• Journal of Life Science
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• v.13 no.1
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• pp.90-98
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• 2003

An allium rhizobacterium Serratia plymuthica AL-1 was previously selected as a biocontrol agent of allium white rot. The chitinase from S. plymuthica AL-1 produced in medium containing colloidal chitin was purified by ammonium sulfate precipitation (40~70%), affinity adsorption, column chromatography on DEAE-sephadex A-50 and sephadex C-200 gel filtration. The enzyme was purified 10.8-fold with a yield of 7.3% from the starting culture broth. The purified chtinase gave a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis, it's molecular weight was estimated to be 55 kDa. The optimum pH and temperature of the purified enzyme were pH 5.5 and $55^{\circ}C$, respectively and it is stable up to $50^{\circ}C$ and maintains around 90% of its activity for 60min. The enzyme were activated by $Ca^{2+}$, $Mn^{2+}$ and $Mg^{2+}$ and inhibited by $Cu^{2+}$, SDS, $\rho$-CMB, MIA, respectively. The purified chitinase showed broad spectrum of antifungal activities against plant pathogenic fungi Sclerotium cepivoruin, Alternana alternnta, Colletotrichum glceosporioidrs, Phoma sp., Sclerotinia sclerotiorum, Stemphylium solani, Fusarium oxysporium f. sp. niveum but rarely inhibited Phytophthora capsici and Pythium ultimum.. The purified chitinase from S. plymuthica AL-1 caused swelling, lysis, deceleration and degradation of the hyphal tips of S. sczerotiorum causing allium white rot. It suggest that S. prymuthica AL-1 chitinase play an important part in the bifunctional chitinase / lysozyme activity.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.17 no.12
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• pp.26-33
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• 2016

The cost of preparing munitions in weapon system operation and management has been rapidly increasing and current weapon systems have become complicated and diverse due to new warfare pattern changes and the rapid growth of advanced scientific technology. Moreover, as a part of the execution plans of creative economics, the Korean government is actively reviewing how to minimize the costs of preparing munitions. Accordingly, this study derived the issues of munitions management for decreasing munitions preparing costs. First, the issues of munitions management were introduced through review and analysis with respect to the munitions classification criteria, regulations and systems, and equipment maintenance information systems. Second, we proposed the application and necessity for the real-name system which is responsible for munitions management and the fragmentation of the maintenance instructions status classification criteria.. Also, we were analyzed that the effects depending on the application. Finally, we proposed that the linkage system which is currently military active with equipment maintenance information systems as well as the total life-cycle management system (TLCSM) improvements to the itemized data and records management system by utilizing IT technology CMB that must be done in order to improve the issues.

• Microbiology and Biotechnology Letters
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• v.16 no.4
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• pp.310-315
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• 1988

Two isoenzymes of chorismate mutase(E.C.5.4.99.5) designated as chorismate mutase I(CM I) and chorismate mutase II(CM II), were detected and partially purified from a sp. of intrasporangium isolated from soil. CM I and CM II had pH optima of pH 6.5 and 8.0, respectively and showed the same temperature optimum of 45$^{\circ}C$. The activation energy of the enzymatic reaction was estimated to be 14.7kcal/ mole with CM I and 10.8kcal/mole with CM II. The affinity of isoenzyme CM I for substrate(Km= 1.35mM) was almost the same level as that of CM II(Km = 1.22mM). Both isoenzymes were stable at pH values ranged from pH 6.5 to 9.0, but rapidly denaturated at temperatures above 45$^{\circ}C$. CM II was activated about 7$^{\circ}C$ of its activity by $Ba^{++}$ or $Mg^{++}$ while CM I was slightly inhibited by the same metal ions. Thiol compounds were found not to be necessary for stability of the two enzymes but Co$^{++}$ and EDTA had a little stabilizing effect on CM II only. p-Chloromercuribenzoate strongly inactivated the activities of both enzymes but the reducing agents such as dithiothreitol and L-cysteine protected them against the pCMB inhibition.

