• Journal of Life Science
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• v.18 no.6
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• pp.845-851
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• 2008

${\beta}-Lactamase$, secreted from Bacillus sp. J105 strain was purified to a single band on SDS-PAGE by ammonium sulfate precipitation, ion exchange column chromatography and gel-filtration. The molecular weight of the purified enzyme was 31 kDa on SDS-PAGE and its isoelectric point was 7.35. Optimal pH and temperature for enzymatic reaction were 5 and $40^{\circ}C$, respectively. As a result of total amino acid composition analysis of the purified enzyme, Gly and Ala were occupied 14.1 and 13.3 mole %, respectively. Km and Vmax value of purified enzyme were 1.33 mM and 0.36 mM/ml using ampicillin as a substrate, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.9
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• pp.1321-1327
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• 2011

The microorganism producing an invertase (E.C. 3.2.1.26) was isolated from wine and tentatively identified as Saccharomyces cerevisiae by cellular fatty acid analysis. The invertase was purified to homogeneity by ammonium sulfate precipitant, dialysis, ion-exchange chromatography on DEAE-Sephadex A-50, and gel chromatography on Sephadex G-200 from the culture supernatant of Saccharomyces cerevisiae JS59. The specific activity and the purification fold of the purified invertase were 7620.9 unit/mg protein and 13.9, respectively. The molecular weight of the purified invertase was estimated to be 38.5 kDa by SDS-PAGE. The optimum pH and temperature for the invertase activity were pH 5 and $55^{\circ}C$, respectively. The invertase activity was relatively stable at pH 4~6 and temperature $55^{\circ}C$. The activity of invertase was inhibited by $Ag^{2+}$ and $Hg^{2+}$, but on the contrary, activated by $Co^{2+}$ and $Mn^{2+}$. Michaelis constant ($K_m$) for invertase reaction in sucrose solution was 11.5 mM. TLC analysis of the products produced in sucrose solution during invertase reaction showed the progressive presence of glucose and fructose in accordance with sucrose hydrolysis.

• Bulletin of the Korean Chemical Society
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• v.30 no.3
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• pp.543-550
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• 2009

The single-crystal structure of largely ammonium-exchanged zeolite Y dehydrated at room temperature (293 K) and 1 ${\times}\;10^{-6}$ Torr. has been determined using synchrotron X-radiation in the cubic space group $Fd\overline{3}m\;(a=24.9639(2)\AA)$ at 294 K. The structure was refined to the final error index $R_1$ = 0.0429 with 926 reflections where $F_o>4\sigma(F_o)$; the composition (best integers) was identified as |$(NH_4)_{60}Na_{11}$|[$Si_{121}Al_{71}O_{384}$]-FAU. The 11 $Na^{+}$ ions per unit cell were found at three different crystallographic sites and 60 ${NH_4}^{+}$ ions were distributed over three sites. The 3 $Na^{+}$ ions were located at site I, the center of the hexagonal prism ($Na-O\;=\;2.842(5)\;\AA\;and\;O-Na-O\;=\;85.98(12)^{\circ}$). The 4 $Na^{+}$ and 22 ${NH_4}^{+}$ ions were found at site I' in the sodalite cavity opposite the double 6-rings, respectively ($Na-O\;=\;2.53(13)\;\AA,\;O-Na-O\;=\;99.9(7)^{\circ},\;N-O\;=\;2.762(11)\;\AA,\;and\;O-N-O =\;89.1(5)^{\circ}$). About 4 $Na^{+}$ ions occupied site II ($(Na-O\;=\;2.40(4)\;\AA\;and\;O-Na-O\;=\;108.9(3)^{\circ}$) and 29 ${NH_4}^{+}$ ions occupy site II ($N-O\;=\;2.824(9)\;\AA\;and\;O-N-O\;=\;87.3(3)^{\circ}$) opposite to the single 6-rings in the supercage. The remaining 9 ${NH_4}^{+}$ ions were distributed over site III' ($N-O\;=\;2.55(3),\;2.725(13)\;\AA\;and\;O-N-O\;=\;94.1(13),\;62.16(15),\;155.7(14)^{\circ}$).

