease of auxin biosynthesis by the application of tungstate. However, the level of free IAA was unaffected by tungstate application. We discuss the possible explanations for the observed results.

• Biomedical Science Letters
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• v.4 no.2
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• pp.103-112
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• 1998

We have developed a simple and accurate strip test that measures the blood glucose level semiquantitatively by visual observation, or qualitatively by using UltraScan spectrocolorimeter. The strip has solid phase reagents, including glucose oxidase, peroxidase, chromogen, affixed to a plastic support. The strip test is capable of measuring blood glucose level in the range of 0∼800 mg/dl and generating the results within 2 to 3 minutes. Human blood specimens obtained from normal individuals and the diabetic patients were evaluated by the new blood glucose strip and by the kit supplied by other commercial products. The test results exhibit the correlation coefficient of 0.964. The new test strip is proven simple and accurate, and it offers an alternative to the commercially available glucose tests.

• 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.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.485-488
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• 2000

Methyl mercaptan oxidase was isolated and purified from Thiobacillus thioparus TK-m for the detection of mercaptans. The procedure of purification involved DEAE-Sephacel and Superose 12 column chromatographies with recovery yields of 47.5 and 48.5 %, and specific activity of 374 and 1240.8 units/mg-protein, respectively. The molecular weight of purified methyl mercaptan oxidase was determined to be 66.1 kDa by SDS-PAGE. Optimum temperature for activity was observed at $55\;^{circ}C$. This enzyme was activated by $(NH_4)_2SO_4$ and NaCl and inhibited by $NH_4Cl$.

• The Microorganisms and Industry
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• v.17 no.2
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• pp.18-21
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• 1991

생물은 자기 복제를 통한 생장이나 생명유지를 위해 에너지를 필요로 한다. 화학영양생물은 화학에너지를 발효 혹은 호흡을 통해 생물학적 에너지로 전환시키며, 광영양생물은 광합성 작용을 통해 광에너지를 이용한다. 발효, 호흡, 광합성은 모두 산화-환원 반응을 통해 이루어진다. 생물의 모든 에너지 전환반응은 산화-환원 반응, 즉 전자의 흐름으로 이루어지며 생명현상이 에너지를 필요로 하기 때문에 생명현상은 전자의 흐름으로 이루어진다고 할 수 있다. 모든 생물이 에너지 전환 반응에 산화-환원 반응을 이용한다는 말은 생물이 많은 종류의 산화-환원 효소를 보유하고 있다는 뜻이며, 실제 많은 종류의 산화-환원 효소가 발견되고 연구되었다.

• Korean Chemical Engineering Research
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• v.61 no.4
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• pp.576-583
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• 2023

This study aimed to investigate the impact of enhancing the electrode conductivity and mitigating the production of hydrogen peroxide - a by-product arising from lactate oxidation - on the performance of lactate electrodes. The electrical conductivity of the electrode was improved by modifying the surface of carbon paper with single-walled carbon nanotubes. Catalase was introduced to effectively eliminate the hydrogen peroxide produced during the lactate oxidation reaction. The carbon paper electrode, with simultaneous immobilization of both lactate oxidase and catalase, yielded a current 1.7 times greater than the electrode where only lactate oxidase was immobilized. The electrode in which lactate oxidase and catalase were co-immobilized on the surface of carbon paper modified with single-walled carbon nanotubes, produced a current of 171 µA, which was more than twice as much current as the carbon paper with only lactate oxidase immobilized. The optimized electrode showed a linear response up to lactate concentration of 20 mM, confirming that it can be used as a sensor electrode.

• KSBB Journal
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• v.11 no.3
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• pp.270-275
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• 1996

Heterologous expression of glucose oxidase gene using recombinant yeast has been carried out. Polymerase chain reaction was conducted to obtain the gene encoding glucose oxidase from Aspergillus niger and sequence comparison indicated the cloned 1.9kb DNA fragment appeared to be the glucose oxidise structural gene containing a signal sequence for extracellular location. Transforming shuttle vector was constructed with YEp352 to express the cloned glucose oxidase gene under the control of either GAL1 or GAL10 promoter. Plate assay of recombinant yeasts has shown that GAL1 promoter was more effective in yielding glucose oxidise than GAL10 promoter. Among the five different concentrations of galactose tried, 1% galactose showed the highest induction of glucose oxidase. Cellular localization experiment of recombinant enzyme using spheroplast revealed that most of enzymes (80%) were secreted into culture media in contrast to A. niger. There is no difference in heat-stability of recombinant enzyme up to $50^{\circ}C$ compared to the glucose oxidase from A. niger However, a dramatic reduction of enzyme activity was observed in both enzymes at $60^{\circ}C$.

• Applied Biological Chemistry
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• v.34 no.1
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• pp.8-13
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• 1991

In order to investigate interactions of autoxidizing lipids with protein, enzyme and peroxidizing linoleate were reacted in freeze-dried and emulsion systems at various level of water activities. Peroxide value, TBA value of oxidized linoleate increased during incubation Solubilities and the activities of enzymes decreased as water activity increased.