• Korean Journal of Microbiology
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• v.25 no.3
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• pp.221-228
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• 1987

The extracellular adenine deaminase from Nocardioides sp. J-275L was purified by the following techniques: ammonium sulfate fractionation, DEAE-Cellulose, DEAE-Sephadex A-50 column chromatography, and Sephacryl S-200 superfine gel filtration. The enzyme was partially purified about 3889.5-fold with about 5.2% yield by these procedures. The molecular weight of the enzyme was 39,000 by a calibrated Sephacryl S-200 superfine column chromatography. The enzyme was stable at pH 7.5 and up to $40^{\circ}C$. Glycerol was effective on the stabilization of the enzyme during storage. The optimum pH and temperature of the enzyme were around pH 7.5 and $40^{\circ}C$, respectively. The apparent Michaelis constant Km of the enzyme for adenine was $7.4\times 10^{-5}$M. The purine analogues, 6-chloropurine, 2,6-diaminopurine, 6-bromopurine, 4-aminopyrazolo [3.4-d]pyrimidine, and 8-azaadenine were substrates for the enzyme. 6-Dimethylaminopurine was a competitive inhibitor of the enzyme. The enzyme was inhibited by 1mM of $Cu^{2+}, Fe^{3+}, Pb^{2+}, Hg^{2+}$, and $Ag^{+}$, and 1mM of $\alpha$,$\alpha$'-dipyridyl, pentachlorophenol, and pCMB.

• The Bulletin of The Korean Astronomical Society
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• v.40 no.1
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• pp.44.1-44.1
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• 2015

We present joint constraints on the number of effective neutrino species $N_{eff}$ and the sum of neutrino masses ${\Sigma}m_{\nu}$, based on a technique which exploits the full information contained in the one-dimensional Lyman-${\alpha}$ forest flux power spectrum, complemented by additional cosmological probes. In particular, we obtain $N_{eff}=2.91{\pm}0.22$ (95% CL) and ${\Sigma}m_{\nu}$ < 0.15 eV (95% CL) when we combine BOSS Lyman-${\alpha}$ forest data with CMB (Planck+ACT+SPT+WMAP polarization) measurements, and $N_{eff}=2.88{\pm}0.20$ (95% CL) and ${Sigma}m_{\nu}$ < 0.14 eV (95% CL) when we further add baryon acoustic oscillations. Our results tend to favor the normal hierarchy scenario for the masses of the active neutrino species, provide strong evidence for the Cosmic Neutrino Background from $N_{eff}{\approx}3$($N_{eff}=0$ is rejected at more than $14{\sigma}$), and rule out the possibility of a sterile neutrino thermalized with active neutrinos (i.e., $N_{eff}=4$) - or more generally any decoupled relativistic relic with $${\Delta}N_{eff}{\sim_=}1$$ - at a significance of over $5{\sigma}$, the strongest bound to date, implying that there is no need for exotic neutrino physics in the concordance ${\Lambda}CDM$ model.

• Journal of Korean Society for Atmospheric Environment
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• v.20 no.1
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• pp.17-31
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• 2004

The subway play an important part in serious traffic problems. However, because subway system is a closed environment, many serious air pollution problems occurred in subway stations and injured passenger's health. Therefor, it is a necessary to identify sources and to estimate pollutant sources in order to protect passenger's health and to keep clean subway environment. The purpose of this study was to analyze a air quality in the subway stations and to apply a new receptor methodology for quantitatively estimate of PM10 sources. In this study, the size distributions of particulate matters has been measured by using Aerosizer LD (U.S.A., API, Inc.). It's real time measurement capability of time-of-flight technique offers a significant advantage of user convenience and air pollution management. Also, the mass concentrations of PM 10 has been measured by using mini-vol portable sampler (U.S.A., Airmetrics Co.). The sampling performed in Seoul subway stations during the period of February 2000 and April 2000. The number distribution data used in this study consisted of 26 raw data sets in the Jongno-sam-ga station. Correlation Analysis can be used in subway stations for source separation and identification. Then, number contribution from each source is determined by the particle number balance (PNB). The mass concentration data used in this study consisted of 31 raw data in the 8 different stations. The mass contributions of PM10 sources in the concourse by using PMF/CMB model.

