• Microbiology and Biotechnology Letters
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• v.30 no.1
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• pp.98-102
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• 2002

Lignocellulosic wastes available in abundance can be excellent substrates for the production of cellulase. Different types of substrates and various pretreatments were used to improve the production of cellulase. The steam-exploded wood chip gave the highest activities of FPase (0.84 IU/mL) and CMCase (6.5 IU/mL) in the shake-flask culture. In 30 L bioreactor the steam-exploded wood chip and residue after saccharification gave the FPase activity (0.72 IU/mL) and the CMCase activity (6.3 IU/mL), respectively, similar those obtained in lactose.

• KSBB Journal
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• v.24 no.1
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• pp.70-74
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• 2009

For continuous culture of cellulolytic enzymes production to saccharify food wastes, refill concentration of Mandel's medium for continuous culture was 0.5%, and refill intervals were determined to 12 hours by analysis of COD and total nitrogen concentration after 4-days batch culture in flask level. As a result, amylase and FPase productivities were 3.5 and 1.0 U/L.hr, respectively. In 10 L bioreactor, the batch culture mode was compared with fed-batch, fill-and-draw for continuous production of cellulolytic enzyme. Enzyme productivities were most high at batch culture and followed by fed-batch culture. Amylase and FPase activities were 42.3 and 5.6 U/L.hr at batch culture, and 23.0, 2.8 U/L.hr at fed-batch culture, respectively. As a result, in continuous cultivation of cellulolytic enzymes by T. inhamatum KSJ1, the mode of fed-batch was most effective in 10 L bioreactor.

• The Korean Journal of Mycology
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• v.26 no.1 s.84
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• pp.127-133
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• 1998

Two regulatory mutants of Trichoderma reesei QM 9414 were isolated by treatment with N-methyl-N'-nitro-N-nitrosoguanidine, and the effects of various inducers on the carboxymethyIcellulose (CMC) and filter paper (FP) production were investigated. Induction of CMCase and FPase production of mutants was shown higher level than wild type strain in 1% lactose minimal broth. When induced by glucose, wild type showed glucose-repression for CMCase and FPase production and mutants showed glucose-derepression. Mutant 1 showed 8.38 fold higher CMCase activity and 5.68 fold higher FPase activity than wild type stain. Mutant 2 showed about 8.42 fold higher CMCase activity and 5.41 fold higher FPase activity than wild type strain. Enzyme activities from the mutants and wild type had the same optimum pH of 4.8 and optimum temperature of $60^{\circ}C$.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.365-369
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• 1989

Thermal inactivation of Tyichoderma viride cellobiohydrolase was investigated by immunoassay and residual enzyme assay such as carboxymethyl cellulase (CMCase) and filter paper degradation activity (FPase). Arrhenius plots of cellobiohydrolase were appeared as straight line. The Z-values of cellobiohydrolase calculated by CMCase, FPase and immunoassay were 5.2$^{\circ}C$, 6.4$^{\circ}C$ and 5.8$^{\circ}C$, respectively. The thermodynamic parameters obtained from FPase were better agreement with those of immunoassay than CMCase assay.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.35 no.1
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• pp.34-40
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• 2003

This study was carried out to select the useful bacteria which secret extracellula enzymes for enzymatic deinking agent of old newspaper. CMCase, FPase and xylanase activities of the bacteria liquid culture were measured at optimal growth conditions. Clear zone test was checked on the solid culture. The results of this study were as follow: Eight strains of 28 bacteria isolated from a paper mill soil ground were shown strong CMCase and xylanase activity with the clear zone test. The optimal pH and temperature for culture growth were 6~8 and 26~$34^{\circ}C$, respectively and optimal culture period were less than 60 hours. Based on CMCase, FPase and xylanase activity, strain No. 18, 21, 22 and 28 which were relatively higher than the other strains, were selected for further enzymatic deinking research.

• 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 $45^{\circ}C$.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.36 no.3
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• pp.9-14
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• 2004

The useful fungi which secret extracellular enzymes was selected for deinking agent of old newsprint. Five fungal strains were isolated from a paper mill soil ground. The CMCase, FPase and xylanase activities of fungi on the liquid culture were investigated at optimal growth conditions. The results of this study were as follow: The optimal pH and temperature for culture growth were 4～8 and 27～$35^{\circ}C$, respectively. For screening of extracellular enzymes at optimal culture conditions the optimal culture period were less than 6-7 days. Fusarium pallidoroseum and Aspergiilus niger which shows relatively higher CMCase, FPase and xylanase activities than the other species were selected for further enzymatic deinking research.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 1999.04b
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• pp.291-295
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• 1999

Coprinus cinereus 2249 that is a kind of basidiomycetes constitutively produced alkaline carboxymethyl cellulase (CMCase), filter paper cellulase (FPase) and xylanase. Crude enzymes prepared with optimal conditions showed higher FPase activity than CMCase activity. The FPase was most active at pH 9 at 50$^{\circ}C$. When applied on deinking of the old newsprint (ONP), it increases the freeness and brightness due to effect of hydrolysis at 0.1% enzyme concentration. Also, The physical properties of deinked pulp were improved.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.29 no.1
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• pp.43-51
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• 1997

The various culture conditions of Trichoderma viride(ATCC 3454) and Phanerochaete chrysosporium(ATCC 26921) with glucose-pepton medium, Mandels medium, YMG medium for wood degradable enzyme were examined. Mycellium of the two species grew profusely on glucose-pepton medium. Maximum fungal growth was observed about 10days. But CMCase, Fpase, laccase activity in the culture medium with glucose-pepton was not detected. When grown in fermenter culture using Mandels medium, Trichoderma viride produced CMCase and Fpase. Its CMCase activity was 0.15 lU/ml and Fpase activity was 0.3 IU/ml within about 4-6days. Phanerochaete chrysosporium grown in a YMG medium gave the best enzyme activity when they were grown under stationary culture with an atmosphere of 100% oxygen. Levels of laccase activity of 3.0 mull were achieved in stationary culture under 100% oxygen. The enzyme condensation by ultrafiltration method caused a 2-fold(cellulase) and 6-fold(laccase) as compared to control activity.

• The Korean Journal of Mycology
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• v.26 no.2 s.85
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• pp.239-245
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• 1998

The feasibility of enzymatic hydrolysis of cellulosic materials is dependent on the cost of cellulase, which is strongly influenced by the selection of proper carbon source in the cellulase production medium. When solka floc was used as a carbon source for the production of cellulase by Trichoderma reesei Rut C-30, a maximum of 53.2 U/ml of CMCase activity (4.8 U/ml of FPase activity) was obtained with a concentration of 1 % of solka floc. The cellulase activity decreased to 50% in the presence of 0.5% of glucose in the medium. The production of cellulase was considerably enhanced when solka floc and wheat bran were used together as a carbon source. A medium which contained 1 % of solka floc and 3 % of wheat bran yielded highest cellulase activity: CMCase activity of 76 U/ml and FPase activity of 12.5 U/ml.