• Korean Journal of Microbiology
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• v.30 no.4
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• pp.260-264
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• 1992

Pseudotnorju.c sp. EL-071P degrading 2.4.5-trichlorophe~~oxyi~cetaicci d (2.3.5-T) was resistantto antibiotics: rifampicin. ampicillin. kanamycin and metal ions : Zn" and Cu".The plasmitl related to the degradation of 2.4.5-'r and rifa~npicin resistance was isolatecifrom the strain. Its size was about 40 Kb. As result of transforming the plasmid intoEsch~rirhiti coli MClOhl, it was confirmed that the plasmid ura.; related to 2.4.5-T degradation.The strain coulil grow in the various chlorinated aromatic analogs as the solc carbon source.In the case of chlorophcnols. the chlorinated mono-substituteti phenols were easily dcgradetlin the order ol' ortho-. ~ ~ a r um- ,c ~tu-position.T he 2.3.5-T mctaholism was inhibited by 4-chlorophenol of 2.4.5-7' analog. In non-chlorinateci aromatics. ~ C I I L O ~ I ~ Csa.l icylilte i~ndtoluene were uscd ax the carbon source by the strain and typestrain Acudonlotrtr.\ plrtirltrKCTC 1643 having clegrad;~bility of various aromatics. But naphtalene was usecl only bythe A~urlomonri.\ sp. EL-07 1 P.the A~urlomonri.\ sp. EL-07 1 P.

• Korean Journal of Microbiology
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• v.48 no.4
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• pp.298-304
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• 2012

Among 63 Bacillus strains grown at $60^{\circ}C$ from sixteen samples of homemade Korean soybean paste, one strain was selected for producing the thermostable protease. The isolate has been identified as Bacillus licheniformis on the basis of its 16S rDNA sequence, morphology and biochemical properties. Culture filtrate of the isolate showed maximal protease activity at the reaction condition of $60-65^{\circ}C$ and pH 11. The culture filtrate retained more than 87% of initial protease activity after incubation for 30 min at $60^{\circ}C$ without substrate. In order to develop the medium composition, effects of ingredients including nitrogen sources, carbon sources, metal ions and phosphate were examined for protease production of the isolate. Lactose and soytone peptone were the most effective carbon and nitrogen source for the enzyme production. After the late logarithmic growth phase the isolate began to produce the protease, and the maximum protease productivity was reached to 550 unit/ml in the optimized medium consisting of lactose (3%), soytone peptone (1.5%), $MgSO_4$ (0.1%), $K_2HPO_4$ (0.03%), and $KH_2PO_4$ (0.03%) at 28 h of incubation.

• Korean Journal of Microbiology
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• v.50 no.1
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• pp.73-83
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• 2014

The objective of the this study was to investigate the binding capacity and removal ability of lactic acid bacterial strains obtained from Korean soybean paste for mutagenic heterocyclic amines (HCAs) formed during cooking of protein-rich food at high temperature. Among 19 strains identified by carbohydrate fermentation and 16S rRNA sequencing, the live cell or cell-free culture supernatant of Lactobacillus acidophilus D11, Enterococcus faecium D12, Pediococcus acidilactici D19, L. acidophilus D38, Lactobacillus sakei D44, Enterococcus faecalis D66, and Lactobacillus plantarum D70 inhibited the mutagenesis caused by either 3-amino-1,4-dimethyl-5H-pyrido[4,3-b] indole (Trp-P-1) or 3-amino-1-methyl-5H-pyrido[4,3-b] indole (Trp-P-2) in Salmonella typhimurium TA98 and TA100. The bacterial cells of the isolated strains showed greater binding activity than the pure cell wall, exopolysaccharide, and pepetidoglycan. The carbohydrate moieties of the cell wall or protein molecules on the cell surface have a significant role in binding Trp-P-1 and Trp-P-2, since protease, heating, sodium metaperiodate, or acidic pH treatments significantly (P<0.05) reduced the binding efficacy of the tested bacteria. Addition of metal ions or sodium dodecyl sulfate decreased the binding ability of E. faecium D12, L. acidophilus D38, and E. faecalis D66. Therefore, the binding mechanisms of these strains may consist of ion-exchange and hydrophobic bonds. Especially, the high mutagen binding by L. acidophilus D38 and L. plantarum D70 may reduce the accumulation or absorption of Trp-P-1 and Trp-P-2 in the small intestine via increased excretion of a mutagen-bacteria complex.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.5
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• pp.842-849
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• 1997

