• Food Science of Animal Resources
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• v.23 no.2
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• pp.155-160
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• 2003

The purpose of this study was to purify epidermal growth factor(EGF) as growth factor from human colostrum. The effects of purified EGF fraction were directly related to the growth of cells. Results were as follows; After eliminated fat from colostrum, skim milk was obtained. We obtained the EGF fraction by performing ultrafiltration and gel filtration, and then were convicted by SDS-PAGE. The result of analysis of purified EGF fraction by high performance liquid chromatography(HPLC) was shown a peak at 31.185 min period. And it was similar with standard EGF that was shown a peak at 31.545 min. 10 ng of EGF was contained in 10 mg/mL through immunoassay to measure EGF content from isolated fraction. After SDS-PAGE, isolation degree of purified fraction was convicted through western blotting. BALB/3T3 cell was the most effectively stimulated and proliferated at 1 mg/mL concentration of the purified EGF fraction and percentage of cell proliferation was about 95%. In the case of IEC-6 cell, that was about 71%.

• Journal of Life Science
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• v.11 no.5
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• pp.457-463
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• 2001

A bacterial strain SC-22 which produced alkaline lipase was isolated from salf-fermented shrimps. Strains SC-22 was identified as Staphylococcus xylosus. An alkaline lipase excreted by Staphylococcus xylosus SC-22 was purified by ammonium sulfate predipitation and column chromatography on Sephadex G-100 and DEAE-Sephace. The specific activity of purified lipase was 756U/mg of protein with 17.2% yield. The approximate molecular weight of the purified enzyme was 47 kDa. The partially purified lipase preparation had and optimum temperature of 4$0^{\circ}C$, an optimum pH of 8.0, and a stable of 5~10. Lipase activities were enhanced by salt ions such as $Ca^{2+}$, $Mg^{2+}$,N $a^{2+}$ while inhibited remarkably by heavy metal ions, C $u^{2+}$ and P $b^{2+}$.EX> 2+/.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.34 no.2
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• pp.120-126
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• 1989

This experiment was carried out to investigate the lectin of soybean (Glycine max L.) seed. Purification was done by 50-80% ammonium sulfate precipitation, CM-cellulose and Sephadex G-100 column. The purity was ascertained by electrophoresis. The molecular weight of purified lectin was estimated as 132,000. It was composed of three subunits which molecular weight was 45,000. The lectin was identified as glycoprotein by Schiff's reagent staining and Dubois method. The lectin agglutinated erythrocytes of rabbit and human. The amounts of the lectin to agglutinate human erythrocytes differed among the blood types: The blood type A required the least amount, the next was B, O, and AB in order. The agglutination was specifically inhibited by 5${\mu}$g/ml of N -acetyl.-D-galactoseamine and 200${\mu}$g/ml of D-galactose. Other tested sugars could not inhibit the agglutination of the erythrocytes by the lectin.

• Microbiology and Biotechnology Letters
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• v.38 no.2
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• pp.158-162
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• 2010

The gene encoding N-terminally truncated Tod polymerase ($\Delta$Tod polymerase) from Thermus thermophilus HJ6 was expressed in Escherichia coli under the control of the lambda pR and pL tandem promoters on the expression vector pJLA503. The N-terminal domain (250 amino acids) of Tod polymerase was removed without significant effect on enzyme activity and stability, while no 5'$\rightarrow$3' exonuclease activity was detected. The $\Delta$Tod polymerase was verified to possess very efficient reverse transcriptase (RT) activity in the presence of $MgCl_2$. The cDNA can also be amplified in the polymerase chain reaction (PCR) with this mutant enzyme. The $\Delta$Tod polymerase was exhibited higher activity than the Taq polymerase in a one-step RT-PCR.

• Journal of Food Hygiene and Safety
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• v.33 no.6
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• pp.516-520
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• 2018

Bacteriocin is a proteinaceous compound produced by microorganisms showing antimicrobial activities. In this study, the physicochemical properties of the bacteriocin produced by Enterococcus faecium CJNU 2008 strain were characterized. Partially purified bacteriocin showed stabilities against heat treatments at $100^{\circ}C$ for 30 min and $121^{\circ}C$ for 15 min and against solvents treatments such as methanol, ethanol, acetone, acetonitrile and chloroform. The bacteriocin also exhibited stabilities against lipase and ${\alpha}-amylase$ treatments but the stability was abolished at protease treatment, indicating that the antimicrobial agent from E. faecium CJNU 2008 was a proteinaceous bacteriocin. The bacteriocin also showed bactericidal mode of action against Listeria monocytogenes. The molecular mass of the bacteriocin was estimated to be under 6.5 kDa by a tricine-SDS-PAGE analysis. The bacteriocin was purified by HPLC. Further studies toward biochemical analysis of the bacteriocin are needed in near future.

