• 자원리싸이클링
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• 제11권5호
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• pp.21-23
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• 2002

A new process based on the co-precipitation method was developed fer removing harmful impurities during Mn-Zn ferrite production such as $SiO_2$ and P from waste pickle liquor. By this process a final result of less than 100 ppm of $SiO_2$ and less than 10 ppm of P content in the ferric oxide is easily attained. Though Ca cannot be removed by this process, water rinsing of the ferric oxide is effective fer reducing Ca content to less than 100 pm. For further purification, the origins of each impurity must be investigated and then taken away.

• 물과 미래
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• 제17권2호
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• pp.85-97
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• 1984

Measuring the river flow and water quality in the midstream of the Nakdong River, the natural purification status in examined through the analyses of the elements which affect the variation of dissolved oxygen, and DO model is evaluated to the midstream reach of the river. The major results of this study are as follows; the pruification factor of the of the river is relatively high, it is worried over eutrophication considering much production of algae, and it is evaluated that important factor affecting the DO value computed by the proposed DO model are in order of reaeration coefficient, carbonaceous BOD and deoxygenation constant.

• KSBB Journal
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• 제6권2호
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• pp.123-128
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• 1991

The production of bassinosteroid-like substances of two hybrid types of Korean rice, Jangseongbyeo, Taebackbyeo were investigated. The shoots at the maximum tillering stage were extracted and purified by solvent fractionation, silica gel adsorption chromatography Sephadex LH-20 chromatography, charcoal adsorption chromatography, Bondesil chromatography and HPLC of reverse phase, successively. Biological activities of each purification step were monitored by the rice lamina inclination test. Higher activities against the rice lamina inclination test in the each purification step showed that the shoots of two cultivars biosynthesize brassinosteroids. Two cultivars also showed a similar distribution of biological activities of endogenous brassinosteroids detected by HPLC.

• 한국식품영양과학회지
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• 제20권4호
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• pp.388-394
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• 1991

Alkaline protease producing bacteria were isolated from soil and identified as Bacillus sp. CW-1121. It was found that the production of alkaline protease reached to maximum in 5 day of fermentation at 4$0^{\circ}C$. The enzyme was purified by ammonium sulfate precipitation, gel filtration on Sephadex G-150 and DEAE-cellulose ion-exchange chromatography. The homogeneity of the purified enzyme was verified by polyacrylamide gel electrophoresis. The enzyme was purified 5.72 fold and yield of the enzyme purification was 16.71%. When the purified enzyme was applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated to be 55, 000.

• 생명과학회지
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• 제8권2호
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• pp.145-157
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• 1998

We isolated 100 Vobrio sp. from marine products and sea from July to September, 1997. We attemped on purification of hemolysin produced by Vibrio sp. The growth, hemolysin production patterns by the 100 strains of Vibrio sp. showed identical, in general. V. unlnificus ys-1 produced hemolysis as the higtest titer. The optimal culture conditions for the hemolysin production by the V. vunificus ys-1 are followings; 1. Hemolysin production was optimal dering the late exponetial phage. 2. Maximal growth, hemolysin production were in heart infusion broth. 3. Maximal yields of hemolysin was obtained when the heart infusion broth had an intial pH of 8.0, 3$0^{\circ}C$, 3% NaCL. Hemolysin was purified from culture filtrate of the strain by ammonium sulfate recipitation, ion exchange and hydrophobic interaction chromatography. The results were as follows; 1. Hemogeneity of the purified hemolysin was demonstrated by revealing single band on SDS-PAGE. The molecular weight of purified hemolysin was 45KDa. 2. The absorbance rattern in ultraviolet wsa typical of those seen with most proteinb with 280nm. 3. Purified hemolysin was atable at 5$0^{\circ}C$ but 7$0^{\circ}C$ of the acivity was lost by heating for 30 min at 6$0^{\circ}C$/ Optimal temperature of purified hemolysin was 35$^{\circ}C$. 4. Purified hemolysin was stable at the pH range of 6~9, but in the less the pH5.0. above the pH 9.0, the hemolysin activity was lost completely.

