• The Korean Journal of Mycology
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• v.12 no.2
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• pp.59-64
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• 1984

The effects of cultural conditions in the rice straw media for cellulolytic enzymes production by Pleurotus sajor-caju were investigated. The optimum moisture content, pH and temperature for enzymes production were 60%, 7.0 and $35^{\circ}C$ in $C_1-cellulase$, and 60%, 5.0 and $25^{\circ}C$ in $C_x-cellulase$, and 60%, 7.0 and $20^{\circ}C$ in ${\beta}-glucosidase$, respectively. When light was irradiated during the cultivation period, $C_1-cellulase$ and ${\beta}-glucosidase$ production were decreased but $C_x-cellulase$ production increased at $500{\sim}1,000\;lux$. During the cultivation period, $C_1-cellulase$ production was contrary to $C_x-cellulase$ and ${\beta}-glucosidase$. Among the various materials added, rice bran was effective to $C_1-cellulase$ production, cotton seed cake and rice bran to $C_x-cellulase$ production, and defatted soybean and fish meal to ${\beta}-glucosidase$ production. The optimum concentration of rice bran for enzymes production were 20% in $C_{1-}$, $C_x-cellulase$ and 10% in ${\beta}-glucosidase$.

• 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.15 no.5
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• pp.346-351
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• 1987

A cellulase gene of Clostridium themocellum was transferred to Escherichia coli by molecular cloning with pBR322. The gene was carried in a Hind III digested DNA sequence of about 1.8 kb. This Rind III fragment expressed activities on carboxymethyl cellulose (CMC) and on filter gaper in E. coli. The expression of clostridial cellulase gene in E. coli was studied and compared with the pro-ducts of cellulase genes in C. themocellum.

• Food Science and Preservation
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• v.21 no.3
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• pp.442-450
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• 2014

In this study, we isolated a cellulase-producing bacterium isolated from traditional Korean fermented soybean paste and investigated the effect of culture conditions on the production of cellulase. This bacterium, which was identified as Bacillus subtilis 4-1 through 16S rRNA gene sequence analysis, showed the highest cellulase activity when the cells were grown at $45^{\circ}C$ for 24 hours in the CMC medium supplemented with 1.0% of soluble starch and 0.1% yeast extract. The initial optimum pH of the medium was observed in the range of 5.0~9.0. The optimal pH and temperature for the production of cellulase from B. subtilis 4-1 were pH 9.0 and $60^{\circ}C$ respectively. In addition, the enzyme showed significant activity in the temperature range of $20{\sim}90^{\circ}C$, which indicates that B. subtilis 4-1 cellulase is an alkaline-resistance and thermo-stable enzyme. This enzyme showed higher activity with CMC as the substrate for endo-type cellulase than avicel or pNPG as the exo-type substrates for exo-type cellulase and ${\beta}$-glucosidase. These results suggest that the cellulase produced from B. subtilis 4-1 is a complex enzyme rather than a mono-enzyme.

• Korean Journal of Microbiology
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• v.13 no.3
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• pp.85-90
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• 1975

Crude cellulases freshly prepared from cultures of Aspergillus niger, Prnicillum motatum, Trichoderma vride 16273 and Trichoderma viride 16374 were assayed on 4 different substrates including Na-CMC, cellulose powder, starch and sucrose. Enzyme prepared from A. niger contained highly active hydrolytic enzymes of the 4 substrates assayed. P. notatum [yielded relatively lower amount of cellulase but the extracts were also highly reactive on starch and sucrose. Trichoderma viride 16274 yielded very little cellulase and invertase, but the extracts showed a high degree of amylase activity. Trichoderma viride 16374, however, yielded collulase comparable to that of Penicillium notatum, but lower activities of amylase and invertase were seen. Commercial cellulases prepared from Penicillium notatum (cellulase[K]) and Trichoderma viride(cellulase[J]) indicated enzyme activities closely parallel to the crude enzymes freshly prepared from fungus cultures. The optimum pH's of cellulolytic activities of cellulase[K] and cellulase[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase[K] and cellualse[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase [K] and cellulase [J] were $60{\circ}C$ and $50{\circ}C$ respectively. Assuming the average molecular weight of Na-CMC is about 115,000, the Km values of cellulase [K] and cellulase[J] were found to be $3.3{\times}10^{-5}/nM$ and $3.3{\times}10^{-4}/nM$ respectively.