• KSBB Journal
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• v.18 no.4
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• pp.324-328
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• 2003

In a mutagenicity test using the Salmonella typhimurium TA98 and TA100, the Xanthium strumarium L. extracts had not a mutagenicity. The extracts were assayed that antioxidative effect using a colony formation assay. The extracts showed protective effects against the cytotoxicity of H$_2$O$_2$ and increased the immunity induced by TNF and IL-1${\beta}$. The modulating effect of Xanthium strumarium L. extract on the induction of carcinogenesis by N-methyl-N'-nitro-N-nitrosoguanidin (MNNG), was investigated in Wistar rats. The GSH content was found to be reduced by MNNG treatment, but increased on adding extract. In addition the Xanthium strumarium L. extract increased p53 expression versus MNNG alone.

• Journal of fish pathology
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• v.17 no.2
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• pp.131-137
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• 2004

In the present study, phosphatidylcholine (PC) hydrolyzing enzyme had been isolated from membrane of flounder liver. PC hydrolyzing enzyme solubilized in 1% Triton X -100 from membrane was partially purified by sequential chromatography on Heparin Sepharose CL-6B and Heparin-5PW columns. The products by membrane-bound hydrolyzing enzyme were identified as phosphatidic acid and choline, but in the presence of primary alcohol, phosphatidylethanol was produced at the expense of phosphatidic acid. These data suggest that membrane-bound enzyme may be a PC-phosphoipase D (PLD) type. The enzyme had pH optimum at below 6.0 and temperature optimum at $37^\circ{C}$. The activity of PC-PLD was dose-dependently increased by $Ca^{2+}$ but not $Mg^{2+}$. The activity of PC-PLD was stimulate by PC, PIP2 and PE.

• The Korean Journal of Mycology
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• v.10 no.2
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• pp.67-73
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• 1982

The $(NH_4)_2\;SO_4$ (70%) treated crude enzymes from the culture filtrates of the$C-7^{+t}$ strain of Pyricularia oryzae which was grown on 2% CMC (carboxymethyl cellulose) for 8 days at $28^{\circ}C$ were chromatographied on Sephadex G-150 and DEAE-Sephadex A-25 columns. From the chromatography, three fractions of CMCase$(C_x)$ was examined using Na-CMC as substrate. The $C_x$ enzyme activity was optimal at pH 6.0 and $40^{\circ}C$, stable up to $40^{\circ}C$. The values of Km and Vmax of the enzyme were $2.8{\times}10\;mM$ and 5.9m moles/hour, respectively. The molecular weight determined by Sephadex G-150 column chromatography was around 80,000. Approximately sevenfold purified $C_x$ enzyme gave a single protein band on the polyacrylamide gel electrophoresis.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.7 no.6
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• pp.1302-1307
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• 2006

This study describes the preparation of high-performance photocatalyst and its environmental applications. We prepared visible-light response nano-particle photocatalyst exhibiting the similar photocatalytic activity with $TiO_2$, dispersed $TiO_2$ on $SiO_2$ with an active rutile type titanium oxide prepared at low temperature. The binder and stable photocatalytic $TiO_2$ sol for photocatalytic system were also prepared. Such products were evaluated by UV/Vis spectrometer, X-ray diffraction analysis, SEM, measurement of photocatalytic activities and surface area, mechanical properties of $TiO_2$-coated surfaces. The results obtained can be applied in efficient photocatalytic systems using POF and metal plate for the purification of air.

• Korean Journal of Microbiology
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• v.32 no.3
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• pp.208-214
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• 1994

We screened many species from a wide variety of bacterial genera for a new type II restriction endonuclease. The purification and characterization of SolI from a soil isolate, Streptoverticillium olivoverticillatum are described here. The enzyme turned out to be an isoschizomer of BamHI. It recognized the hexanucleotide sequence of 5'-G$\downarrow$GATCC-3' and cleaved as in dicated by the arrow, generating a 4 base 5' extension. Unlike its isoschizomer, BamHI, the activity was sensitive to dam methylation within the recognition sequence. Following ammonium sulfate fractionation of the crude extract, heparin-agarose and Affi-gel Blue column chromatography were employed to purify the enzyme. SolI required at least 0.2 mM of $MgCl_2$ for the cleavage to occur. The enzyme exhibited its maximal activity in the absence of NaCl, but was inhibited completely in the presence of 120 mM NaCl. The pH and temperature optima for activity were pH 8.6 and $40^{\circ}C$, respectively. The molecular weight of SolI was estimated to be 43,000 Da by Superose-12 gel filtraion chromatography.