• The Korean Journal of Mycology
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• v.11 no.1
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• pp.15-21
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• 1983

Exodextranase from Aspergillus ustus was purified by chromatography and characterized by various conditions. The optimal pH of the purified dextranase was 6.5 and this enzyme was maximally activated at $40^{\circ}C$. The enzyme was stable at the temperature below $50^{\circ}C$. The enzyme was markedly inactivated by $Hg^{2+},\;Cu^{2+},\;KCN\;and\;Co^{2+},\;but\;Ba^{2+},\;Fe^{2+},$ cysteine, EDTA, and ascorbic acid enhanced the activity of the enzyme. The main products from the hydrolysis of dextran incubated with the dextranase were glucose, isomaltotriose and oligosaccharide. When dextran was incubated with the mixture of pullulanase and ${\alpha}-amylase$, it was hydrolyzed into glucose, isomaltose and oligosaccharide. Polysaccharides in the decade teeth powder were hydrolyzed by the dextranase into glucose, isomaltotriose and oligosaccharides. In the hydrolysis of the teeth powder with the mixture of dextranase, pullulanase and ${\alpha}-amylase$, were proved to be similar to the dextran hydrolysates.

• Korean Journal of Food Science and Technology
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• v.12 no.1
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• pp.1-5
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• 1980

Crude invertase was obtained from the water extracts of Korean ginseng, Panax ginseng C. A. Meyer, by fractionation with $0.8{\sim}1.0$ saturation of ammonium sulfate. The properties of the crude invertase were as follows: Crude invertase was stable in the pH range between 5 and 9, and at the temperature below $35^{\circ}C$. Crude invertase showed the optimum pH at 5.0 and the optimum temperature at $50^{\circ}C$. The activity of the crude invertase was inhibited by $Ag^{+}\;Mn^{+}\;Hg^{+}\;Zn^{+},\;and\;Rb^{+}$, while $Ca^{+}\;Cu^{+},\;and\;Fe^{3+}$ demonstrated remarkable increasing effects on the enzyme activity.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.5
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• pp.593-600
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• 1999

The survival rates of Littorina brevicula exposed to experimental concentration regimes of TBTCl, HB and Cd on the large and the small size individuals during 80 days were $80\%$ at 0,9ppb TBTCl, 40 and $25\%$, respectively at 200ppb Hg, and 75 and $45\%$, respectively at 100ppb Cd. The growth rates of the experimental animals exposed to each concentration for 80 days was 0.023mm/day at control, 0.019mm/day at 0.1ppb and 0.014mm/day at 0.9ppb TBTCl, 0.022 mm/day at 5ppb, 0.008 mm/day at 200ppb Hg, and 0.017 mm/day at 5ppb, 0.008mm/day at 100ppb Cd. The respiration rates and excretion rates of the experimental animals exposed to chronic concentration of TBTCl, Hg and Cd were decreased until approximatively 40 days and increased after, Toxic effect of pollutants on L. brevicula was highest at TBTCl. The histological injury of L. brevicula exposed to TBTCl, Hg and Cd was shown at gill, digestive organ and muscle, respectively.

• Applied Biological Chemistry
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• v.11
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• pp.109-117
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• 1969

Out of some 400 strains of Microorganisms, cellulase forming organisms was isolated from night soil during the course of screening tests. Two strains, Ku-3371 and Ku-4383 were found capable of producing cellulase in the shaking culture. General properties of the crude enzyme were as the following results. 1. The optimum pH values on CMC-saccharifying, CMC-liquefying and filter paper disintegrating activities were 4.0 to 5.5. 2. The stable pH range was within 3.5 to 6.5, 3. The optimum temperature was $40-45^{\circ}C$, the thermal stability was below $50^{\circ}C$ except on paper disintegrating activity and completely inactivated at $70^{\circ}C$. 4. Dialyzed crude enzyme was activated by $Mn^{2+}\;and\;Co^{2+}$ repectively but $Hg^{2+}$ was strong inhibitor.

• Journal of the Korean Chemical Society
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• v.28 no.2
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• pp.114-120
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• 1984

The reversible oxygenation of a solid stae polymeric cobalt(II) porphyrin complex, PVP-CoTPP was studied at 0, -24 and $-78^{\circ}C$. When PVP-CoTPP was contacted with $O_2 $at$-78^{\circ}C$ the oxygen uptake increased with oxygen partial pressure. At about 700mmHg $O_2$, the amount of oxygen taken up corresponded approximately one oxygen molecule to one Co(II) complex. The amount of $O_2$ taken up by PVP-CoTPP decreased with increasing temperature. When $16O_2$ was admitted to the Co(II) complex a EPR signal corresponding to $O_2^-$ increased with a decrease in Co(II) signal. The results suggest that an electron is transfered from Co(II) in PVP-CoTPP to oxygen forming a $Co(III)-O_2^-$ complex where $O_2^- $is superoxide type.