• Journal of Microbiology and Biotechnology
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• v.9 no.1
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• pp.44-49
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• 1999

Cellulase production by fed-batch cultivation of Trichoderma reesei Rut C30 with various initial concentrations of Solka Floc in 1 % wheat bran-containing medium was investigated. The cellulase activity and productivity increased with initial Solka Floc concentration up to 5%. When a total Solka Floc concentration of 90 g/l was used for cellulase production, CMC (carboxymethyl cellulose) and FP (filter paper) activities, productivity, and yield were 359.7 U/ml, 30.61 U/ml, 161 FPU $L^{-1}$ $h^{-1}$, and 340 FPU $g^{-1}$, respectively. It was important to maintain a high cell concentration during cellulase production to obtain high cellulase activity and productivity. Cellulase powder was prepared by ammonium sulfate precipitation: FP activity was 396.7 U/g and CMC activity was 6481 U/g.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.139-146
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• 2004

A bacterium producing alkaline cellulase was isolated from soil, leaf mold and compost, and was identified as alkalophilic Bacillus sp. HSH-810 by morphological, cultural and biochemical determination. The optimum cul-ture condition of Bacillus sp. HSH-810 for the growth and alkaline cellulase production was $30^{\circ}C$ and pH 10.0. The maximum alkaline cellulase production was obtained when 1.0%(w/v) CMC, 0.5%(w/v) peptone, 0.02%(w/v) $CaCl_2$ and 0.02(w/v) $CoCl_2$ were used as carbon source, nitrogen source and mineral source, respectively. The optimum pH and temperature of the enzyme activity were pH 10.5 and $50^{\circ}C$, respectively. This enzyme was fairly stable in the pH range of 6.0-13.0 and at $50^{\circ}C$. For the effect of surfactants, the activity of alkaline cellulase was stable in the presence of sodium-$\alpha$-olefin sulfonate (AOS), sodium dodecyl sulfonate (SDS), Tween 20 and Tween 80, but inhibited by the presence of 0.1 linear alkyl-benzene sulfonate (LAS) sig-nificantly.

• Korean Journal of Pharmacognosy
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• v.7 no.2
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• pp.85-93
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• 1976

Since cellulose is the only organic material that is annually replenishable in very large quantities, we must explore ways to utilize it as a source of energy, food and chemicals. For the utilization of this resource, it is first enzymatic hydrolyzed to glucose, then the glucose can be used as a food, converted single cell protein by microorganism, fermented to clean burning fuel and other chemicals. Cellulolytic enzyme, cellulase, consists of two or three major components, $C_1-cellulase$, $C_x-cellulase$ and ${\beta}-glucosidase$. $C_x-cellulase$ are fairly common but $C_1-cellulase$ are quite rare. Trichoderma viride is the best source of active cellulose, especially $C_1-enzyme$. Saccharification rate of cellulose in greatly influenced by the degree of crystallinity and extent of lignification. But by the pretreatment the substrate with cellulose swelling agent, delignifying reagent and physical treatment, the degree of saccharification is enhanced. Thus, glucose syrups of 2 to 10% concentration are realized from milled newspaper. The enzymatic hydrolysis of such energy rich material, such as cellulose, to glucose is technically feasible and practically achievable on a very large scale.

• Applied Biological Chemistry
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• v.11
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• pp.109-117
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• 1969

Out of some 400 strains of Microorganisms, cellulase forming organisms was isolated from night soil during the course of screening tests. Two strains, Ku-3371 and Ku-4383 were found capable of producing cellulase in the shaking culture. General properties of the crude enzyme were as the following results. 1. The optimum pH values on CMC-saccharifying, CMC-liquefying and filter paper disintegrating activities were 4.0 to 5.5. 2. The stable pH range was within 3.5 to 6.5, 3. The optimum temperature was $40-45^{\circ}C$, the thermal stability was below $50^{\circ}C$ except on paper disintegrating activity and completely inactivated at $70^{\circ}C$. 4. Dialyzed crude enzyme was activated by $Mn^{2+}\;and\;Co^{2+}$ repectively but $Hg^{2+}$ was strong inhibitor.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1196-1199
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• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.