This study was designed to investigate the antioxidative activity of enzymatic hydrolysates prepared from defatted anchor muscle by various pretenses. In these hydrolysates, the hydrolysates derived from pepsin and Protamex showed the strongest antioxidative activity. Enzymatic hydrolysates also showed the synergistic effects on antioxidative activity of $\alpha-tocopherol$, and almost no change in butylated hydroxytoluene (BHT). Peroxidation of metal ions $(Fe^{3+},\;Cu^{2+})$ was inhibited by enzymatic hydrolysates. Ten fractions (P-1 to P-10) were fractionated from the peptic hydrolysates by Amberlite IR-120 and Bio-gel P-2 column chromatography. The maximum antioxidative activity was observed in the traction P-2 (fraction No. $26\~31$). In amino acid composition of before and after hydrolysis of defatted anchovy muscle and the active fractions (P-2), contents of aspartic arid and glutamic acid were increased, but alanine, cysteine, tyrosine and phenylalanine were decreased.

• Journal of the Korean Chemical Society
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• v.45 no.5
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• pp.442-447
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• 2001

The charge-transfer compound (OMTTF)AuCl$_4$ was prepared from the direct reaction of octamethylenethiafulvalene (OMTTF) with HAuCl$_4{\cdot}xH_2$O in THF. (OMTTF)$_2PtCl_4$, (OMTTF)_2IrCl_6{\cdot}2H_2$O, and (OMTTF)Os$Cl_5{\cdot}THF$ were also formed using $H_2PtCl_6{\cdot}xH_2O$, $H_2IrCl_6{\cdot}xH_2O$ and $H_2OsCl_6$, respectively. The prepared compounds were characterized by magnetic (EPR, magnetic susceptibility), spectroscopic (IR, UV-Vis), electrochemical (CV) methods, and the powdered electrical conductivity measurement. The powdered electrical conductivities at room temperature were ~$10^{-7}S{\cdot}cm^{-1}$. The experimental results show that $OMTTF^+$ monocation radicals exist in all of the prepared compounds. The redox potential of OMTTF supports that $OMTTF^+$ is relatively stable. The magnetic properties indicate that there are significant magnetic interactions between the localized odd electrons on the central metal (Ir and Os) ions and the odd electrons resided on $OMTTF^+$ cation radicals in both (OMTTF) $_2IrCl_6{\cdot}2H_2O$ and (OMTTF)$OsCl_5{\cdot}THF$.

• Journal of Microbiology and Biotechnology
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• v.17 no.4
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• pp.638-643
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• 2007

The full encoding sequence for human type II hexokinase (HXK II) was cloned into the E. coli expression vector pET 21b and expressed as a C-terminally hexahistidine-tagged protein in the BL2l (DE3) strain. The IPTG-induced HXK II approximately accounted for 17% of the total E. coli proteins, and 81% of HXK $II_{6{\times}His}$ existed in inclusion bodies. To improve the production of soluble recombinant HXK II protein, in the functionally active form, we used low temperature, and the osmotic stress expression method. When expressed at $18^{\circ}C$, about 83% of HXK $II_{6{\times}His}$ existed in the soluble fraction, which amounted to a 4.1-fold yield over that expressed at $37^{\circ}C$. The soluble form of HXK $II_{6{\times}His}$ was also highly produced in the presence of 1M sorbitol under the standard condition $(37^{\circ}C)$, which indicated that temperature downshift and low water potentials were required to improve the yield of active recombinant HXK II protein. The expressed protein was purified by metal chelate affinity chromatography performed in an IDA Excellose column charged with $Ni^{2+}$ ions, resulting in about 40mg recombinant HXK II protein obtained with purity over 89% from 51 of E. coli culture. The identity of HXK $II_{6{\times}His}$ was confirmed by Western blotting analysis. Taken together, using the stress-governed expression described in this study, human active HXK II can be purified in sufficient amounts for biochemical and biomedical studies.

• Analytical Science and Technology
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• v.8 no.1
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• pp.63-68
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• 1995

For the preparation of pH-selectrode, tribenzylamine, polyvinylchloride, dioctylphthalate, sodium tetraphenylborate and tetrahydrofuran were mixed with 0.02, 0.62, 1.34, 0.02g and 10ml respectively, and added 1g of acetylene black, graphite, silicon carbide or tungsten carbide respectively to improve electric conductivity. The selectrodes of seven kinds were shown linear to hydrogen ion in the range of pH 2 and 9. The best electric conductor for preparation of pH-selectrode based on tribenzylamine as neutral carrier was acetylene black and responded potential of the selectrode to hydrogen ion was shown the values near to theoretical Nernstian slope at $20^{\circ}C$. The interfering effects of the selectrode on hydrogen ion in the presence of alkali and alkaline earth metal ions were shown the better results with less error than glass electrode. The reproducibility and stability were good for use as a selectrode, especially in the presence of fluoride ion.

