• Journal of Life Science
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• v.8 no.5
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• pp.598-603
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• 1998

A marine microbe, Vibrio anguillarum was isolated from fish and studied for its concerning pathogenic substance of hemolysin. Purification of hemolysin was achieved by the procedure of ammonium sulfate precipitation from cul-ture filtrate, DEAE-cellulose chromatography, and G-200 gel filtration with 36 fold of purification and 2.3% yield. The molecular weight of the purified hemolysin was 38,000 dalton by SDS-PAGE. The purified hemolysin was stable at pH 6-9, below 45$^{\circ}C$, and up to 1% of NaCl, respectively. $Ca^{2+}, Cu^{2+}, Zn^{2+}, Fe^{2+}$ inhibited the hemolytic activity whereas EDTA and $Mg^{2+}$ did not.

• Journal of Life Science
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• v.6 no.4
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• pp.241-249
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• 1996

A collagenase was isolated from the culture filtrate of Vibrio mimicus (ATCC 33658). The enzyme was purified to homogeneity by ammonium sulfate precipitation and DEAE-Sephadex A-50 chromatography, which an activity recovery of 22%. The molecular weight of the purified enzyme was estimated to be 42 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indication a monomer structure. The optimum pH and temperature od the enzyme for insoluble collagen (Type I) were around 7.75 and 28$\circ$C, respectively. Some chelating agents and serine protease inhibitor inactivated the enzyme, but L-cysteine and histidine did not affect the activity. The amino acid composition indicated that the collagenase contained high amounts of amino acid residues of glycine and alanine. The K$_{m}$ and R$_{cat}$/K$_{m}$ values for the collagenase, using insoluble collagen (type I) as substrate, were 2.86 mg/ml and 972.28 U/mg-protein, respectively.

• KSBB Journal
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• v.14 no.3
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• pp.322-327
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• 1999

The cholesterol oxidase(EC.1.1.3.6) produced from Streptomyces sp. No.4 which isolated from soil was purified and investigated for the enzymatic properties. The enzyme was purified specifically by cholesterol affinity column chromatography with a yield of 28.3%. The purified enzyme showed a single polypeptide on SDS-PAGE and the molecular weight was estimated to be 60,000 daltons. The enzyme activity was strongly inhibited by metal ions such as $HgCl_2$ and $CuSO_4$. Dithiothreitol and mercaptoethanol inhibited the enzyme activity at concentration of 1mM. The Michaelis constant(Km) for cholesterol was found to be 1.38mM by Lineweaver-Burk plot analysis. Amino acid analysis showed that the enzyme protein was composed of 416 amino acid residues including 52moles of glycine and 19moles of tryptophane.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.587-593
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• 1995

Lectin was purified by using $(NH_4)_2SO_4$, DEAE-cellulose ion-exchange chromatography and Sephadex G-150 column chromatography from Alismatis Rhizoma(AR). The specific activity of AR lectin was 50, 441units/mg, and purification folds were 114. The AR lectin agglutinated human erythrocytes of all types(A, B, O, AB). The molecular weight of AR lectin was estimated about 90, 500 daltons by gel filtration and each subunits were 42,000, 27,000 and 22,500 daltons on SDS-PAGE respectively. The hemagglutinating activity of the lectin was inhibited by sialic acid, glucose, ribose, galactose, sucrose, and lactose. It was also inhibited by cations such as $Hg^{++},\;Fe^{++},\;Cu^{++}\;and\;Pb^{++}$.

• Korean Journal of Food Science and Technology
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• v.21 no.3
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• pp.404-408
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• 1989

This study was conducted to confirm amino acids from the filterate of pollen treated by purified enzyme of bee larva gut for improving pollen food. The larva gut enzyme were purified by ammonium sulfate, ethanol and Sephadex gel filtration. The filterate of pollen treated with enzyme purified by ammonium sulfate showed the highest amount of amino acids. The amount of amino acids of the filterate from which the pollen was fermented with natural contaminants is 5.5 times as much as the pollen which was not fermented. The filterate of pollen treated with enzyme of bee larva gut contained eighteen different amino acids as follows : aspartates, glutamate, serine, glycine, histidine, arginine, threonine, alanine, proline , tyrosine, valine, methionine, cysteine, isoleucine, leucine, phenylalanine, lysine and trytophane.