• Parasites, Hosts and Diseases
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• v.25 no.2
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• pp.141-148
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• 1987

Circulating antigens in rats experimentally infected with Paragonimus westermani were examined by ELISA. From a total of 22 albino rats, each fed with 25 metacercariae, blood samples were collected until 12 weeks after infection. The specific antibodies against P. westermani in the serum of an infected cat were purified by ammonium sulfate precipitation, DEAE anion-exchange chromatography and affinity chromatography serially. So-called double antibody sandwich ELISA method was used for the detection of circulating antigens. The results were as follows: Mean value of O.D. in control sera was O. 04 (S.D.=0. 04). After infection, mean O.D.(S.D.) values were changed serially: 0.03(0.01) at 0.5 week(3 days), 0.55(0.50) at 1 week, 0.69(0.45) at 1.5 week, O.20 (0.19) at 2 weeks and O.13(0.10) at 2.5 weeks of infection. They returned, thereafter, to the level before infection. When O. 16 (mean+3 S.D.) were considered as cut-off value, those higher than O. 16 were observed only in the sera collected between 1 and 2.5 weeks after infection. Average 8. 4 immature worms (2.2 from the lungs and pleural cavities; 6.2 from muscles) were recovered in a rat at 12 weeks after infection. The fact that circulating antigens were not detected after 3 weeks of infection was considered to the caused by the formation of antigen-antibady complexs.

• Korean Journal of Soil Science and Fertilizer
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• v.31 no.1
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• pp.67-71
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• 1998

This study was carried out to granulate artificial zeolite powder that remove ammonium nitrogen and phosphorous simultaneously in wastewater treatment. Optimum water content was required for 30 percent volume to granulate artificial zeolite with 1.7mm diameter and 1~2cm length using granulator. Portland cement could remove much $NH_4{^+}$ and $PO_4{^{3-}}$ from the wastewater than other binding materials. Mixed 33, 25. 20. 16 percent of portland cement to artificial zeolite powder(v/v), cation exchange capacity of the granulars were 66.5, 81.4, 126.8, $151.2cmol^+kg^{-1}$ and hardness of that were 176.1, 24.4, 4.1, $0.4kg\;cm^{-2}$, respectively. Content of portland cement in the granular were related with removal of $PO_4{^{3-}}$ positively and that of $NH_4{^+}$ negatively. Shaked 1g of the granulars that made of portland cement 33 percent with 40ml synthetic wastewater containing $NH_4{^+}$ $1545mgl^{-1}$ and $PO_4{^{3-}}$ $417mgl^{-1}$, 99.4 percent of $NH_4{^+}$ and 90.3 percent of $PO_4{^{3-}}$ were removed simultaneously after 48 hours shaking. The longer shaking, the more $NH_4{^+}$ and $PO_4{^{3-}}$were removed. The artificial zeolite granular had both micropore and macropore that could be useful in the wastewater purification.

• Applied Chemistry for Engineering
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• v.17 no.2
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• pp.177-182
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• 2006

In this work, we have prepared organophilic MMT having thermal stability by ion exchange reaction of various aromatic ammonium salts with MMT containing sodium ion. The organic modifiers having alkyl side chains and amine functional group were successfully synthesized by effectively introducing the surfaces of MMT via ion exchange reaction to form organophilic MMTs with a view to improve the reactivity and thermal stability. The WAXD patterns of organophilic MMT showed the more increased gallery spacing by $3.3{\AA}$ than that of the pristine MMT and also the onset of initial decomposition of organophilic MMT was $275^{\circ}C$ as determined by a thermogravimetric analysis. The polyimide (PI) nanocomposite films based on poly(amic acid) and organophilic MMT were prepared by a solution blending followed by cyclodehydration reaction. We have investigated the dispersity of organophilic MMTs in PI matrix by using WAXD and the effect of the organophilic MMT content on the mechanical properties of PI nanocomposite films was studied.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.6-12
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• 1998

