• Textile Coloration and Finishing
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• v.13 no.1
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• pp.9-17
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• 2001

The purpose of this study is to present basic data for the enzymatic modification of acetate fabrics. The weight loss and rate of weight loss of acetate fabrics increased with increasing NaOH concentration and treating time. Acetyl value decreased as the weight loss became higher. The weight loss of alkaline-treated acetate fabrics were directly proportional to the concentration and treating time of cellulase. The optimum temperature and pH in cellulase treatment were $55^\circ{C}$ and pH 3.5. The surface shape revealed that density of fiber decreased by alkaline-treatment. With the treating time of cellulase, fibrillation occurred. In case of higher weight loss in alkaline treatment, fibril is removed after 180 min. The tensile strength decreased by alkaline and cellulase treatment. Especially, in case of higher weight loss of alkaline treatment, tensile strength decreased suddenly. Alkaline treatment increased the drapability of acetates, while cellulase treatment increased it initially but decreased gradually with treatment time. The dyeability after alkaline treatment was improved for reactive dye, but deteriorated for disperse dye. The cellulase treatment of acetate lowered the dyeability for both types of dyes.

• Textile Coloration and Finishing
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• v.8 no.3
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• pp.59-65
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• 1996

Cotton fabrics were treated by low temperature plasma and/or cellulase, and its physical and dyeing properties were investigated. All the pretreatments of the cotton with low temperature plasma of oxygen, nitrogen and argon slowed down the rate of weight loss of cotton in cellulase solution. Plasma pretreatment did not show any strength retention effect on cotton fiber in the subsequent cellulase treatment. Pretreatment of cotton with low temperature oxygen plasma decreased the rate of dyeing in direct dye bath, while cellulase or plasma/cellulase pretreatment increased the rate. Equilibrium dye uptake of cotton was not changed greatly by the pretreatments except the normal untreated cotton showed more or less high uptake. The pretreatment of cellulase with a water-soluble carbodiimide reduced the enzymatic activity, and did not show any strength retention of cotton in enzymatic weight loss.

• Mycobiology
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• v.37 no.4
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• pp.267-271
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• 2009

A fungal strain producing a high level of cellulase was selected from 320 fungal isolates and identified as Aspergillus sp. This strain was further improved for cellulase production by sequential treatments by two repeated rounds of $\gamma$-irradiation of $Co^{60}$, ultraviolet treatment and four repeated rounds of treatment with N-methyl-N'-nitro-N-nitrosoguanidine. The best mutant strain, Aspergillus sp. XTG-4, was selected after screening and the activities of carboxymethyl cellulase, filter paper cellulase and $\beta$-glucosidase of the cellulase were improved by 2.03-, 3.20-, and 1.80-fold, respectively, when compared to the wild type strain. After being subcultured 19 times, the enzyme production of the mutant Aspergillus sp. XTG-4s was stable.

• The Microorganisms and Industry
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• v.11 no.1
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• pp.21-33
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• 1985

이글은 다음과 같이 구성되어져 있다. preface 1) introduction 2) general information 3) folin protein determination 4) cellobiase assay 5) filter paper assay for saccharifying cellulase 6) carboxymethyl cellulase assay for endo-.betha.-1,4-glucanase 7) additional assay procedure for endoglucanase 8) evalutaiton of cellulase under process conditions 9) general remartks, references.

• Journal of Plant Biology
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• v.37 no.4
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• pp.435-439
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• 1994

채종 후 성숙한 인삼 종자 배유에서 cellulase의 국재를 rabbit anti-cellulase와 protein A-gold를 사용한 면역세포화학적 방법을 이용하여 확인하였다. Cellulase의 immunogold particle이 전자밀도가 높은 단백질체와 배유세포벽 주변부에 나타났다. 또한 금입자가 세포벽에 균일하게 분포하였고, 제형층에 접한 분해과정 중의 배유세포벽을 따라 나타났다. 그러나 세포벽의 섬유성 물질과 배유세포의 분해물질로 구성된 제형층에서는 금입자가 관찰되지 않았다.

• KSBB Journal
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• v.22 no.1
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• pp.16-21
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• 2007

Although Energy demands of modern society increase rapidly, current energy would be exhausted shortly. Therefore development of bio-ethanol production process from cellulose containing materials was extremly demanded. Therefore development of highly functional cellulase is requisite for this purpose. In this study cellobio-hydrolase (CBH1) gene from Trichorderma reesei was used to increase cellulase activity by directed evolution and highly functional cellobio-hydrolase was obtained and characterized.