• Microbiology and Biotechnology Letters
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• v.23 no.4
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• pp.432-438
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• 1995

The intracellular alginase from Vibrio sp. AL-145 was purified by ion chromatography on DEAE-Cellulose column, Q-Sepharose column, and gel filtration on Sephadex G-100 column. The optimum pH and temperature for the activity of the purified intracellular enzyme were 8.0 and 37$\circ$C, respectively. The enzyme was stable at the pH range of 7.5-8.5, and at 30$\circ$C for 30 min. The molecular weight of the intracellular enzyme was estimated to be about 23, 000 daltons by SDS-polyacrylamide gel electrophoresis. NaCl was required for enzyme activity and the optimum concentration was 0.5 M. The activity of intracellular enzyme was inhibited by Co$^{2+}$, Hg$^{2+}$, Zn$^{2+}$, 0-phenanthroline, $\rho$-CMB, EDTA and iodoacetate, and stimulated by Ca$^{2+}$, L-cysteine and 2-mercaptoethanol. This enzyme was an alginase specifically degrading alginic acid.

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.68-72
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• 1992

To investigate the characteristics of active sites of the chitinase isolated from AWOrnonus sulmonicidu YA7-625, effects of various chemicals un the enzyme activity were analyzed. $Hg^{2+}, Mn^[2+} \;and \; Cu^{2+}$ ' ions inhibited the activity of chitinase, while $Ca^{2+} , Zn^[2+} , Co^[2+} \; and\; Mg^[2+}$ ions at 1 mM stimulated enzyme activity. The chitinase was not inhibited by sulfhydryl ;gents, phenylglyoxal, and hydroxylamine, but was inhibited by iodine and N-bromosuccinimide. The $pK_{ps2} and pK_{ps2}$, values of chitinase were 4.04 a d 10.10, respectively. These results suggested that the chitinase from A~ronmzus salmonici& YA7-625 contains histidine, tyrosine. and tryptophan at the active center.

• Journal of Applied Biological Chemistry
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• v.42 no.1
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• pp.7-11
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• 1999

An extracellular chitinase of the selected strong antifungal microorganism, Serratia sp. 3095, was purified by salting out, affinity adsorption, Sepadex G-100 gel fitration, Sepadex G-75 gel fitration and DEAE Sepadex A-50 chromatography. The molecular weight of the purified chitinase was estimated to be 62,000 dalton by SDS-PAGE. Optimal pH and temperature of the chitinase were pH 7.5 and 45, respectively. The enzyme retained more than 80% of the activity between pH 5.5 and pH 10.5, and below $50^{\circ}C$ but was unstable above $60^{\circ}C$, below pH 5.0. The activity of the chitinase was inhibited about 60% by $Sn^{2+}$, 40% by $Hg^{2+}$ and $Ag^+$, 70% by AHA, 40% by iodoacetate, 35% by thiourea and p-CMB, but stabilized by SDS. $K_m$ value of the purified chitinase was 3.68 mg/ml for colloidal chitin. The chitinase from Serratia sp. 3095 showed antifungal activity to Fusariurm solani.

• Microbiology and Biotechnology Letters
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• v.15 no.5
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• pp.312-318
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• 1987

The apparent Michaelis constant Km of extracellular adenine deaminase from Streptomyces sp. J-350P was 5.8$\times$10$^{-5}$M. The activation energy or the enzyme was calculated from Arrhenius plots for adenine and the value was 3.13 Kcal/mole. The purine analogues, 6-chloropurine, 2,6-diaminopurine, 6-bromopurine, 4-aminopyrazolo[3,4-d] pyrimidine, 6-iodopurine, and 8-bromoadenine were substrates for the enzyme. 6-Dimethylaminopurine was a competitive inhibitor of the enzyme. The enzyme was inhibited by 0.1mM of Fe$^{3+}$, Ag+, and Hg$^{2+}$ and 1 mM of $\alpha$, $\alpha$＇-dipyridyl, Penta-chiorophenol, and p-chloromercuribenzoate.