• Journal of Life Science
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• v.11 no.5
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• pp.457-463
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• 2001

A bacterial strain SC-22 which produced alkaline lipase was isolated from salf-fermented shrimps. Strains SC-22 was identified as Staphylococcus xylosus. An alkaline lipase excreted by Staphylococcus xylosus SC-22 was purified by ammonium sulfate predipitation and column chromatography on Sephadex G-100 and DEAE-Sephace. The specific activity of purified lipase was 756U/mg of protein with 17.2% yield. The approximate molecular weight of the purified enzyme was 47 kDa. The partially purified lipase preparation had and optimum temperature of 4$0^{\circ}C$, an optimum pH of 8.0, and a stable of 5~10. Lipase activities were enhanced by salt ions such as $Ca^{2+}$, $Mg^{2+}$,N $a^{2+}$ while inhibited remarkably by heavy metal ions, C $u^{2+}$ and P $b^{2+}$.EX> 2+/.

• Bulletin of the Korean Chemical Society
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• v.15 no.12
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• pp.1108-1112
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• 1994

25-Acetoxy-26,27,28-trimethoxycalix[4]arene was synthesized by the treatment of calix[4]arene trimethyl ether with acetyl chloride in the presence of NaH. The solution conformation was inferred as a partial cone conformation based on the $^1H$-and $^{13}C$ NMR spectra. The crystal structure has been determined by X-ray diffraction method. The crystals are monoclinic, space group $P2_1$/n, a=8.186 (1), b=17.137 (2), c=19.878 (3) ${\AA}$, ${\beta}$=95.67 (1)$^{\circ}$, Z=4, V=2774.90 ${\AA}^3$, $D_c$= 1.22 g $cm^{-3}$, $D_m$=1.23 g $cm^{-3}$. The intensity data were collected on an Enraf-Noninus CAD-4 Diffractometer with a graphite monochromated $Cu-K{\alpha}$ radiation. The structure was solved by direct method and refined by full-matrix least-squares methods to a final R value of 0.054 for 3675 observed reflections. The molecule possesses a partial cone conformation with one flattened phenyl unit, in which one anisol ring, distal to the ester ring, is inverted. The acetoxyphenyl ring is flattened.

• Journal of the Korean Ceramic Society
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• v.37 no.7
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• pp.700-704
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• 2000

Titanium hydroxide precipitate was obtained by the reaction of 0.5M TiOCl2 and 5M NH4OH solutions, then anatase TiO2 powder with nanotubes was prepared by the digestion of the heat-treated powder in 5M NaOH solution. Nanotube was formed for anatase TiO2 powder digested at 10$0^{\circ}C$ above, and the amount and length of nanotube increased with the digestion temperature. In the case of the powder digested at 15$0^{\circ}C$ for 12h, the formed nanotube was 100~150nm in length, 10~20 nm in diameter, and 2nm in width of the walls on both sides of the nanotube. The powder digested at 15$0^{\circ}C$ for 12h showed the highest specific surface area of 270$m^2$/g.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2001.02a
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• pp.14-28
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• 2001

As basic study for purpose bioremedation in oil-contaminated environment, Primarily, we isolated biosurfactant producer- strains utilized of oil-agar plate, and measured surface tension and emulsifying activity. We investigated in oil-contaminated soil and sea water. In this laboratory, Pseudomonas sp. EL-012S strain isolated from oil-contaminated soil was able to product novel biosurfactant under the optimal culture condition. Its condition was n-hexadecane 2.0%, NH$_4$NO$_3$0.4%, Na$_2$HPO$_4$0.6%, KH$_2$PO$_4$0.4%, MgSO$_4$.7$H_2O$ 0.02%, CaCl$_2$.2$H_2O$ 0.001%, FeSO.7$H_2O$ 0.001%, initial pH 7.0 and aeration at 3$0^{\circ}C$, respectively. This biosurfactant was produced in both late-exponential and early-stationary phase. The biosurfactant from Pseudomonas sp. EL-012S was composed of carbohydrate, lipid and protein. The purified-biosurfactant was examined two (biosurfactant type I, II) with the silica gel G60 column chromatography and the purified biosurfactant confirmed thin layer chromatography, high performed liquid chromatography and gas chromatography. The biosurfactant type I involved in carbohydrate-lipid-protein characteristics lowered surface tension of water to 27dyne/cm and interfacial tension 4.5dyne/cm aginst to n-hexadecane and the biosurfactant type B involved in carbohydrate lipid characteristics lowered surface tension of water to 30dyne/cm and interfacial tension 8dyne/cm against to n-hexadecane. Specially type I had the properties such as strong emulsifying activity, emulsion stability, pH-stability, thermo-stability, high cleaning activity and forming ability.

• Nuclear Engineering and Technology
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• v.18 no.2
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• pp.92-96
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• 1986

The $^{93}Nb(n,n\alpha)^{89m}Y$, $^{93}Nb(n,{\alpha})^{90m}Y$ and $^{93}Nb(n,2n)^{92m}Nb$ cross sections at a neutron energy of 14.6 MeV have been measured relative to the $^{27}Al(n,p)^{27}Mg$ and $^{27}Al(n,{\alpha})^{24}Na$ cross sections. A small accelerator utilizing $T(D,n)^4He$ reaction was used as a neutron source and the neutron energy spread is about 0.4MeV at the sample. All induced activities were measured with a 70cc HPGe detector in the same geometry.