• Applied Biological Chemistry
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• v.38 no.4
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• pp.313-319
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• 1995

The involvement of the cell-wall degrading enzymes in Rhizobium has long been an unsolved question about the infection process in the formation of root nodule. To assess the contribution of the cellulase to the nodulation of rhzobia, here we report the production of cellulase from R. meliloti TAL1372 which degrade carboxymethylcellulose (CMC) model substrate with CMC-plate method. We constructed a genomic library by cloning Sau3A-digested genomic DNA from R. meliloti TAL1372 into the BamHI site of the cosmid vector pLAFR3. Out of more than one thousand transductants of E. coli, one clone (pRC8-71) had CM-cellulase activity and contained pLAFR3 cosmid with 30 kb insert of R. meliloti DNA The product of CM-cellulase gene was analyzed by native PAGE. About 45 kD protein was considered to be a product of the gene. Tn5 mutagenesis reveals that the structural gene located in a ca. 3 kb KpnI fragment. The cellulase-minus mutants of R. meliloti TAL1372 were obtained by Tn5 mutagenesis of pRC8-71 and marker exchange techniques. Analyses of the nodulation ability of these Tn5 mutants showed that the CM-cellulase gene of R. meliloti TAL1372 may be involved in early nodulation development on alfalfa (Medicago satiua).

• Journal of Animal Science and Technology
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• v.50 no.3
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• pp.429-436
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• 2008

A bacterium producing cold-active cellulase and xylanase was isolated from pig feces. The isolate, DK42 strain, was found to be the Gram-positive, non-motile, catalase-positive, and spore-forming stain. Under an electron microscope, the cells were observed to be rod-shaped. The isolate was identified as Bacillus licheniformis DK42 on the basis of morphological and biochemical properties as well as 16S rRNA gene sequences. The characterization of crude cellulase and xylanase from B. licheniformis DK42 was investigated. Cellulase exhibited an optimum temperature and pH at 45℃ and 6.0, whereas xylanase exhibited an optimum temperature and pH at 55℃ and 6.0. Especially cellulase maintained approx. 50% of its maximum activity even at 10℃, indicating that it is cold-active. Both cellulase and xylanase were stable after 2hr at 35℃, whereas they lost their activities after 30min at 65℃.

• Asian-Australasian Journal of Animal Sciences
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• v.12 no.4
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• pp.531-536
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• 1999

This study was conducted to compare the effects of lactic acid bacteria (LAB) or LAB+cellulases on the cell wall compositions and the in vitro dry matter digestibility (IVDMD) of Rhodesgrass (RG) and Italian ryegrass (IRG) silages. LAB (Lactobacillus cassei) at a concentration of $10{\times}10^5\;cfu.g^{-1}$ fresh forage was added to all ensiling samples (except the untreated control) of RG and IRG. The cellulases used were Acremoniumcellulase (A), Meicelase (M) or a mixture of both (AM). Each cellulase was applied at levels of 0.005, 0.01 and 0.02 % fresh sample. The samples were incubated at 20, 30 and $40^{\circ}C$ for about 2 months of storage. LAB inoculation did not affect cell wall components or IVDMD of both the RG and IRG silages, but LAB+cellulase treatments did. Increasing the amount of cellulase addition resulted in further decreases of cell wall concentrations. This reduction more markedly occurred with cellulases A and AM than it did with cellulase M. Cell wall components losses were higher in the IRG silages than in the RG silages. LAB+cellulase treatments decreased IVDMD of the RG silages, but had no effect on the IRG silages. The different effect of LAB+cellulase treatments on cell wall degradation and IVDMD of the RG and IRG silages suggested that RG contains more structural carbohydrates, which were difficult to degrade with cellulase, than did IRG.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.499-503
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• 2003

In the study, we have obtained modified cellulase with higher cellulose degradation activity by molecular evolution method. Cellobiohydrolase(CBH I ) gene of Trichorderma reerri has been used. Cellulase mutant 228-G2 was selected and the activity of cellulase mutant 228-G2 was increased by 300% compared to original CBH I The 17 among 1542bases were found to be modified with mutant 228-G2.