• Journal of the Korean Society of Food Science and Nutrition
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• v.16 no.2
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• pp.128-135
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• 1987

Extracellular ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase produced by a thermophilic and cellulolytic bacterium, Herpetosiphon geysericola CUM 317, were partially purified by salting out with ammonium sulfate and by chromatography on a DEAE-cellulose column and on a CM-cellulose column. The Km values of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase for potato starch were $2.31mg/m{\ell}$, $7.69mg/m{\ell}$, and $8.33mg/m{\ell}$. The molecular weights of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase were calculated to be about 84000 dalton, 76000 dalton and 80000 dalton, respectively.

• Microbiology and Biotechnology Letters
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• v.7 no.3
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• pp.149-155
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• 1979

Streptomyces sp. 115-5 was selected as the most active microorganism of about 200 strains for the production of chitinase. The enzyme was purified by (NH$_4$)$_2$SO$_4$ treatment, 1st-Sephadex G-100, DEAE-Cellulose, 2nd-Sephadex G-100 column chromatography, and evidence for homogenity was obtained from CM-Sephadex C-50 column chromatography and polyacylamide gel electrophoresis. The purified enzyme hydrolyzed chitin (N-acetyl glucosamine polymer) and chitosan (glucosamine polymer) but not cellulose. And with chitin as the substrate, a Km value of 3.6 mg of chitin per ml and a Vmax of 100 $\mu$mo1e fer hr were found. The activation of the chitinase was 3.66 kcal per mole. The molecular weight of the enzyme was esti-mated about 56,000 daltons by Sephadex G-100 chromatography and isoelectric point as pH 3.0.

• Applied Biological Chemistry
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• v.12
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• pp.33-41
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• 1969

1. Crude cellulase extracted from wheat bran media of Chaetomium globosum with pH 7.0 McIlvaine buffer was fractionated by precipitation with ammonium sulfate and by treatment with the cellulose powder, DEAE-Sephadex A-25 and Amberite XE-65 (IRC-50) column chromatography. 2. Consquently two cellulases C-1 and C-2 were obtained by cellulose column chromatography. Cellulose C-1 was a powerful CMC-saccharifying and CMC-liquefying activity but cellulose C-2 was stronger CMC-liquefying activity compared to CMC-saccharifying activity and cellulase C-2 had smaller protein than that of cellulose C-1. And cellulose C-2 was fractionated by DEAE-Sephadex A-25 column chromatography into cellulase C-1-1 and cellulose C-1-2. 3. It can be obtained, therefore, that cellulose produced Chaelomium globosum consisted, at least, of three cellulases C-2, C-1-1 and C-1-2. 4. Cellulose C-1-1 was homogenous in the ultraviolet and the ultracentrifuge pattern. And cellulose C-1-1 had enzyme for CMC-saccharifying activity. 5. The optimum pH for the enzyme activity of cellulose C-1-1 was 4.0 in any methods of meas urement reducing sugar and viscosity. The optimum temperature was $40^{\circ}C$ in any methods. 6. The pH stability of cellulase C-1-1 was within pH 5.0 to pH 6.0 at $40^{\circ}C$ and fairly stable in acidic solution. 7. The heat stability was below $50^{\circ}C$ at pH 4.0 and complete heat inactivation of this cellulase occurred at $70^{\circ}C$.

• Microbiology and Biotechnology Letters
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• v.11 no.1
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• pp.47-52
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• 1983

The extracellular inulase produced by Aspergillus sp. C-58 was isolated by pH and charcoal treatment, precipitation with ammonium sulfate from the crude extract, and separated into 3 fractions (P-I, II, III) by DEAE-cellulose column chromatography in the ratio of 31.1:1.7:1 with respect to the activity. The ratio of inulase activity to sucrase activity of P-I, P-II and P-III fraction was 0.23, 0.24 and 1.1 respectively. The enzyme P-I fraction was purified 482 fold with a 22.8% yield by DEAE-Sephadex A-50, Sephadex G-75, Sephadex G-100 (1st and 2nd) column chromatography, and appeared homogeneous on polyacrylamide disc gel electrophoresis and ultracentrifugation.