• KSBB Journal
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• 제19권5호
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• pp.368-373
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• 2004

The optimal condition for the production of a glucan and a fructan synthesizing enzymes from Leuconostoc mesenteroides NRRL B-1149 were studied based on the different medium compositions. Response surface methodology was applied to find the optimistic condition showing the relationship between the fermentation response (enzyme activities) and the fermentation variable concentrations of yeast extract, peptone concentration, K2HP04 concentration and sucrose. Optimum medium composition for both enzymes production was $0.75\%$ yeast extract, $0.72\%$ peptone, $1\%$ K2HP04 and $2.17\%$ sucrose. Using this medium, the activities produced in culture was 0.90 U/m~ for glucosyltransferase (GTase) and 0.96 U/ml for fructosyltransferase (FTase). After purification of 1149FTase by consecutive chromatographies using Sephadex G-150 and DEAE-Sepharose, a 1149FTase of 210 kDa on $7\%$ polyacrylamide gel was isolated and it synthesized soluble fructan. The 1149GTase showed a band of 180 kDa on $8\%$ polyacrylamide gel after purification using Bio-Gel P-100 gel chromatography and DEAE-Sepharose ion exchange chromatography and it synthesized insoluble glucan. The linkages of polymers were determined by methylation using Hakomori reagent and following NMR analysis. The glucan was composed of a(1~6) and a(1~3) linkages and the fructan was levan.

• Biotechnology and Bioprocess Engineering:BBE
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• 제6권2호
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• pp.144-149
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• 2001

For the production and purification of a single chain human insulin precursor, four types of fusion peptides $\beta$-galactosidase (LacZ), maltose binding protein (MBP), glutathione-S-transferase (GST), and (His)(sub)6-tagged sequence (HTS) were investigated. Recombinant E. coli harboring hybrid genes was cultivated at 37$\^{C}$ for 1h, and gene induction occurred when 0.2mM of isopropyl-D-thiogalactoside (IPTG) was added to the culture broth, except for E. coli BL21 (DE3) pLysS harboring a pET-BA cultivation with 1.0mM IPTG, followed by a longer than 4h batch fermentation respectively. DEAE-Sphacel and Sephadex G-200 gel filtration chromatography, amylose affinity chromatography, glutathione-sepharose 4B affinity chromatography, and a nickel chelating affinity chromatography system as a kind of immobilized metal ion affinity chromatography (IMAC) were all employed for the purification of a single chain human insulin precursor. The recovery yields of the HTS-fused, GST-fused, MBP-fused, and LacZ-fused single chain human insulin precursors resulted in 47%, 20%, 20%, and 18% as the total protein amounts respectively. These results show that a higher recovery yield of the finally purified recombinant peptides was achieved when affinity column chromatography was employed and when the fused peptide had a smaller molecular weight. In addition the pET expression system gave the highest productivity of a fused insulin precursor due to a two-step regulation of the gene expression, and the HTS-fused system provided the highest recovery of a fused insulin precursor based on a simple and specific separation using the IMAC technique.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2003년도 생물공학의 동향(XIII)
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• pp.666-666
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• 2003

• Bulletin of the Korean Chemical Society
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• 제32권12호
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• pp.4337-4340
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• 2011

The vitamin D receptor binding peptide, VDRBP, was overexpressed as a fused form with the ubiquitin molecule in Rosetta(DE3)pLysS, a protein production strain of Escherichia coli harboring an induction controller plasmid. The fusion protein was bound to the immobilized metal ions, and the denaturation and renaturation of the fusion protein were performed as a part of the purification procedure. After the elution of the fusion protein, the peptide hormone was released from its fusion partner by using yeast ubiquitin hydrolase (YUH), and subsequently purified by reverse phase chromatography. The purity of the resulting peptide fragment was checked by MALDI-TOF mass and NMR spectroscopy. The final yields of the target peptide were around 5 and 2 mg per liter of LB and minimal media, respectively. The recombinant expression and purification of this peptide will enable structural and functional studies using multidimensional NMR spectroscopy and X-ray crystallography.

• Asian-Australasian Journal of Animal Sciences
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• 제27권4호
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• pp.574-579
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• 2014

A lysozyme gene from breast of Tibetan sheep was successfully expressed by secretion using a-factor signal sequence in the methylotrophic yeast, Pichia pastoris GS115. An expression yield and specific activity greater than 500 mg/L and 4,000 U/mg was obtained. Results at optimal pH and temperature showed recombinant lysozyme has higher lytic activity at pH 6.5 and $45^{\circ}C$. This study demonstrates the successful expression of recombinant lysozyme using the eukaryotic host organism P. pastoris paving the way for protein engineering. Additionally, this study shows the feasibility of subsequent industrial manufacture of the enzyme with this expression system together with a high purity scheme for easy high-yield purification.