• 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.

• Applied Biological Chemistry
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• v.12
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• pp.99-105
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• 1969

The yield of cellulase derived from Trichoderma $(O_2-1)$ was remarkably varied with various concentration of ethanol and acetone in purification of the enzyme. In the purification with ethanol of ${\beta}-glucosidase$, the best result was obtained in the concentration of 60% and, of CMCase and of filter paper disintegrating enzyme 80%. And in the purification with acetone of ${\beta}-glucosidase$, filter paper disintegrating enzyme, and CMCase, in the concentration of 60%, 80%, and 90% respectively, was shown the best yield. The activities of crude Cellulase preparation could be seperated into few of fractions by column chromatography with Silica gel, Cellulose powder, and gauze. Most of CMCase, avicelase, and ${\beta}-glucosidase$ were eluted, but most of filter paper disintegrating enzyme and the rest of enzymes mentioned the above were absorbed, and were eluted with water. Therefore, it was considered that CMCase is different from filter paper disintegrating enzyme in properties. The relative activity of CMCase was different from that of avicelase in the peak of elusion part. And it was considered that filter paper disintegrating enzyme and cellulose powder saccharifying enzyme was seperated respectively as absorption part and non absorption part. The auther came to the conclusion that at least there were more than three sorts of cellulase in Trichoderma $(O_2-1)$ cellulase preparation.

• Microbiology and Biotechnology Letters
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• v.4 no.3
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• pp.105-110
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• 1976

In the studies of microbiological utilization of cellulosic wastes, cellulolytic fungi were isolated and screened out. At the first stage, 221 cellulolytic fungi were isolated from different sources such as soils, humus, composts and rotten wood debris by enrichment culture techniques. In the second stage, 36 strains of fungi out of those previously isolated were selected for their cellulase activities estimated by means of filter paper degradation, carboxy methyl cellulose liquefaction and cup method. Activities of C$_1$-cellulase, C$\sub$x/-cellulase and filter paper activity were adopted on the final screening stage and five different strains which are tentatively identified as Aspergillus sp.(strain No. AS-9), Penicillium sp. (strain No. KNI-1-2), Trichoderma, sp. (strain No. KI-7-2, KI-7-5, KI-4-1-1B) were selected for their high potency of C$_1$ and C$\sub$x/-cellulase activities. When rice straw milled and treated with NH$_4$OH was hydrolyzed with the crude enzyme Prepared from the culture broth of Trichoderma sp. (strain No. KI-4-1-1B), saccharification rate was obtained up to 26％.

• The Korean Journal of Mycology
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• v.1 no.1
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• pp.23-28
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• 1973

The soil of Kwangneung area(Kyeunggi-Do) was inoculated directly into wheat-bran-media and after $3{\sim}4$ days of incubation, a Penicillium species whose cellulase activity was 1011u/g was isolated. With the treatment of mutagenic agents an improved strain(cellulase activity: 1303u/g) was obtained. This strain was screened again by mono-spore isolation method. Finally a strain C8-14 (cellulase activity: 2351u/g) which had lesser spores than the wild strain was obtained.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.347-350
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• 2000

Enzymatic deinking of office-waste paper was studied using crude cellulase and papain-hydrolyzed cellulase from Trichoderma reesei Rut C-30 in small-scale and mid-scale. The results were compared with deinkings using commercial enzyme(Novozym 342) and conventional chemical methods. Maximum brightness and freeness were obtained at 3 units/g Oven Dry Paper(ODP) of CMCase activity using crude cellulase in mid-scale deinking experiments. The deinked pulp had higher physical strength and brightness, and lower freeness and yield than the pulp deinked in small scale. In small scale deinking, maximum brightness and freeness were obtained at 2 unit/g ODP. Deinking by papain-hydrolyzed cellulase showed similar results with one by Novozym 342. It was better in brightness and freeness, but showed lower physical strength and yield, than the conventional deinking by sodium hydroxide. The ratio of endo-1,4-glucanase and exo-1,4-glucanase components in papain hydrolyzed cellulase from T. reesei Rut C-30 was similar to that of commercial enzyme, Novozym 342, implicating a successful application as a deinking enzyme.

