• The Bulletin of The Korean Astronomical Society
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• v.35 no.1
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• pp.39.2-39.2
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• 2010

In this paper, I present the domestic development of near infrared camera systems for the ground telescope and the space satellite. These systems are the first infrared instruments made for astronomical observation in Korea. KASINICS (KASI Near Infrared Camera System) was developed to be installed on the 1.8m telescope of the Bohyunsan Optical Astronomy Observatory (BOAO) in Korea. KASINICS is equipped with a $512{\times}512$ InSb array enable L band observations as well as J, H, and Ks bands. The field-of-view of the array is $3.3'{\times}3.3'$ with a resolution of 0.39"/pixel. It employs an Offner relay optical system providing a cold stop to eliminate thermal background emission from the telescope structures. From the test observation, limiting magnitudes are J=17.6, H=17.5, Ks=16.1 and L(narrow)=10.0 mag at a signal-to-noise ratio of 10 in an integration time of 100 s. MIRIS (Multi-purpose InfraRed Imaging System) is the main payload of the STSAT-3 in Korea. MIRIS Space Observation Camera (SOC) covers the observation wavelength from $0.9{\mu}m$ to $2.0{\mu}m$ with a wide field of view $3.67^{\circ}{\times}3.67^{\circ}$. The PICNIC HgCdTe detector in a cold box is cooled down below 100K by a micro Stirling cooler of which cooling capacity is 220mW at 77K. MIRIS SOC adopts passive cooling technique to chill the telescope below 200K by pointing to the deep space (3K). The cooling mechanism employs a radiator, a Winston cone baffle, a thermal shield, MLI of 30 layers, and GFRP pipe support in the system. Opto-mechanical analysis was made in order to estimate and compensate possible stresses from the thermal contraction of mounting parts at cryogenic temperatures. Finite Element Analysis (FEA) of mechanical structure was also conducted to ensure safety and stability in launching environments and in orbit. MIRIS SOC will mainly perform the Galactic plane survey with narrow band filters (Pa $\alpha$ and Pa $\alpha$ continuum) and CIB (Cosmic Infrared Background) observation with wide band filters (I and H) driven by a cryogenic stepping motor.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.11
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• pp.1509-1517
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• 2004

A study was conducted to determine the safety of feeding processed broiler litter (BL) to beef cattle. The litter was processed by deepstacking, ensiling and composting. The health issues addressed relevant to the safety of feeding litter included pathogenic bacteria, mycotoxins, heavy metals, medicinal drugs and pesticide residues. Exp. 1 evaluated the feed hygiene of processed rice hulls-bedded BL. The presence of pathogenic bacteria in BL was determined before and after deepstacking. A total of 21 BL samples were collected over a 3-year period of commercial and experimental production of BL for beef cattle. Exp. 2 evaluated the safety of meat of cattle fed deepstacked BL. In Exp. 1, there were no pathogenic bacteria, such as coliform, E. coli, E. coli O157:H7, Salmonella, Listeria and Proteus, in deepstacked BL. Levels of heavy metals (Cu, Fe, Mn and Zn) and toxic heavy metals (As, Pb, Cd and Hg) were lower than the commercial feed tolerances. Aflatoxin, medicinal drug and pesticide residues were detected at extremely low levels. In Exp. 2, the meat of the BL-fed animals exhibited few differences in all analyzed items from that of the control group, showing safety from pathogenic microorganisms and heavy metals. When BL was withdrawn for 14 days prior to slaughtering the BLfed cattle, no medicinal drug residues were detected in the meat. Pesticides in the tissues of either group of animals were much lower than the tolerances. In conclusion, processed rice hulls-bedded BL and the meat of cattle fed BL were safe from the potential hazards of pathogenic bacteria, heavy metals, aflatoxin, medicinal drugs and pesticide residues.

• Journal of Microbiology and Biotechnology
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• v.14 no.1
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• pp.97-104
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• 2004

Water-sludge bacteria were screened to find a lipase enantioselectively hydrolyzing itraconazole precursor, which is well known as the starting material of antifungal drug agents. A bacterial strain was isolated and identified as Acinetobacter junii SY-01. After the strain was cultivated, the enzyme was purified 39.4-fold using ultrafiltration and gel filtration through a Sephadex G-100 chromatographic column and the activity yield was 34.9%. The molecular weight of the enzyme was about 40 kDa, as measured by SDS-PAGE, and the optimum pH was 7.0- 9.0 and stable at pH 6.0- 9.0. The optimum temperature was 45- $5^{\circ}C$, and 73% of the enzymes activity remained after incubation at 70% for 1 h. Enzyme activity was enhanced by gall powder, sodium deoxycholate, a cationic detergent Tween 80, and a non-ionic detergent Triton X-100, but was markedly inhibited by metal ions such as $Hg^{2＋},Cu^{2＋},Ni^{2＋}/,Ca^{2＋}$, and an anionic-surfactant sodium dodecylsulfate. The $K_{m}$ values for (R)- and (S)-enantiomers of the itraconazole precursor were 0.385 and 21.83 mM, respectively, and the $V_{max} values ($\mu$Mㆍmin^{-1}.)$ were 6.73 and 6.49, respectively. The acetyl group among the different acyl moieties of itraconazole precursor showed the highest enantioselectivity for the hydrolysis by the Acinetobacter junii SY-01 lipase, and the lipase from Acinetobacter junii SY-01 displayed better enantioselectivity than that of commercially available lipases and esterases.

