• KSBB Journal
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• v.9 no.5
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• pp.525-531
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• 1994

Tyrosinase has two types of enzymatic activities, cresolase catalyzing the hydroxylation of monophenol and catecholase catalyzing the oxidation of o-phenol. Gradual inactivation of the enzyme during the reaction is a barrier to be overcome for the commercial application of the enzyme. Tyrosinase was stabilized by modifying the lysine residue of the enzyme using glutaraldehyde. In addition to that, tyrosinase was also stabilized by adapting the continuous reactor system. In packed bed reactor quinone could be easily removed, so the stability of tyrosinase increased. Borate buffer retarded the reaction rate of catechol to quinone and consequently decreased the tyroslnase inactivation. Tyrosinase immobilizer on controlled pore glass showed significantly enhanced stability in a packed-bed reactor.

• BMB Reports
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• v.31 no.3
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• pp.296-302
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• 1998

A potentiometric flow injection biosensor for the analysis of anti-cholinesterases (anti-ChEs), based on inhibition of enzyme activity, was developed. The sensor system consists of a reactor with acetylcholinesterase (AChE) immobilized on controlled pore glass and a detector with an $H^{+}-selective$ PVC-based membrane electrode. The principle of the analysis is based on the fact that the degree of inhibition of AChE by an anti-ChE is dependent on the concentration of the anti-ChE in contact with AChE. The sensor system was optimized by changing systematically the operating parameters of the sensor to evaluate the effect of the changes on sensor response to ACh. The optimized biosensor was applied to the analysis of paraoxon, an organophosphorus pesticide. Treatment of the inhibited enzyme with pyridine-2-aldoxime fully restored the enzyme activity allowing repeated use of the sensor.

• Membrane Journal
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• v.17 no.3
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• pp.233-243
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• 2007

In this study, a separate. which is a microporous membrane based on poly(vinylidene fluoride)(PVdF) was prepared by phase inversion method. Being prepared by dissolving the PVdF in the N,N'-dimethylformamide(DMF) with mechanical stirring, the homogenous casting solution was cast onto a clean glass plate. Pore size and porosity of the membranes were controlled by changing preparation condition. The highest porosity of the membrane was 78.6%. The mechanical property of the membrane was determined by using an universal testing machine(UTM). The morphology of the membrane was investigated by scanning electron microscopy(SEM). The cross-section of the membrane shows sponge-like small micro-pores.

• KSBB Journal
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• v.8 no.4
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• pp.328-335
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• 1993

A flow injection analysis(FIA) system was developed for the determination of cholesterol using immobilized cholesterol oxidase and cholesterol ester hydrolase. The enzymes were immobilized on controlled pore galas(CPG) by the glutaraldehyde method. The glass colunms packed with immobilized enzymes were found to contain 3-5 I.U. for each enzyme. A hydrogen peroxide sensitive electrode was contructed and applied to the FIA system. The operational conditions for FIA response were investigated and optimized with variation of sampling volume, flow rate and composition of carrier solution. The FIA response were linear upto 60 and 400mg/m1 for free cholesterol and cholesterol ester, respectively. All samples were analyzed with a good precision (<2.5% CV) and accuracy. 23 samples were mea sured succesively within about an hour. Intermittent assays of more than 500 times caused 50% decrease in response sensitivity.

• Journal of the Korean Ceramic Society
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• v.42 no.8 s.279
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• pp.554-560
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• 2005

The engineering ceramic needs the properties of high strength, hardness, corrosion-resistance and heat-resistance in order to withstand thermal shock or applied nonuniform stresses without failure. The densely coated porous ceramics can be used for machine component, electromagnetic component, bio-system component and energy-system component by their high-performances from superior coating properties and light-weight characteristics due to the structure including pore by itself. In this study we controlled the porosity of silica and alumina, $8.2\~25.4\%$ and $23.4\~36.0\%$, respectively, by the control of sintering temperature and starting powder size. We made bilayer structures, consisting of a transparent glass coating layer bonded to a thick substrate of different porous ceramics by a thin layer of epoxy adhesive, facilitated observations of crack initiation and propagation. The elastic modulus mismatch could be controlled using different porous ceramics as the substrate layer. Then we applied 150 N force using WC sphere with a radius of 3.18 mm by Hertzian indentation. As a result, the crack initiation in the coating layer was delayed at lower porosity in the substrate layer, and the damage in the coating layer was relatively smaller at the bilayer structure coated on higher elastic substrate.

• Journal of the Korean Chemical Society
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• v.54 no.6
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• pp.696-700
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• 2010

Yeast is immobilized upon $100{\mu}m$ CPG(controlled pore glass bead) to separate $Sb^{3+}$ and $Sb^{5+}$. Continuous hydride generation is performed after the bio-column. The optimum conditions are 0.8 M nitric acid as an eluent with the flow rate of 1.0 mL $min^{-1}$ and the optimum conditions for the generation of hydride are 2 M HCl, 3% (w/v) $NaBH_4$ with the flow rate of 0.83 mL $min^{-1}$, Ar carrier gas flow rate of 50 mL $min^{-1}$. Two species are separated at 112 and 354 seconds each. The sensitivity is enhanced by 10 times for $200{\mu}L$ of sample and the detection limits are 3.0 ppb and 7.0 ppb for $Sb^{3+}$ and $Sb^{5+}$, respectively. When compared with the standard samples, this method showed accurate results.

• KSBB Journal
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• v.9 no.3
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• pp.239-245
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• 1994

The effects of reaction temperature and the level of hydration(water activity) were studied for gas phase reactions of alcohol oxidase and alcohol dehydrogenase immobilized on DEAE-cellulose and controlled pore glass(CPG). Optimum reaction temperature zone of gas phase reaction was similar to that of aqueous phase reaction. The activity of alcohol oxidase increased dramatically and the stability decreased when the water activity was increased from 0.3 to 0.8. The apparent activation energies of the gas phase reaction decreased approaching the values obtained in the aqueous phase reaction as the water activity increased. In the both cases of alcohol oxidase and alcohol dehydrogenase, the rate constants of the gas phase reaction were lower than those of aqueous phase reaction by two orders of magnitude and these results could be correlated to the vapor-liquid equilibrium data of the substrate, ethanol.