• Korea Petroleum Association Journal
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• no.3 s.133
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• pp.100-102
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• 1992

이 자료는 최근 일본의 석유심의회 석유부회 석유정제설비문제소위원회에서 작성한 보고서를 옮긴 것이다. <편집자 주>

• Korea Petroleum Association Journal
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• no.1 s.35
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• pp.85-89
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• 1984

• Proceedings of the KSEEG Conference
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• 1999.04a
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• pp.297-300
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• 1999

• Korea Petroleum Association Journal
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• no.5 s.87
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• pp.74-79
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• 1988

●수소화정제법의 종류 ●약품정제법

• Korea Petroleum Association Journal
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• no.8 s.42
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• pp.51-55
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• 1984

이 글은 미국가스정제업자협회의 전무이사인 Ron Cannon씨가 최근 Oil & Gas Journal지에 발표한 글을 발췌ㆍ번역한 것이다. <편집자 주>

• Journal of the Korea Academia-Industrial cooperation Society
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• v.17 no.6
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• pp.9-17
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• 2016

A purification method was established for high-purity chondroitin sulfate from skate cartilage. Hydrolytic extraction of skate backbone cartilage was investigated with the proteases alcalase and protamex, and the extraction contents of chondroitin sulfate were measured with several physicochemical processes. The yield of extract from skate cartilage with $40^{\circ}Brix$ concentration was 23.3% with 2% alcalase hydrolysis, which was decreased to 8.47% and 3.37% with the first and second additional ethanol purifications, respectively. The yield was 16.62% with one ethanol purification after hydrolysis with a mixture of 1% alcalase and 1% protamex. The content of chondroitin sulfate was measured as 39.88-45.08% with different ratios of ethanol solvent. The content was 42.92% at a solvent ratio of 1:1 with alcalase protease and 45.08% with a ratio of 1:2 using a protease mixture of alcalase and protamex. The molecular weight range of chondroitin sulfate was about 110-310 thousand Da, and the purity of chondroitin sulfate was 24.87-49.92% with a mixture of alcalase and protamex in GPC analysis. The maximum purity of chondroitin sulfate was 53.93% after ultrafiltration. The odor strength of chondroitin sulfate was decreased by 33% and 38% after ethanol purification and additional filtration with activated carbon, respectively. The odor concentration of ammonia and TMA from chondroitin sulfate was decreased by 52.1% and 37.89% with activated carbon filtration and two ethanol purifications, respectively, but it was necessary to eliminate the odor components efficiently using additional physicochemical processes.

• Microbiology and Biotechnology Letters
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• v.38 no.1
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• pp.84-92
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• 2010

Antibacterial compound from Bacillus subtilis MJP1 was purified using C18 Sep-Pak cartridge, ion exchange chromatography, and gel filtration chromatography. The purified antibacterial compound showed antibacterial activity against Listeria monocytogenes, Bacillus subtilis, Staphylococcus aureus subsp. aureus, and Enterococcus faecalis. The purified antibacterial compound was found to be stable at $100^{\circ}C$ for 5 min and in the pH range of 3.0~9.0, but it was unstable at pH 10.0. It was inactivated by proteinase K and pronase E, and heat treatment at $121^{\circ}C$ for 15 min, but it was stable with lipase and $\alpha$-amylase treatment, which indicated its proteineous nature. Ultra performance liquid chromatography and electrospray ionization tandem mass spectrometry analysis were used to identify the purified antibacterial compound and confirmed the existence of two peptides (3356.54 Da, 3400.5244 Da).

• Korean Journal of Agricultural Science
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• v.36 no.1
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• pp.111-122
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• 2009

When the cattail pollen was identified by using fibrinolytic agents, we found that the fibrinolytic activity was controlled by an enzyme. Therefore, for determining the fibrinolytic activity of cattail pollen, the fibrinolytic enzyme in cattail pollen was purified by gel filtration using DEAE-cellulose, Sephadex G-150 and HPLC. Also, its purity was certified by polyacrylamide gel electrophoresis, and its physico-chemical properties, such as pH and temperature stabilities and effects of metal, inhibitors and substrates, were examined. The specific activity, purification fold, and molecular weight of the enzyme were 38U/mg, 86.4,and 75kDa, respectively. The optimum pH for the purified enzyme was at 4.0 and it was stable at pH 4.0-6.0. The optimum temperature was $55^{\circ}C$ and it was stable at $30-60^{\circ}C$. But the enzyme began to be inactivated at $70^{\circ}C$ and its activity was totally lost at temperatures above $80^{\circ}C$. As for substrate specificity, the enzyme was most effective in dissolving fibrin, followed by whole casein, ${\kappa}$-casein, ${\alpha}$-casein, ${\beta}$-casein, and BSA. With casein as the substrate, Km value was found to be 0.44mM and the enzyme showed a high affinity for casein. As for the metal ions affecting enzyme activity, $K^+$, $Na^+$, and $Mg^{2+}$ had no effect on enzyme reaction while $Zn^{2+}$ and $Fe^{2+}$ showed potent inhibitory activity. Judging from the fact that the purified enzyme was also strongly inhibited by PMSF, iodoacetic acid, and SDA, it assumed to be a serine protease.

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.316-322
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• 1998

An ${\alpha}$-D-galactosidase (${\alpha}$-D-galactoside galactohydrolase, EC 3. 2. 1. 22) from sunflower seed was purified by affinity chromatography using N-$\varepsilon$-aminocaproyl-${\alpha}$-D-galactopyranosylamine coupled to sepharose and its properties were examined. The specific activity of the purified enzyme, tested with p-nitrophenyl-${\alpha}$-D-galactopyranoside as substrate, was 291.66 units/mg protein, representing an 115-folds purification of the original crude extract. The final preparation obtained from by Sephadex G-25 chromatography showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 42,000 by SDS-polyacrylamide gel electrophoresis. The purified galactosidase showed maximum activity at pH 4.5 and 55$^{\circ}C$, and was stable in the pH and temperature ranges of 4.0 to 5.0 and 30 to 55$^{\circ}C$, respectively. The enzyme activity was inhibited by Ag$\^$2+/, Hg$\^$2+/ and Co$\^$2+/. The enzyme activity was not affected considerably by treatment with other metal compounds. The enzyme liberated galactose from melibiose, raffinose, copra galactomannan, guar gum and locust bean gum by TLC, and also the hydrolysis rate of substrate was compared by HPLC.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.1
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• pp.76-83
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• 1992

Enterotoxigenic E. coli is one of the major causative agents of the infantile diarrhea and traveler's diarrhea. The heat-stable enterotoxin (ST) is thought to be a virulence factor in the pathogenesis of the diarrhea and to be a maker for identification of the enterotoxigenic E. coli from non pathogenic E. coli. ST producing E. coli KM-7 strain was isolated from the swine and molecular cloning of ST gene of KM-7 strain. Transformant eKT-53 $(ST^+,\;LT^-)$ was selected by infant mouse assay (IMA). The culture supernatant of eKT-53 strain was performed purification by multipled steps. The culture supernatant (crude ST) was purified by sequentially applying batch adsorption chromatography on Amberlite XAD-2 resin, ion exchange chromatography on DEAE-Sephacel anion exchanger, gel filtration chromatography on Bio-Gel P-6 and preparative polyacrylamide slab gel electrophoresis. About 113-fold purification was achieved with a yield of about 11% of crude ST and the minimum effective dose(MED) of this purified ST was about 2.8ng in IMA. Homogeneity of purified ST was demonstrated by showing a single band in analytical SDS polyacrylamide disc gel electrophoresis.