• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.33 no.5
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• pp.405-410
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• 2020

In this study, the following results were obtained by analysis of electric properties with FT-IR, DSC, XRD, and SEM, in the range of temperature 30~160℃ and frequency 0.1~200 kHz, when filling agent (0~100 phr) and silicone oil (0~12 phr) were added to raw silicone rubber. In the case of 100 phr mixed samples, the relative dielectric constant εr gradually decreased from 4.3 to 3.96 as frequency increased, and the dielectric loss tan δ decreased to 0.01 at 300 Hz, then increased to 0.022 at 30 kHz, then decreased to 200 kHz. The FT-IR analysis identified the same binding structure according to the chemical composition of added silica (SiO₂). Through DSC analysis, we could determine the change of heat quantity and the glass transition temperature of each specimen. In the XRD analysis, it was found that the images SiO₂, TiO₂, and Fe₂O₃ appeared for specimens with 0%, 50% and 100% filling agent. Finally, the SEM analysis confirmed that particles of 0.5 to 1.5 ㎛ size with silica (SiO₂) mixing were dispersed evenly.

• Korean Journal of Materials Research
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• v.13 no.5
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• pp.338-342
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• 2003

Adhesion between Cu and low-k films has been investigated. Low-k films deposited using a mixture of hexamethyldisilane(HMDS) and Para-xylene had a dielectric constant as low as 2.7, showing the thermally stable properties up to $400^{\circ}C$. In this study, Ti glue layer, boron dopant, and $N_2$plasma treatment were used to improve adhesion property of between Cu and low-k films. Ti glue layer slightly improved adhesion property. After $N_2$plasma treatment, the adhesion property was significantly improved due to the increased roughness and the formation of new binding states between Ti and plasma-treated PPpX : HMDS. However, $300^{\circ}C$ annealing of $N_2$plasma treated sample caused the diffusion of Cu into the PPpX : HMDS, degrading the low-k properties. In the case of Cu(B)/Ti/PPpX : HMDS, the adhesion was remarkably increased. This enhanced adhesion was attributed to formation of Ti-boride at the Cu-Ti interface. It is because the formed Ti-boride prevented the diffusion of Cu into the PPpX : HMDS and the Cu-Ti reaction at the Ti interface.

• Korean Journal of Food Science and Technology
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• v.25 no.6
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• pp.608-613
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• 1993

Production of cyclodextrin (CD) by cyclodextrin glycosyltransferase (CGTase) isolated from alkalophilic Bacillus sp. was carried out to determine optimal reaction conditions. The maximum initial rate of CD production from amylose was obtained at dextrose equivalent 10.5. The CD production yield showed inverse proportionality to DE values over the range from 0.5 to 37.7. Even though the deactivation constant of CGTase at $60^{\circ}C$ was higher than those at lower temperatures, the production rate and yield at $60^{\circ}C$ were still higher. These results suggest thermal stabilization of CGTase by binding with starch.

• Bulletin of the Korean Chemical Society
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• v.26 no.2
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• pp.260-264
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• 2005

The nature of the active site of Tobacco acetohydroxyacid synthase (AHAS) in the substrate- and cofactorbinding was studied by kinetics and fluorescence spectroscopy. The substrate saturation curve does not follow Michaelis-Menten kinetics at different temperatures (7, 21 and 37 ${^{\circ}C}$), pH (6.5, 7.5 and 8.5) and buffers (Tris-HCl and MOPS). The concentration of one half of the maximum velocity ($S_{0.5}$) decreased in the following order: pyruvate $\gt$ ThDP $\approx$$Mg^{+2}$ $\gt$ FAD. However, the catalytic efficiency (K$_{cat}/S_{0.5}$) inversely decreased in the following order; FAD $\gt$ $Mg^{+2}$ $\approx$ThDP $\gt$ pyruvate, indicating that the cofactors by in decreasing order; FAD, $Mg^{+2}$, ThDP, affect the catalysis of AHAS. The dissociation constant ($K_d$) of the intrinsic tryptophan fluorescence decreased with the same tendency of the concentration of one half of the maximum velocity ($S_{0.5}$) decreasing order. This data provides evidence that the substrate and cofactor binding natures of the active site, as well as its activation characteristics, resemble those of other ThDP-dependent enzymes.

• 한국생물공학회:학술대회논문집
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• 2002.04a
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• pp.201-204
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• 2002

The gellan was extracellular polysaccharide produced by Pseudomonas elodea A TCC 31461 at aerobic condition. Gellan provides various functionalities such as gelling, suspending, stabilizing, emulsifying and binding properties in aqueous systems. In this study, the effect of pH on the cell growth and the gellan production were evaluated in shake- flasks and in 5 ${\ell}$ batch fermentor. In the shake-flasks culture, maximum gellan production was obtained with 1.66g/ ${\ell}$ when initial pH was 7.0. The batch fermentation was performed in the medium pH control ranged pH 5.5-8.5. The maximum gellan production of 1.97g/l was obtained with constant pH 6.0.