• Parasites, Hosts and Diseases
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• v.21 no.1
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• pp.41-48
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• 1983

The activity and distribution of aspartate aminotransferase (EC 2.6. 1. 1) and alanine aminotransferase (EC 2.6.1.2) in adult Fascicle hepatica have been studied. Fasciola hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of GOT and GPT was measured by the method of Reitman and Frankel. Isozyme patterns of those enzyme were also examined by DEAE-cellulose column chromatography. The results obtained were as follows; 1. The activity of aspartate and alanine aminotransferase was about 0.55 unit and 0.92 unit per 1g of Fascicle hepatica, respectively. 2. The activity of those enzymes was relatively low compared with those in mammalian tissues. 3. The distribution of aspartate aminotransferase in the subcellular organelles showed that 71% of the activity was in cytosolic, 24% in mitochondrial and 5% was in nuclear fraction. 4. About 22% of the total alanine aminotransferase activity was found in the mitochondrial fratstion, about 66% in the cytosolic fraction. 5. Aspartate aminotransferase from cytosolic fraction was separated into two types of isozymes, whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatography.

• Applied Biological Chemistry
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• v.13 no.3
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• pp.223-229
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• 1970

1. The preparation and some enzymatic properties of crude alkaline protease from a thermophilic mold, Myriococcum sp. was investigated. 2. Optimum pH for the hydrolysis of casein was 9.0 at $50^{\circ}C$ for 10 minutes. Optimum temperature was $55^{\circ}C$ at pH 9.0 for 10 minutes. The enzyme was highly stable at the range of pH 6.0 to 11.0 at $30^{\circ}C$ 3. The alkaline protease in the culture filterate was isolated two fractions by elution column chromatography on DEAE-Cellulose.

• Microbiology and Biotechnology Letters
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• v.15 no.6
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• pp.420-424
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• 1987

Isocitrate lyase from crude extract of Saccharomycopsis lipolytica ATCC44601 and MX9-11RX8 temperature-sensitive mutant was purified about 54 times and 87 times, respectively by ammonium sulfate fractionation, Toyo peal HW-55F gel filtration and DEAE-Cellulose ion exchange chromatography, The molecular weight of the purified isocitrate lyase from this yeast was estimated to be 230, 000 by gel filtration on Sephadex G-200, and SDS-polyacrylamide Eel electrophoresis showed that the enzyme consisted of four identical or similar subunits with a molecular weight of 59, 000 and the enzyme showed optimum activity at pH 6.9.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.777-784
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• 1993

The bleaching effect of potato lipoxygenase Isoenzymes on ${\beta}-carotene$ was studied. Two lipoxygenase Isoenzymes(LOX-1, LOX-2) from potato tuber were purified by CM-cellulose, DEAE-cellulose ion exchange chromatography. LOX-1 and LOX-2 seemed to have bleaching effect on ${\beta}-carotene$ in the presence of linoleic acid, which the decrease in the formation of conjugated dienes. LOX-2 was founded to have a greater pigment bleaching activity than that of LOX-1.

• Proceedings of the Ginseng society Conference
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• 1978.09a
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• pp.75-77
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• 1978

It was found that water extract of Panax ginseng strongly inhibited adrenaline-induced lipolysis in isolated fat cells of rat epididymal adipose tissue. An antilipolytic action of the water extract was easily inactivated by treatment with pronase, suggesting that the active principle might be a protein or a peptide. Experiments were designed to purify the antilipolytic substance, or insulin-like substance, of the water extract. The water extract was dialyzed against disti'led water. The outer dialysate was subjected to DEAE-cellulose column chromatography, gelfuaration on sephadex G-50 column, avicel cellulose column chromatography and phospho-cellulose column chromatography, successively. The finally purified substance gave one spot on thin layer chromatography. The molecular weight was found to be around 1000. Experiments are now in progress to elucidate the structure of this insulin-like peptide.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 1995.11a
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• pp.104-104
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• 1995