• Applied Biological Chemistry
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• v.24 no.4
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• pp.260-266
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• 1981

Some properties of cellulase and xylanase produced from Pleurotus ostreatus 301 and Lentinus edodes 3-1 during its growth in rice straw medium were investigated. The cellulase activities of P. ostreatus 301 and L. edodes 3-1 were increased in proportion to substrate concentration within 0.6% and 0.8%, respectively, and xylanase activities of two strains were increased within 1%. The reducing sugar production of cellulase and xylanase in two strains were proportionaly increased until 30 min. and 60 min. respectively. The opium pH for cellulase activities of P. ostreatus 301 and L. edodes 3-1 were pH 4.0 and pH 4.5, respectively, and xylanase activities of two strains were pH 5.0. The stable pH range for cellulase activities of P. ostreatus 301 was within 4.0 to 6.0 and L. edodes 3-1 was within 3.0 to 5.0, Xylanase activities of P. ostreatus 301 was within 4.5 to 6.0 and L. edodes 3-1 was within 3.5 to 6.0. The optium temperature for cellulase activities of P. ostraeatus 301 and L. edodes 3-1 were $40^{\circ}C$ and $50^{\circ}C$, respectively, but xylanase activities of P. ostreatus 301 and L. edodes 3-1 were $50^{\circ}C$ and $45^{\circ}C$, respectively. Thermal stability of enzymes were below of optimum temperature and these were mostly inactivate at $70^{\circ}C$ for 10 min of the metalic ions tested, cellulase activities of L. edodes 3-1 was increased by $Co^{++},\; Mg^{++}$ at the concentration of $10^{-2}M$, but were greatly inhibited by $Hg^{++},\;Cu^{++}$ in two strains. Xylanase activities were increased by $Ca^{++},\;Co^{++},\;Mg^{++}$ and $Cd^{++}$ but was greatly inhibited by $Hg^{++}$.

• Korean Journal of Microbiology
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• v.25 no.4
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• pp.297-297
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• 1987

A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be 60.deg.C and 6.0, respectively.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.575-580
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• 1998

Cellulase production by batch culture using the Trichoderma reesei Rut C30 strain with various concentrations of Solka Floc with 1 % wheat bran was studied in a 2.5 I fermenter. The cellulase activity increased with Solka Floc concentration up to 5%. When 5% Solka Floc and 1% wheat bran were contained in the medium, carboxymethyl cellulose (CMC) and filter paper (FP) activities were 232.4 U/$m\ell$ and 21.25 U/$m\ell$, respectively. The productivity was 143.6 FPU $1^{-l}h^{-1}$ and the yield was 425 FPU/g. The colonial morphology of T. reesei Rut C30 grown on Avicel agar plates and the changes in mycelial morphology of T. reesei Rut C30 with culture time are also presented.

• Korean Journal of Human Ecology
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• v.9 no.4
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• pp.483-489
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• 2000

The purpose of this study is to verify the effect of cellulase treatment on crease resistance of cotton. Cotton fabrics was treated with cellulase under different concentration at $50^{\circ}C$ for 40 min. Also to compare the effect of DMDHEU treatment, DMDHEU treatment was conducted before and after cellulase treatment, also with cellulase. Weight loss, crease resistance and tentile strength of each samples were measured and compared. Maximum weight loss showed at 1g/l con. with 40 min. treatment. Cellulase enzyme treatment was more effective than DMDHEU in the crease resistance and tensile strength. Crease resistant of cotton which treated under different condition with cellulase and DMDHEU showed in the order of cellulase+DMDHEU> cellulase> DMDHEU treatment. Also, tensile strength showed in the order of cellulase> cellulase+DMDHEU> DMDHEU. Among those treatment conditions, condition which treated with cellulase considered more effective to increase crease resistance while keeping tensile strength too.

• Microbiology and Biotechnology Letters
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• v.31 no.1
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• pp.42-45
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• 2003

A Trichoderma sp. SO-571 producing cellulase was isolated from soil, and a pilot-scale cultivation and separation of cellulase were conducted. The cellulase activity was about 14.5 unit/ml after 112 hr of cultivation in a 301 fermenter containing 3.0% cellulose, 4.0% soybean powder, 3.0% wheat bran, 0.5% ($NH_4$)$_2$$SO_4$0.2% urea, 1.0% CSL, 0.5% $KH_2$PO$_4$, and 0.2% Tween 80. The cellulase was purified over 4.6 folds in three steps with 47.86% yield. The optimum pH of cellulase was pH 5.0 and optimum temperature was $60^{\circ}C$. To investigate the effect of the cellulase-treated cellulosic fabric, the weight loss was compared. The weight loss of denim treated with cellulase from Trichoderma sp.SO-571 was 2.9% and that with Celluclast 1.5L was 2.2%. In tencel treatement with enzyme, cellulase showed 0.7% higer weight loss than that with Celluclast 1.5L.