• International Journal of Industrial Entomology and Biomaterials
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• v.23 no.1
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• pp.147-153
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• 2011

The Pseudorabies (PR), also called Aujeszky's disease (AD), is an infectious viral disease caused by an alpha herpes virus and has domestic and wild pigs, as well as a wide range of domestic and wild animals, as the natural host. Pseudorabies virus (PRV) virions contain several envelope glycoproteins. Among them, gB, gC and gD are regarded as the major immunogenic proteins. We expressed these glycoproteins using the bacterial expression system and analyzed recombinant proteins. Expression of glycoproteins gC and gD were observed on SDS-PAGE or Western blot analysis, but gB was not. Optimal concentration of IPTG and inducing time were determined as 1.0 mM and 4 h, respectively, for the expression of both gC and gD in E. coli. A sodium dodecyl sulfate (SDS) was the most efficient detergent in solubilizing insoluble recombinant protein.

• Microbiology and Biotechnology Letters
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• v.23 no.4
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• pp.454-460
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• 1995

Acetylxylan esterase II was produced by Escherichia coli HB101 harboring the recombinant plasmid pKMG7 which contained the estII gene of Bacillus stearothermophilus. Optimal medium for the production of the acetylxylan esterase by E. coli HB101/pKMG7 was determined to contain 0.5% galactose, 1% yeast extract and 1% NaCl. The enzyme produced was purified to homogeneity using a combination of 20-50% ammonium sulfate precipitation, DEAE-Sepharose CL-6B chromatography and Sephacryl S-200 gel filtration. The temperature and pH optimum of the esterase were 45$\circ$C and pH 6, respectively. The essential amino acids for the esterase activity were found to be methionine, serine, and cysteine. Molecular weight of the esterase was determined to be 28 kDa by SDS-polyacrylamide gel electrophoresis, and 120 kDa by gel filtration. This suggests that the functional enzyme is a homomeric tetramer. The esterase had an isoelectric point of pH 3.4. The N-terminal amino acid sequence of the enzyme was Ala-Leu-Phe-Glu-Ser-Arg-Phe-Phe-Ser-Glu-Val-Leu-Gly-Leu.

• Journal of Microbiology and Biotechnology
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• v.24 no.7
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• pp.969-978
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• 2014

The aprE2 gene with its prosequence from Bacillus subtilis CH3-5 was overexpressed in Escherichia coli BL21(DE3) by using plasmid pET26b(+). After IPTG induction, active and mature AprE2 was produced when cells were grown at $20^{\circ}C$, whereas inactive and insoluble enzyme was produced in a large amount when cells were grown at $37^{\circ}C$. The insoluble fraction was resuspended with 6 M guanidine-HCl and dialyzed against 2 M Tris-HCl (pH 7.0) or 0.5 M sodium acetate (pH 7.0) buffer. Then active AprE2 was regenerated and purified by a Ni-NTA column. Purified AprE2 from the soluble fraction had a specific activity of $1,069.4{\pm}42.4U/mg$ protein, higher than that from the renatured insoluble fraction. However, more active AprE2 was obtained by renaturation of the insoluble fraction. AprE2 was most stable at pH 7 and $40^{\circ}C$, respectively. The fibrinolytic activity of AprE2 was inhibited by PMSF, but not by EDTA and metal ions. AprE2 degraded $A{\alpha}$ and $B{\beta}$ chains of fibrinogen quickly, but not the ${\gamma}$-chain. AprE2 exhibited the highest specificity for N-succinyl-Ala-Ala-Pro-Phe-pNA. The $K_m$ and $k_{cat}/K_m$ of AprE2 was 0.56 mM and $3.10{\times}10^4S^{-1}M^{-1}$, respectively.

• Corrosion Science and Technology
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• v.7 no.3
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• pp.168-172
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• 2008

A new type of electrochemical random signal (electrochemical noise) analysis technique was applied to localized corrosion of anodic oxide film formed 1100 aluminum alloy in $0.5kmol/m^3$ $H_3BO_4/0.05kmol/m^3$ $Na_2B_4O_7$ with $0.01kmol/m^3$ NaCl. The effect of anodic oxide film structure, barrier type, porous type, and composite type on galvanic corrosion resistance was also examined. Before localized corrosion started, incubation period for pitting corrosion, both current and potential slightly change as initial value with time. The incubation period of porous type anodic oxide specimens are longer than that of barrier type anodic oxide specimens. While pitting corrosion, the current and potential were changed with fluctuations and the potential and the current fluctuations show a good correlation. The records of the current and potential were processed by calculating the power spectrum density (PSD) by the Fast Fourier Transform (FFT) method. The potential and current PSD decrease with increasing frequency, and the slopes are steeper than or equal to minus one (-1). This technique allows observation of electrochemical impedance changes during localized corrosion.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.307-311
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• 2005

Marine microorganisms to produce functional biopolymers were isolated from the seashore of the Kyungsang province. Microorganisms to hydrolyze carboxy-methyl cellulose(CMC) were cultured in marin broth and the other liquid medium that contained 2.0% (w/v) glucose, 0.25% yeast extract, 0.5% $K_2HPO_4$, 1% NaCl, 0.02% $MgSO_4{\cdot}7H_2O$ and 0.06% $(NH_4)_2SO_4$ to investigate the ability to produce carboxymethyl cellululase (CMCase) under aerobic conditions. Twelve microorganisms among them showed higher activities of CMCase than B. amyloliquefaciens DL-3, which was known as a cellulase-producing strain. The microorganism showing highest activity of CMCase in this study was identified as Bacillus subtilis subsp. subtilis with 16S rDNA partial sequencing and gyrase A partial sequencing and named as B. subtilis subsp. subtilis A-53.