• Journal of Sensor Science and Technology
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• v.23 no.3
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• pp.185-191
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• 2014

The width of depletion region in a varactor diode can be modulated by varying a reverse bias voltage. Thus, the preferred characteristics of depletion capacitance can obtained by the change in the width of depletion region so that it can select only the desirable frequencies. In this paper, the TV tuner varactor diode fabricated by hyper-abrupt profile control technique is presented. This diode can be operated within 3.3 V of driving voltage with capability of UHF band tuning. To form the hyperabrupt profile, firstly, p+ high concentration shallow junction with $0.2{\mu}m$ of junction depth and $1E+20ions/cm^3$ of surface concentration was formed using $BF_2$ implantation source. Simulation results optimized important factors such as epitaxial thickness and dose quality, diffusion time of n+ layer. To form steep hyper-abrupt profile, Formed n+ profile implanted the $PH_3$ source at Si(100) n-type epitaxial layer that has resistivity of $1.4{\Omega}cm$ and thickness of $2.4{\mu}m$ using p+ high concentration Shallow junction. Aluminum containing to 1% of Si was used as a electrode metal. Area of electrode was $30,200{\mu}m^2$. The C-V and Q-V electric characteristics were investigated by using impedance Analyzer (HP4291B). By controlling of concentration profile by n+ dosage at p+ high concentration shallow junction, the device with maximum $L_F$ at -1.5 V and 21.5~3.47 pF at 0.3~3.3 V was fabricated. We got the appropriate device in driving voltage 3.3 V having hyper-abrupt junction that profile order (m factor) is about -3/2. The deviation of capacitance by hyper-abrupt junction with C0.3 V of initial capacitance is due to the deviation of thermal process, ion implantation and diffusion. The deviation of initial capacitance at 0.3 V can be reduced by control of thermal process tolerance using RTP on wafer.

• Journal of Mushroom
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• v.17 no.4
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• pp.191-196
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• 2019

The edible ectomycorrhizal mushroom Amanita javanica is a valuable species protected by forest law in Korea. However, basic characterization data on its use as an important forest resource has been limited. This study was performed to determine mycelia growth characteristics of the domestically isolated Amanita javanica strain NIFoS 1267 on potato dextrose agar media under diverse culture conditions. Physical factors temperature, pH, and light, as well as chemical factors salts, heavy metals, and pesticides were examined for their effects on the growth of the mushroom strain. The mycelia of A. javanica strain exhibited optimal growth when cultured in dark at 30℃ in media with a pH of 5-6. Normal levels of growth were observed in media containing up to 2% saline. At a heavy metal ion content of 50 ppm, mycelial growth was not affected by arsenic ion but was affected by cadmium and lead ions. In the tests performed with two pesticides used in Korean forests, the growth of the mushroom strain was not affected by the presence of abamectin, but was inhibited in media containing acetamiprid, emamectin benzoate, or thiacloprid. These results are expected to facilitate artificial cultivation of A. javanica as a new commercial product.

• Korean Journal of Microbiology
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• v.39 no.4
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• pp.223-229
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• 2003

The purpose of this work was to perform the characterization of NAD(P)H-nitroreductase isolated from Stenotrophomonas sp. OK-5 capable of degrading 2,4,6-trinitrotoluene (TNT). Initially, NADP(H)-nitroreductase by a series of purification processes including ammonium sulfate precipitation, DEAE-sepharose, andQ-sepharose was prepared. From samples harvested from fraction collector, three different fractions (I, II & III)having the enzyme activity of NAD(P)H-itroreductase were detected. Specific activities of three fractions I, II,and III of NAD(P)H-nitroreductase were determined to approximately 5.06 unit/mg, 4.95 unit/mg and 4.86 unit/mg, and concentrated to 10.5, 9.8, and 8.9-fold compared to crude extract, respectively. Among these three fractions,the fraction I of NAD(P)H-nitroreductase demonstrated the highest specific activity in this experiment. Several factors affecting on the enzyme activity of NAD(P)H-nitroreductase (fractions I, II & III) were investigated.The optimum temperature of all NAD(P)H-nitroreductase (fractions I, II & III) was 30oC, and the optimal pH was approximately 7.5. Metal ions such as Ag+, Cu2+, Hg2+ inhibited approximately 80% enzyme activity of all NAD(P)H-nitroreductase, and the enzyme activities were decreased about 30-40% inhibition in the presence of Mn2+ or Ca2+. However, Fe3+ showed stimulatory effect on the enzyme activity. The molecular weights of NAD(P)H-nitroreductase (fractions I, II & III) were measured about 27 kDa on the SDS-PAGE.