• Journal of the Optical Society of Korea
• /
• v.19 no.5
• /
• pp.508-513
• /
• 2015

A capacitive-type touch screen panel (TSP) composed of silver nanowire (AgNW) crossing electrodes and transparent bridge structures was fabricated on a polycarbonate film. The transparent bridge structure was formed with a stack of Al-doped ZnO (AZO) electrodes and SU-8 insulator. The stable and robust continuity of the bridge electrode over the bridge insulator was achieved by making the side-wall slope of the bridge insulator low and depositing the conformal AZO film with atomic layer deposition. With an extended exposure time of photolithography, the lower part of the SU-8 layer around the region uncovered by the photomask can be exposed enough to the UV light scattered from the substrate. This leads to the low side-wall slope of the bridge insulator. The fabricated TSP sample showed a large capacitance change of 22.71% between with and without touching. Our work supplies the technological clue for ensuring long-term reliability to the highly flexible and transparent TSP made by using conventional fabrication processes.

• Journal of the Korean institute of surface engineering
• /
• v.47 no.2
• /
• pp.81-85
• /
• 2014

Ga doped ZnO (GZO)/Al bi-layered films were deposited on the glass substrate by RF and DC magnetron sputtering and then vacuum annealed at different temperatures of 100, 200 and $300^{\circ}C$ for 30 minutes to consider the effects of annealing temperature on the structural, electrical and optical properties of the films. For all depositions, the thicknesses of the GZO and Al films were kept constant at 95 and 5 nm, respectively, by controlling the deposition time. As-deposited GZO/Al bi-layered films showed a relatively low optical transmittance of 62%, while the films annealed at $300^{\circ}C$ showed a higher transmittance of 81%, compared to the other films. In addition, the electrical resistivity of the films was influenced by annealing temperature and the lowest resistivity of $9.8{\times}10^{-4}{\Omega}cm$ was observed in the films annealed at $300^{\circ}C$. Due to the increased carrier mobility, 2.35 $cm^2V^{-1}S^{-1}$ of the films. From the experimental results, it can be concluded that increasing the annealing temperature enhanced the optical and electrical properties of the GZO/Al films.

• KSBB Journal
• /
• v.17 no.6
• /
• pp.571-576
• /
• 2002

Recombinant E. coli DH5 ${\alpha}$/pSB311 was made by cloning the genes encoding bacterial luciferase and aldehyde substrate proteins from Photohabdus luminescense, to complement defects of Lumistox, which is normally used in bioassays to monitor toxic substances in water environmental systems. The conditions for stable light production by the recombinant strains were investigated with respect to cell growth stage, cell number, and buffer conditions. The optimum growth stage was a middle-exponential stage with an OD$_{660nm}$ value of 0.6-0.7. ADout 10$^{6}$-10$^{7}$ cells per test tube was optimum for stable light emission. The effect of buffer was not significant if an optimum viable cell number was maintained. The bioluminescence of the recombinant E. coli harboring the lux operon of Photohabdus luminescense was not affected by temperature, while the bioluminescence of Lumistox was temperature sensitive. The recombinant E. coli was more sensitive to heavy metals (Cd, Cu, Hg, Zn) than Lumistox, because it does not require high concentrations of NaCl in the buffer.

• Microbiology and Biotechnology Letters
• /
• v.41 no.2
• /
• pp.145-152
• /
• 2013

The culture conditions to maximize the production of endoglucanase (EC 3.2.1.4) from the brown rot fungus Fomitopsis pinicola MKACC 54347 mycelia were investigated. Among the tested media for endoglucanase production, Mandel's mineral salts medium (MSM; 1% cellulose, 0.1% peptone, 0.14% $(NH_4)_2SO_4$, 0.03% urea, 0.2% $KH_2PO_4$, 0.03% $MgSO_4{\cdot}7H_2O$, 0.03% $CaCl_2$, and 0.1% trace metal solution (19.8 mM $FeSO_4$, 13.0 mM $MnSO_4$, 12.2 mM $ZnSO_4$, and 15.4 mM $CoCl_2$)) produced the highest activity of the enzyme. To optimize the medium composition for enzyme activity, the effects of various carbon, nitrogen, phosphorus, and inorganic sources were investigated in MSM. Maximal enzyme production was accomplished using a medium containing 2% carboxymethyl cellulose (CMC), 2% yeast extract, 0.2% $KH_2PO_4$, 0.03% $MnSO_4$, and 0.3% trace metal solution. Different physiological conditions, like incubation period and temperature, were also examined to assess their influence on enzyme production. Enzyme production from F. pinicola reached its highest level after cultivation for 8 days at $25^{\circ}C$. Nondenaturing polyacrylamide gel electrophoresis (PAGE), followed by the endoglucanase activity staining using CMC as the substrate, was performed to identify the endoglucanase under the culture conditions studied. Zymogram analysis of the culture supernatant revealed an endoglucanase band with a molecular mass of 52 kDa. The optimum pH and temperature for enzyme activity were $55^{\circ}C$ and pH 5.0, respectively.

• Microbiology and Biotechnology Letters
• /
• v.15 no.2
• /
• pp.129-134
• /
• 1987

Aspergillus sp. (MK-24) producing a biological active substance that inhibited the venom proteinase activity was isolated from soil. The substance also inhibited the activity of trypsin and coagulation of blood, but did not inhibit papain, $\alpha$-chymotrypsin and pepsin. The substance was partially purified from culture filtrate by precipitaion with acetone, and by chromatography of DEAE-Sepadex A-50 column and Amberlite IRC-50 ion exchange. The inhibitory substance was stable in the wide pH range from 2.0 to 12.0 at 37$^{\circ}C$, but not stable at $65^{\circ}C$ in the alkaline pH. Only 12% of the activity was decreased by the heat treatment at 10$0^{\circ}C$ for two hours. The inhibition on venom proteinase (Agkistrodon bromohoffi brevicaudus) was a mixed type. The inhibitory activity depended on the preincubation time and completely depressed by cupric, zinc and cobalt ions. The inhibition on the venom proteinase was appeared strongly on casein but not on ovalbumin or hemoglobin as a substrate.