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.3
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• pp.279-286
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• 1989

The alkaline protease producing mold isolated from and identified as Aspergillus fumigatus. It was found that the production of alkaline protease reach to maximum was cultured for 3 days at $30^{\circ}C$. The enzyme was purified 86.13 fold and yield of the enzyme purification was 6.4%, The purification procedure include ammonium sulfate treatment, gelfiltration on Sephadex G-25, G-75, G-150 and DEAE-cellulose ion-exchange chromatography. When the purified enzyme was applied sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated about 63000. This enzyme composed 17 amino acids and main amino acids of this enzyme were glycine and glutamic acid.

• Korean Journal of Food Science and Technology
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• v.21 no.5
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• pp.606-612
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• 1989

A New lectin from baby clam, Tapes japonica, was isolated and purified through the following procedures; acetone powder, 0.15M NaCl extraction, ammonium sulfate fractionation, N-acetyl-D-galactosamine-agarose affinity column, and ion exchange Mono Q of FPLC. This lectin nonspecifically agglutinated human erythrocytes but didn't agglutinate mouse and rabbit erythrocytes. And the lectin neither stimulated human lymphocytes nor agglutinated Sarcoma 180 cells. On polyacrylamide gel electrophoresis, the lectin migrated as a major single band indicating homogeneous. A molecular weight was estimated to be about 131,000 daltons by Biogel P-300 and 125,000 daltons by SDS-PAGE without ${\beta}-mercaptoethanol$. This lectin is supposed to be a tetramer composed of heterogeneous subunits, about 30,000 and 33,000 daltons. Baby clam lectin was inhibited by EDTA and recovered agglutinating activity by $Ca^{++}\;and\;Mn^{++}$. This lectin is revealed as glycoprotein that contained about 4.2% neutral sugar.

• Journal of Digital Convergence
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• v.17 no.1
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• pp.357-364
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• 2019

This study comparatively analyzed hair damage by hair bleach particles and identified three different bleach particle sizes using a scanning electron microscope (SEM). The powdered bleaching agents made of ammonium persulfate (APS) and potassium persulfate had particle sizes of $131{\mu}m$, $72{\mu}m$ and $48.8{\mu}m$. According to a hair damage test, cuticle lift-up or peeling hardly occurred when small bleach particles were used. In terms of hair color, the hair bleached with larger bleach particles was the darkest, while the hair bleached with small bleach particles was the brightest. The results found that for bleaching agents that are more effective in easing hair damage, those with little particles should be used. In addition, it appears that the selection of particles depending on the degree of hair bleaching would enhance bleaching effects and reduce hair damage. The above process is a way to get great results in selecting a bleaching agent. It is anticipated that hair damage could be reduced during hair bleaching based on the above results.

• Analytical Science and Technology
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• v.6 no.3
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• pp.307-311
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• 1993

Ionophore, which contains 5-membered heterocyclic compound, was prepared. $Mg^{2+}$ was determined by salting-out technique using ionophore as a chelating reagent. After $Mg^{2+}$ was extracted into the acetonitrile layer as a Mg-$(Ionophore)_2$ complex from acetate buffered aqueous solution by salting-out extraction technique, absorbance of complex was recorded by atomic absorption spectrophotometry. Optimum pH was between 2.5 and 5.0 for extraction and 1:2([$Mg^{2+}$]/[ionophore]) complex were formed. The range of detection was 0.24ppm~2.4ppm and $Ca^{2+}$ and EDTA were interfered in the determination of $Mg^{2+}$.

• Food Science and Preservation
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• v.12 no.5
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• pp.489-495
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• 2005

Polyphenol oxidase (PPO) from Burdock (Arctium lappa L.) was purified and characterized. Purification of polyphenol oxidase was achieved by ammonium sulfate precipitation, Phenyl-sepharose CL-4B hydrophobic chromatography and Sephadex G-100 gel filtration chromatography. The molecular mass of the purified PPO was estimated to be 30 kDa by SDS polyacrylamide gel electrophoresis. In a substrate specificity, maximum activity was achieved with chlorogenic acid, followed by catechol and catechin. Whereas, there was low activity with hydroquinic acid, resorcinol or tyrosine. The optimum pH and temperature for enzyme activity were 7.0 and 35$\circC$ with catechol, respectively. The enzyme was most stable at pH 7.0 while unstable at acidic and alkaline pH. The enzyme was stable when heated to 40$\circC$. But heating at 50$\circC$ for more than 30 min caused 50% loss of activity. Ascorbic acid, L-cystein and $Cu^{2+}$ inhibited the activity of pholyphenol oxidase.