To extract insoluble proteins and to improve functional properties of abolished proteins, a protease producing Aspergillus sp. MS-18 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of protease reached to the maximum when the wheat brae medium containing, 3% arabinose, 0.5% polypepton, 0.1% $(NH_4)_2SO_4$ and 0.2% magnesium chloride was cultured for 3 days. Protease was purified 16.9 folds after ion exchange chromatography and gel filtration and the specific activity was 340.4 unit/mg. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of protease was estimated to be 30,000. Crystalization form of purified protease was a stick shape with rounding edges. The optimum pH and temperature for the protease activity were 9.0 and $60^{\circ}C$, respectively. The enzyme was stable in pH 7.0-12.0 at $50^{\circ}C$. The activity of purified enzyme was inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$ and $Pb^{2+}$, whereas it was activited by $Na^+$, $Mg^{2+}$ and $Mn^{2+}$. The activity of the protease was inhibited by the treatment with ethylenediaminetetraacetic acid and phenylmethane sulfonyl fluoride. The result suggests that the purified enzyme is a serine protease with metal ion at active site. Km and Vmax of purified protease were $29.33\;{\mu}mole/L$ and $5.13\;{\mu}g/min$, respectively.

• Journal of Dairy Science and Biotechnology
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• v.15 no.1
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• pp.1-9
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• 1997

This study was conducted to efficiently separate the Ig from Korean native cattle colostrum and to utilize them as an immunogen for the production of antibodies aginst rabbit. The results obtained were as follows : 1. About 84% of Ig G could be separated from Korean native cattle colostrum by·gel filtration using Superose 12 column on HPLC. The separation profile of Korean native cattle colostral immunoglobulin was similar that of Holstein colostral Ig. 2. Separation of Korean native cattle colostral Ig by anion exchange chromatography using Mono Q column on HPLC was poor resolution chromatographic pattern. 3. Hi-Trap Protein G column showed better results than the Protein A Sepharose CL-4B column in the Ig G binding capacity from Korean native cattle colostral Ig. 4. Protein G Sepharose Fast Flow system resulted in higher Ig g binding capacity as the industrial size scale-up approach. 5. Sufficient titer reaction of antibody to Korean native cattle colostral Ig G was confirmed by ELISA.

• Applied Biological Chemistry
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• v.40 no.3
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• pp.178-183
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• 1997

A protease was purified from Bacillus subtilis CCKS-111 by ammonium sulfate treatment, DEAE-cellulose ion-exchange chromatography, Sephadex G-100 gel filtration and high performance liquid chromatography (HPLC). The specific activity of the purified enzyme was 24.3 unit/mg protein and the purification fold of enzyme was 50.6. Molecular weight of the purified enzyme estimated about 28,000 by HPLC gel filtration. The amino acid residues of this enzyme were 251.3 except threonine, serine and glycine. This result was similar to Bacillus subtilis subtilisin DY. From the first N-terminal amino acid to the 32th amino acid, the amino acid sequence was estimated after RP-HPLC elution. N-terminal and the 32th amino acids were alanine and aspartic acid. Alanine, serine, glycine and arginine were four major acids in the enzyme.

• Korean Journal of Microbiology
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• v.40 no.3
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• pp.199-204
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• 2004

The parathion hydrolase (OPH) produced by Pseudomonas rhodesiae H5 was purified by ammonium sulfate precipitation, DEAE-Toyopearl 650M ion exchange chromatography and Sephadex gel filtration chromatography. Parathion hydrolase from crude extracts of P. rhodesiae H5 has two components designated as OPH $I_1$ and OPH $I_2$, Optimum pH and temperature of OPH $I_1$and OPH $I_2$ were pH 7.2 and $30^{\circ}C$, and pH 7.6 and $37^{\circ}C$, respectively. The activation energy of OPH $I_1$ for the hydrolysis of parathion was 3.01 ㎉/I, II, III in the temperature range of $4^{\circ}C$ to $30^{\circ}C$, and Michaelis constant ($K_m$) for parathion was 69.2 ${\mu}M$. The activation energy of OPH $I_2$ for the hydrolysis of parathion was 4.07㎉/㏖ in the temperature range of $4^{\circ}C$ to $37^{\circ}C$, and Michaelis constant for parathion was 150.9${\mu}M$. Furthermore OPH $I_1$ was completely inhibited by 1 mM $Ca^2+$, $Cu^2+$, $Mg^2+$, $Ni^2+$, but OPH $I_2$ was less inhibited than OPH $I_1$ by the metals used in this study.