• Microbiology and Biotechnology Letters
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• v.22 no.6
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• pp.636-642
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• 1994

Essential amino acids involving in the catalytic mechanism of the $\beta$-D-xylosidase of Bacillus stearothermophilus were determined by chemical modification studies. Among various che- mical modifiers tested N-bromosuccinimide (NBS), $\rho$-hydroxymercurybenzoate (PHMB), N-ethylma- leimide, 1-[3-(di-ethylamino)-propyl]$-3-ethylcarbodi-imide (EDC), and Woodward's Reagent K(WRK)inactivated the enzyme, resulting in the residual activity of less than 20%. WRK reduced the enzyme activity by modifying carboxylic amino acids, and the inactivation reacion proceeded in the form of pseudo-first-order kinetics. The double-lagarithmic plot of the observed pseudo-first- order rate constant against the modifier concentration yielded a reaction order of 2, indicating that two carboxylic amino acids were essential for the enzyme activity. The $\beta$-D-xylosidase was also inactivated by N-ethylmaleimide which specifically modified a cysteine residue with a reaction order of 1, implying that one cysteine residue was important for the enzyme activity. Xylobiose protected the enzyme against inactivation by WRK and N-ethylmaleimide, revealing that carboxylic amino acids and a cysteine residue were present at the substrate-binding site of the enzyme molecule.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1995.04a
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• pp.75-75
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• 1995

Succinic semialdehyde reductase, one of key enzyme of GABA shunt in CNS, is inactivated by o-phthalaldehyde, The inactivation followed pseudo first-order kinetics, and the second-order rate constant for the inactivation process was 28 M$\^$-1/s$\^$-1/ at pH 7.4 and 25$^{\circ}C$. The absorption spectrum(λ$\_$max/=377nm), fluorescence exitation(λ$\_$max/=340nm) and fluorescence emission spectra (λ$\_$max/=409nm) were consistent with the formation of an isoindole derivative in the catalytic site between a cysteine and a lysine residues about 3${\AA}$ apart. The substrate, succinic semialdehyde, did not protect the enzymatic activity against inactivation, whereas the coenzyme, NADPH, protected against o-phthalaldehyde induced inactivation of the enzyme. About 1 isoindole group per moi of the enzyme was formed following complete loss of the enzymatic activity. These results suggest that the amino acid residues of the enzyme participating in reaction with o-phthalaldehyde more likely residues at or near the coenzyme binding site.

• Analytical Science and Technology
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• v.8 no.4
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• pp.793-798
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• 1995

A new chromoionophore sym-(decyl)(2-hydroxy-5-nitrobenzyloxy)-dibenzo-16-crown-5 (1) has been synthesized for $Na^+$ photometry in aqueous media. Apparent $pK_a$ values of 1 in the presence of 0.10 M LiCl, NaCl, and KCl were measured by spectrophotometry in 50% 1,4-dioxane-50% water (v/v) and compared with the $pK_a$ of 8.68 in the presence of 0.10 M TMACl. A significant $pK_a$ shift to a lower pH was only observed for $Na^+$ (${\Delta}pH=1.31$) due to selective binding of 1 with $Na^+$. Based upon this $pK_a$ shift, chromoionophore 1 was found to selectively respond to $Na^+$ with a detection limit of $10^{-3}M$ and no interference from $K^+$ up to 0.05 M for detection of 10.0 mM $Na^+$ in 50% 1,4-dioxane-50% water (v/v).

• Analytical Science and Technology
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• v.8 no.4
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• pp.591-596
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• 1995

Enzyme multilayers composed of avidin and biotin-labeled enzymes were prepared on the surface of electrode, through a strong affinity between avidin and biotin (binding constant: ca $10^{15} M^{-1}$). The enzyme multilayers were useful for the improvement of the performance characteristies of enzyme sensors. The output current of the enzyme sensors depended linearly on the number of enzyme layers deposited. Thus, lactate oxidase (LOx) and alcohol oxidase (AlOx) were deposited after being modified with biotin for constructing enzyme sensors sensitive to L-lactate and ethanol respectively. It was also possible to deposit two different kinds of enzymes successively in a single multilayer. The glucose oxidase (GOx) and ascorbate oxidase (AsOx) were built into a multilayer structure on a Platinum electrode. The GOx, AsOx multilayer-modified electrode was useful for the elimination of ascorbic acid interference of the glucose sensor.

• Applied Biological Chemistry
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• v.37 no.3
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• pp.189-193
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• 1994

The hydrolysis of fungicidal N-[1-(benzotriazol-1-yl)benzyl]aniline (BBA) molecule in the presence of cationic cetyltrimethylammonium bromide (CTABr) and anionic sodium laurylsulfate (NaLs) micellar solutions has been studied kinetically. The Micellar catalysis effect shows that the rate is slightly accelerated by the addition of the anionic NaLs at high pH and the binding constant (Ks) is $1.45{\times}10^4M^{-1}$. This result presumably is due to the electrostatic stabilization by the anionic micelle of the developing carbocation in the transition state rather than the hydrophobic character (${\pi}$: 4.93) of (BBA).