• Journal of Korean Society of Forest Science
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• v.4 no.1
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• pp.14-16
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• 1965

(1) The sterilizing effects of NaF, $CuSO_4$, $CuCO_3$, $HgCl_2$, $ZnSO_4$, and coaltar creosote on the mycelial growth of Irpex consors Berk. Polystictus versicolor L. Fr, Polystictus versicalor L. var. nigricans, and Schizophyllum commune Fr. Were studied. (2) The range of minimum density of the fungicides to check the growth of four fungi mentioned above was as follows; NaF 0.15~0.25(%) $CuSO_4$ 0.20~0.35(%) $CuCO_3$ 0.40~0.50(%) $HgCl_2$ 0.05(%) $ZnSO_4$ 0.40~0.45(%) Creosote 0.10~0.15(%) Of the fungicides tested, $HgCl_2$ was most effective in fungicidal effects, and Creosote, NaF, $CuSO_4$, $ZnSO_4$, $CuCO_3$, followed. The order of resistance of the fungi to the fungicides was as follows: S. Commune Fr. P. Versicalor L. var.nigricans I. Consors Berk P. Versicalor L. Fr. (3) The fungicides were added to the pepton-agor culture medium at the concentration between 0.01 and 0.5%, and the medium was filled into 9cm petridshes. Two square millimeter agar blocks prepared separately from the fungi Contained agar were placed in the middle of the Petri-dishes, in cubated six days at $26^{\circ}C$. Diameter of biggest Colonies were measured.

• Microbiology and Biotechnology Letters
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• v.6 no.4
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• pp.149-153
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• 1978

A strain of Streptomyces sp producing chitinase was isolated from soil and its cultural condition and some properties of this enzyme were investigated. When 0.375 per cent of glucose was added to basal medium, this organism produced the most quantities of this enzyme after shaking culture at 3$0^{\circ}C$ for 48 hrs., while the production of the enzyme was repressed at the more concentration of glucose than that. The enzyme had a optimal pH of 7.0, optimal temperature of 5$0^{\circ}C$ and the activity of that was not decreased by heat treatment for 20 minute at 7$0^{\circ}C$. And then the activity was increased by Co$^{2+}$ but was slightly inhibited by Hg$^{2+}$, Ni$^{2+}$, Pb$^{2+}$.EX> 2+/.

• Membrane and Water Treatment
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• v.1 no.4
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• pp.231-251
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• 2010

The sulfatation of chitosan, by reaction with chlorosulfonic acid under controlled conditions, allowed increasing the pH range of chitosan solubility. The biopolymer was characterized using FTIR and $^{13}C$-NMR spectroscopy, elemental analysis and titration analysis and it was tested for mercury recovery by polymer enhanced ultrafiltration (PEUF). In slightly alkaline conditions (i.e., pH 8) mercury recovery was possible and at saturation of the polymer the molar ratio $-NH_2$/Hg(II) tended to 2.6. Polymer recycling was possible changing the pH to 2 and the polymer was reused for 3 cycles maintaining high metal recovery. The presence of chloride ions influences metal speciation and affinity for the polymer and "playing" with metal speciation allowed using the PEUF process for mercury separation from cadmium; at pH 11 the formation of hydroxo-complexes of Hg(II) limits it retention. Cake formation reveals the predominant controlling step for permeation flux.

• Analytical Science and Technology
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• v.17 no.6
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• pp.470-475
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• 2004

The mercury film thin layer flow cell (MFTLFC) which yielded the highest sensitivity for the electrochemical reduction of doxorubicin was constructed by coating the glassy carbon working electrode (GCE; $A=0.208cm^2$) with $5{\mu}L$ of HgO coating solution (0.5% HgO + 0.25% polystyrene/cyclohexanone) and subsequently followed by applying a potential of -0.40 V for 300 sec in the flow stream of an acetate buffer of pH 4.5. The voltammogram of doxorubicin reached the diffusion current plateau at -0.53 V vs. a Ag/AgCl (3 M NaCl) in the MFTLFC. The diffusion current (Id) of doxorubicin at the MFTLFC was 1.7 times greater than the Id obtained at the TLFC employing a bare glassy carbon working electrode. When the peak areas (electric charge) were plotted vs. concentrations of standard anthracyclines, the calibration factors of doxorubicin and daunorubicin were $1.12{\times}10^8{\mu}C/M$ (coefficient of determination; $R^2$: 0.969) and $0.98{\times}10^8{\mu}C/M$> ($R^2$: 0.999), respectively in the concentration range between $1.0{\times}10^{-8}M$ and $1.0{\times}10^{-6}M$.

• Korean Journal of Microbiology
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• v.30 no.4
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• pp.239-245
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• 1992

Buci1llr.s 11c~h~n~1rnSiSi.As 3-2MI which is responsible for the special taste of traditionalKorean soy sause produced two kinds of proteinase. The activity of the proteinasc I washigher about two fold than that of proteinase 11. The optimai, reaction pH of proteinaseI and I1 wcre found to be 7-1 1.5 and 7-9. respectively. Proteinase I1 was more stable andactive than proteinase I at pH ranges around 3 to 5. The optimal te~tlperature of proteinaseI and I1 were 502. The temperature stabilitl of proteinase I1 was Inore stable thanproteinase 1 at temperature range around 30-quot;~A. ctivities of proteinase I and I1 graduallydeclined above $30^{\circ}$C and 45C. respectively. Proteinasc 1 was more active than proteinaseI1 at salt concentration range around 25-3500. The K,,, values of casein and soy proteinfor proteinase I were 6.89 mglml and 3.98 mglml. In case of proteinase 11. they were 9.00mgiml anti 11.44 111g/ml. respectively. The activity of the crudc enzyme was increased by1 rnM Pb(CH3COO). but was decreased by 5 n1M and 10 rnM of HgS04 and ZnS04. Thetwo proteinases produced amino acids and peptides from the soybean protein. The peptideswere digested into amino acids. Both protcinases were found to be the main enzymes thatproduced amino acids which make the main taste of traditional Korean soy sauce.al Korean soy sauce.