• Journal of Microbiology and Biotechnology
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• v.17 no.4
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• pp.604-610
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• 2007

A psychrotrophic strain 7195 showing extracellular lipolytic activity towards tributyrin was isolated from deep-sea sediment of Prydz Bay and identified as a Psychrobacter species. By screening a genomic DNA library of Psychrobacter sp. 7195, an open reading frame of 954 bp coding for a lipase gene, lipA1, was identified, cloned, and sequenced. The deduced LipA1 consisted of 317 amino acids with a molecular mass of 35,210 kDa. It had one consensus motif, G-N-S-M-G (GXSXG), containing the putative active-site serine, which was conserved in other cold-adapted lipolytic enzymes. The recombinant LipA1 was purified by column chromatography with DEAE Sepharose CL-4B, and Sephadex G-75, and preparative polyacrylamide gel electrophoresis, in sequence. The purified enzyme showed highest activity at $30^{\circ}C$, and was unstable at temperatures higher than $30^{\circ}C$, indicating that it was a typical cold-adapted enzyme. The optimal pH for activity was 9.0, and the enzyme was stable between pH 7.0-10.0 after 24h incubation at $4^{\circ}C$. The addition of $Ca^{2+}\;and\;Mg^{2+}$ enhanced the enzyme activity of LipA1, whereas the $Cd^{2+},\;Zn^{2+},\;CO^{2+},\;Fe^{3+},\;Hg^{2+},\;Fe^{2+},\;Rb^{2+}$, and EDTA strongly inhibited the activity. The LipA1 was activated by various detergents, such as Triton X-100, Tween 80, Tween 40, Span 60, Span 40, CHAPS, and SDS, and showed better resistance towards them. Substrate specificity analysis showed that there was a preference for trimyristin and p-nitrophenyl myristate $(C_{14}\;acyl\; groups)$.

• Microbiology and Biotechnology Letters
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• v.22 no.5
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• pp.507-514
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• 1994

Acetyl xylan esterase was produced by E. coli HB101 harboring a recombinant plasmid pKMG6 which contained the estI gene of Bacillus stearothermophilus. The maximum production was observed when the E. coli strain was grown at 37$\circC for 12 hours in the medium containing 0.5% acetyl xylan, 1.0% tryptons, 1.0% sodium chloride, and 0.5% yeast extract. The esterase produced was purified to homogeneity using a combination of ammonium sulfate fractionation, DEAE Sepharose CL-6B ion exchange chromatography and Sephacryl S-200 gel filtration. The native enzyme had an apparent molecular mass of 60 kd and was composed of two identical subunits of 29 kd. The N-terminal amino acid sequence of the polypeptide was Ala-X-Leu-Gln- Ile-Gln-Phe-X-X-Gln. The acetyl esterase displayed a pH optimum of 6.5 and a temperature opti- mum of 45$\circC. The heavy metal ions such as Ag$^{++}$, Hg$^{++}$ and Cu$^{++}$ inhibited nearly completely the activity of the esterase, and no specific metal ion was found to be required for the enzyme activity. The enzyme readily cleaved MAS, $\beta$-D-glucose pentaacetate, $\alpha$-naphthyl acetate, $\rho$-nitrophenyl acetate as well as acetyl xylan, but had no activity on $\rho$-nitrophenyl propionate, $\beta$-nitrophenyl butyrate or $\beta$-nitrophenyl valerate. The Km and Vmax values for MAS were 2.87 mM and 11.55 $\mu$mole/min, respectively. Synergistic behavior was demonstrated with a combination of xylanase and esterase from B. stearothermophilus in hydrolyzing acetyl xylan.

• Fisheries and Aquatic Sciences
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• v.16 no.4
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• pp.311-318
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• 2013

The gene encoding an esterase from Photobacterium sp. MA1-3 was cloned in Escherichia coli using the shotgun method. The amino acid sequence deduced from the nucleotide sequence (948 bp) corresponded to a protein of 315 amino acid residues with a molecular weight of 35 kDa and a pI of 6.06. The deduced protein showed 74% and 68% amino acid sequence identities with the putative esterases from Photobacterium profundum SS9 and Photobacterium damselae, respectively. Absence of a signal peptide indicated that it was a cell-bound protein. Sequence analysis showed that the protein contained the signature G-X-S-X-G included in most serine-esterases and lipases. The MA1-3 esterase was produced in both soluble and insoluble forms when E. coli cells harboring the gene were cultured at $18^{\circ}C$. The enzyme was a serine-esterase and was active against $C_2$, $C_4$, $C_8$ and $C_{10}$ p-nitrophenyl esters. The optimum pH and temperature for enzyme activity were pH 8.0 and $30^{\circ}C$, respectively. Relative activity remained up to 45% even at $5^{\circ}C$ with an activation energy of 7.69 kcal/mol, which indicated that it was a cold-adapted enzyme. Enzyme activity was inhibited by $Cd^{2+}$, $Cu^{2+}$, $Zn^{2+}$, and $Hg^{2+}$ ions.

