• Journal of Life Science
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• v.14 no.5
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• pp.794-799
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• 2004

Cyclodextrin glucanotransferase (CGTase) produced by Bacillus subtilis NAl/pKBl was used for the production of cyclodextrin (CD). The enzyme was purified by ion exchange and gel filtration chromatography. The purified enzyme exhibited its maximum activity in the pH range of 6.0 to 7.0 and temperature range of 60 to $70^{\circ}C$. Immobilization of purified CGTase was carried out with various immobilization matrices. Amberlite IRA-900, a strong basic anion exchange resin, showed the highest immobilization ability (38 units per gram resin). Optimal pH and temperature for enzymatic reaction of the immobilized CGTase were pH 6.0 and 60t. The activity of immobilized CGTase maintained more than a month and could be reused for a month in a continuous enzyme reactor for the production of CD.

• KSBB Journal
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• v.11 no.5
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• pp.529-535
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• 1996

Methyl frucloside was purified from the aqueous sugar/methyl fructoside solution by liquid chromatography using Amberlite IRA-900, strong anion-exchange resin. The optimum operating conditions, resolution and productivity of methyl fructoside were discussed to evaluate the practical feasibility of the proposed chromatographic separation process of methyl fructoside which is useful as a new starting material for sugar ester synthesis. The linear chromatography model with HETP was well applied to the chromatographic separation process of methyl fructoside and the theoretical solution successfully predicted the elution chromatogram of methyl fructoside and sucrose at different superficial linear velocity of eluent for rectangular feed with different loading volume of packed bed. The optimum operating conditions were found to be 75% with the loading volume of packed bed at 1.13 cm/min of the superficial linear velocity at $60^{\circ}C$, and gave the productivity of methyl fructoside of 7 mg/g-resin/h with the resolution of 1.1.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.3
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• pp.174-180
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• 2000

Cyclodextrin glucanotransferase (CGTasa) from Thermoanaerobacter sp. was adsorbed on the ion exchange resin Amberlite IRA-900. The optimum conditions for the immobilization of the CGTase were pH6.0 and 600 U CGTase/g resin, and the maximum yield of immobilization was around 63% on the basis of amount ratio of the adsorbed enzyme to intial amount in the solution. Immobilixation of CGTase shifted the optimum temperature for the enzyme to peoduce transglycosylated xylitol from 7$0^{\circ}C$ to 9$0^{\circ}C$ and improved the thermal stability of immobilized CGTase, especially after the addition of soluble starch and calcium ions. Transglycosylated xylitol was continuoncly produced using immobilized CGTase in the column type packed bed reactor, and the operating conditions for maximum yield were 10%(w/v) dextrin (13 of the dextrose equivalent) as the glycosyl donor, 10%(w/v) dextrin (13 of the dextrose equivalent) as the glycosyl donor, 10%(w/v) xylitor as the glycosyl acceptor, 20mL/h of medium fiow rate, and 6$0^{\circ}C$. The maximum yield of transglycosylated xylitol and productivity were 25% and 7.82 g.L-1.h-1, respectively. The half-life of the immobilized CGTase in a column type packed bed reactor was longer than 30 days.

• Journal of the Korean Chemical Society
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• v.27 no.5
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• pp.361-367
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• 1983

The selective separation and the quantitative recovery of uranium from Korean monazite sand have been studied by anion-exchange chromatography. It has been shown that method of anion-exchange chromatography under controlled conditions of elution can be applied to the production of relatively high purity of Uranium Oxide from monazite sand. Under the optimum separation conditions, the recoveries from standard sample were up to 99.3% as $U_3O_8$ on sulfate form anion resin bed and 99.2% as $U_2O_3{\cdot}P_2O_7$ on phosphate form anion resin bed. The possibility of recovering uranium from the monazite sulfate solution using a strong base anion exchange resin-Amberlite IRA-900. Uranium was successfully recovered about 92 percent. Phosphate ion did not seem to interfere with the process.

• Journal of Microbiology and Biotechnology
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• v.18 no.11
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• pp.1789-1791
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• 2008

This study was aimed (i) to develop an effective method for the purification of ginsenosides for industrial use and (ii) to compare the distribution of ginsenosides in cultured wild ginseng roots (adventitious root culture of Panax ginseng) with those of red ginseng (steamed ginseng) and white ginseng (air-dried ginseng). The crude extracts of cultured wild ginseng roots, red ginseng, and white ginseng were obtained by using a 75% ethanol extraction combined with ultrasonication. This was followed sequentially by AB-8 macroporous adsorption chromatography, Amberlite IRA 900 Cl anion-exchange chromatography, and Amberlite XAD16 adsorption chromatography for further purification. The contents of total ginsenosides were increased from 4.1%, 12.1%, and 11.3% in the crude extracts of cultured wild ginseng roots, red ginseng, and white ginseng to 79.4%, 71.7%, and 72.5% in the final products, respectively. HPLC analysis demonstrated that ginsenosides in cultured wild ginseng roots were distributed in a different ratio compared with red ginseng and white ginseng.