• Journal of Food Hygiene and Safety
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• v.3 no.2
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• pp.53-58
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• 1988

This study was carried out to discuss a colorimetric method for the determination of nitrite in meat products issued by the Ministry of Health and Social Affaires of Korea (1985). 1) The recovery rates of nitrite of test solution extracted in the room temperature were higher than those obtained by the heating extraction. 2) In the room temperature, samples prepared with the sUce were more effective than the blendina method and the distlled water as extractina solvent for nitrite was more effective tban tbe phospbate buffer solution. 3) The extracting time showed that thirty minutes were enough to extract nitrite and the diazotizingcoupling reagents, 30% of sulfanilamide and N-l-naphthylethyienediamine were better than others. 4) The nitrite in a test soiution greatly decreased when the solution was distilled. In this case, the test solution should be used as a control. 5) Ten minutes were enough to couple nitrite.

• Restorative Dentistry and Endodontics
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• v.18 no.2
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• pp.431-445
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• 1993

The purpose of this study was to observe corrosion characteristics of six dental amalgams and was to analyse corrosion products electrochemically. After each amalgam alloy and Hg was triturated as the direction of the manufacturer by using mechanical amalgamator, the triturated mass was inserted into the cylinderical metal mold ($12{\times}10mm$) and was condensed with 160kg/$cm^2$ by using the hydrolic press. The specimen was removed from the mold and was stored at room temperature for 1 week, and was polished with amalgam polishing kit. The anodic and cathodic polarization curve was obtained by using cyclic voltammetric method with 3-electrode potentiostat in saline for each amalgam and Ag, Sn, Cu plate specimen at $37{\pm}0.5^{\circ}C$. The potential sweep range was -1.7V~0. 4V(vs SCE) in working electrode and scan rate was 50mV/s and the exposed surface area of each specimen to the electrolytic solution was $0.79cm^2$. The results were as follows. 1. In anodic-cathodic polarization curve of amalgam specimens, two anodic current rising areas and two cathodic current peaks were obtained at the low Cu amalgam(CF, CS) specimen and three anodic current rising areas and three cathodic current peaks were obtained at the high Cu amalgam (TY, DS, HV) specimen. 2. As this compared with the anodic and cathodic current peak potentials of Sn, Cu and Ag specimen, the first cathodic current peak I c was caused by the reduction of divalent tin salt, second cathodic current peak IIIc results from the reduction of quadravalent tin salt, and third cathodic current peak me results from the reduction of copper salt. 3. As reverse potential sweeping was done repeatedly, anodic current was decreased slightly in all amalgam specimens.

• Textile Coloration and Finishing
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• v.18 no.6 s.91
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• pp.16-24
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• 2006

The purpose of this study is to improve the defects of chitosan crosslinked viscose rayon by ECH and to describe the change of hand of chitosan crosslinked viscose rayon fabrics. The chitosan crosslinked viscose rayon were manufactured by crosslinking process using ECH as crosslinking agent, 2 wt% aqueous acetic acid as a solvent of chitosan and ECH, and 20 wt% aqueous sodium hydroxide as crosslinking catalyst. Viscose rayon were first immersed in the pad bath of the mixed solution of chitosan and ECH, padded up to 100 wt% wet pick-up on weight of fiber(owf), precured on pin frames at $130^{\circ}C$ for 2 minutes, immersed in NaOH solution and finally wash and dry. Antimicrobial properties of the viscose rayon treated with chitosan were measured by the shake flask C.T.M. 0923 test method with staphylococcus aureus(ATCC 6538) as the microorganism. When the concentration of chitosan was increased chitosan crosslinked viscose rayon's LT, WT, B, 2HB and MIU were increased and G, 2HG, SMD, T and $T_m$ were decreased. On the other hand, WT, EM were decreased and RT was increased at $1{\times}10^{-2}M$ ECH. The optimum condition for crosslinking was that ECH concentration was between $1{\times}10^{-2}M\;and\;5{\times}10^{-2}M$. Antimicrobial effects of rayon fabric treated with chitosan was excellent.

• The Journal of Korean Institute of Communications and Information Sciences
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• v.27 no.7B
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• pp.719-726
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• 2002

In WRC-2000, Resolution 734 was adopted to study the use of high altitude platform station(HAPS) operating in the bands above 30GHz. Therefore, frequency sharing feasibility between a new HAPS systems and an existing terrestrial fixed-service(FS) system should be analyzed primarily. In this paper, interference effects from the HAPS system into the radio-relay station are analyzed in terms of two cases; one is the interference distribution from the power-flux density(PFD) of HAPS airships, and the other the interference power from the ground stations. In conclusion, the new PFD criteria different from the exiting satellite system should be required, and the coordinated distance between the HAPS nadir and the radio-relay station should be 60km ∼ 253km for P$\sub$HG/ = -50dBW/MHz of transmitting power spectral density to share the new HAPS system into the existing FS system.