• Journal of Life Science
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• v.16 no.2 s.75
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• pp.245-252
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• 2006

A bacterial strain, identified as Staphylococcus aureus JJ-11, producing collagenase was isolated out of 40 persons having skin troubles. S. aureus JJ-11 produced collagenase optimally in the media containing 1.5%(w/v) gelatin, 1%(w/v) yeast extract, 0.4%(w/v) $K_2HPO_4$, 0.005%(w/v) $NiSO_4{\cdot}6H_2O$ at $37^{\circ}C$ for 18 hrs. The collagenase produced by Staphylococcus aureus JJ-11 was purified at 6.66-folds purity through application of chromatography with Amberlite IRA-900 and Sephacryl S-300 HR columns. The molecular weight of the partially purified enzyme was estimated to be 62 kDa by SDS-PAGE. The protein exhibited optimum enzymatic activity at pH 7.0, and showed a stable activity at pH 4-8. The optimum temperature for collagenase was at $37^{\circ}C$, and activity was maintained upto $40^{\circ}C$. The enzyme activity was slightly elevated in the presence of divalents such as, $Fe^{2+},\;Co^{2+}\;and\;Ba^{2+}$ However, the activity was inhibited in the presence of $Sr^{2+}\;or\;Hg^{2+}$. The inhibition of activity by O-phenanthroline and EDTA suggested that the enzyme may contain metal which is required for activity. The enzyme showed the highest activity when insoluble collagen (type I) was, used as a substrate.

• Journal of Life Science
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• v.15 no.4 s.71
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• pp.657-663
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• 2005

Collagenases are generally defined as enzymes that are capable of degrading the polypeptide backbone of native collagen under conditions that do not denature the protein. An extracellular collagenase-producing bacterial strain was isolated from kimchi and identified to be Bacillus subtilis JS-17 through morphological, cultural, biochemical characteristics and 16S rDNA sequence analysis. Optimum culture condition of Bacillus subtilis JS-17 for the production of collagenase was $1.5\%$ fructose, $1\%$ yeast extract, $0.5\%\;K_2HPO_4,\;0.4\%\;KH_2PO_4,\;0.01\%\;MgSO_4\cdot7H_2O,\;0.01\%\; MnSO_4\cdot4H_2O,\;,0.1\%$ citrate and $0.1\%\;CaCl_2$. The production of collagenase was optimal at $30^{\circ}C$ for 72 hr. A collagenase was isolated from the culture filtrate of Bacillus subtilis JS-17. The enzyme was purified using Amberlite IRA-900 column chromatography, Sephacryl S-300 HR column chromatography and DEAE-Sephadex A-50 column chromatography The purified collagenase has an specific activity 192.1 units/mg. The molecular weight of the purified enzyme was estimated to be 28 kDa by SDS-PACE. The purified collagenase has $100\%$ activity up to $55^{\circ}C$.

• Journal of Physiology & Pathology in Korean Medicine
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• v.20 no.5
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• pp.1321-1326
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• 2006

Total ginsenosides were purified and their antioxidant, antibacterial and anticancer activities were measured. The crude extracts of ginseng, which were extracted with 75% ethanol by ultrasonification method, were firstly purified on AB-8 macroporous adsorption column to remove water soluble impurities, and decolored on Amberlite IRA 900 Cl anion-exchange column. Then, they were purified on Amberlite XAD16 adsorption column to delete the non-polar impurities. Total ginsenosides contents of the purified extracts were 79.4%, 71.7% and 72.5% in cultured wild ginseng, red ginseng and white ginseng, which were significantly increased than those of crude extracts. All of the three extracts showed concentration-dependant scavenging activities against DPPH radicals, among which white ginseng showed the most powerful activity. Cultured wild ginseng roots showed strongest effect against both B. subtilis PM 125(Gram-positive) and E. coli D31 (Gram-negative) bacteria, while red ginseng and white ginseng only showed the activity against B. subtilis. According to the result of the MTT assay, ail of the three extracts inhibited the growth of U-937 human hohistiocytic lympma cell, which were significantly different (p < 0.05) when compared to the control.