• Title, Summary, Keyword: Cellulase

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The Effect of Cellulase Treatment on the Crease Resistance of Cotton (Cellulase처리가 면직물의 방추성에 미치는 영향)

  • Song, Kyung-Hun
    • 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.

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The Washing Finish of Blue Jeans(I) - the comparison of neutral cellulase, acid cellulase, stone, and stone-neutral cellulase washings - (청바지의 세탁가공에 관한 연구(I) -세탁가공의 종류를 중심으로-)

  • 신혜원;유효선
    • Journal of the Korean Society of Clothing and Textiles
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    • v.21 no.2
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    • pp.471-481
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    • 1997
  • Denims were treated with neutral cellulase, acid cellulase, stone, and stone-neutral cellulase respectively at different cellulase concentrations varying treatment times in rotary washer. The effect of washing on denim was estimated by the changes in weight, color, back staining, tear strength, flex stiffness, and surface characteristics. Also the comparison of neutral cellulase, acid cellulase, stone, and stone-neutral cellulase washings was studied. Washing removes surface fibers and provides weight loss, color difference, back staining, and a decrease in tear strength and in flex stiffness. Stone-neutral cellulase washing and acid cellulase washing have a larger washing effect than neutral cellulase washing and stone washing.

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Cloning and Expression of A Bacillus licheniformis Cellulase Gene (Bacillus licheniformis WL-12의 cellulase 유전자 클로닝과 발현)

  • Yoon, Ki-Hong
    • Korean Journal of Microbiology
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    • v.42 no.4
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    • pp.313-318
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    • 2006
  • A thermophilic bacterium producing the extracellular cellulase was isolated from soybean paste, and the isolate WL-12 has been identified as Bacillus licheniformis on the basis on its 16S rRNA sequence, morphology and biochemical properties. A gene encoding the cellulase of B. licheniformis WL-12 was cloned and its nucleotide sequence was determined. This cellulase gene, designated celA, consisted of 1,551 nucleotides, encoding a polypeptide of 517 amino acid residues. The gene product contained catalytic domain and cellulose binding domain. The deduced amino acid sequence was highly homologous to those of cellulases of B. licheniformis, B. subtilis and B. amytoliquefaciens belonging to the glycosyl hydrolase family 5. When the celA gene was highly expressed using a strong B. subtilis promoter, the extracellular cellulase was produced up to 7.0 units/ml in B. subtilis WB700.

Influence of some Metal Ions on the Cellulase Activity (Cellulase 활성에 대한 몇가지 금속이온의 영향)

  • 최명자;김영민;김은수
    • Korean Journal of Microbiology
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    • v.14 no.2
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    • pp.75-83
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    • 1976
  • Three conmmercial cellulases prepared from Penicillium notatum(cellulalse[K]), Trichoderma viride(cellulase[J]) and Aspergillus niger(cellulase[A]) were nalyzed with respect to their relative purity, activity and the effects of several metal ions on their activities. The activity of cellulase[K] was the strongest of all and that of cellulase[A] being the weaker. The purity of cellulalse[K] was the highest while that of cellulase[J] was the lowest. Under the assay conditions, the optimum concentrations of $Zn^{++}$ and $Mg^{++}$ ions for the activity of cellulase[K] was the highest while that of cellulase[J] was the lowest. Under the assay conditions, the optimum concentrations of $Zn^{++}$ and $Mg^{++}$ ions for the activity of cellulalse[K] was the highest while that of cellulase [A] being weaker. The purity of cellulase[K] was the highest while that of cellulase[J] was the lowest. Under the assay conditions, the optimum concentrations of $Zn^{++}$ and $MG^{++}$ ions for the activity of cellulase[K] were 2 and 7mM while those of cellulase[A] were 5 and 6 mM respectively and those of cellulase[J] were 3mM for both ions. Cellulase[K] and cellulase[J] were more strongly activated by $Zn^{++}$ than $Mg^{++}$ and cellulase[J] by $Mg^{++}$ than $Zn^{++}$. Both $Cu^{++}$ and $Mn^{++}$ ions inhibited by these metal ions. the inhibitory effects of $Mn^{++}$ ions for enzyme activities were stronger than $Cu^{++}$ ions. The Ki values of $Cu^{++}$ and $Mn^{++}$ for cellulase[K] were found to be 6.1 and 0.7mM, those of cellulase[J] were 2.6 and 0.32 mM, and those of cellulalse[A] were 2.0 and 0.2 mM respectively. Both $Cu^{++}$ and $Mn^{++}$ ions showed a pattrn of competitive inhibition of the enzyme activity. When Na-CMC was used as substrate, the Km and V values of celluase [K] were calculated to be $2.0{\times}10^{-4}mM$ and 3.43mmoles/hour, those of cellulase[J] were $2.4{\times}10^{-4}mM$ and 3.77mmoles/hour, and those of cellulase[A] were $4.0{\times}10^{-4}mM$ and 4.00mmoles/hour respectively.

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Cloning and Expression in Escherichia coli of a Cellulase Gene from Clostridium thermocellum (Clostridium thermocellum의 Cellulase 유전자의 Cloning)

  • 하지홍;한성숙;김욱한;이용현
    • 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.

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Autohydrolysis and Enzymatic Saccharification of Lignocellulosic Materials(III) - Recycling and Reutilization of Cellulase Enzyme - (목질 재료의 자기가수분해 및 효소당화에 관한 연구 (Ⅲ) - Cellulase 효소의 회수 및 재사용 -)

  • Cho, Nam-Seok
    • Journal of the Korean Wood Science and Technology
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    • v.17 no.3
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    • pp.45-51
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    • 1989
  • A major problem in the enzymatic hydrolysis of lignocellulosic substrates is the very strong bonding of cellulase to lignin and even cellulose in the hydrolysis residues. This phenomenon inhibits recycle of the cellulase which is a major expense of the enzymatic hydrolysis process. In this paper, autohydrolyzed wood was delignified by two-stage with a 0.3% Na OH extraction and oxygen-alkali bleaching and was subjected to enzymatic hydrolysis with cellulase. Also, an improved almost quantitative recycle process of cellulase enzyme was discussed. In enzyme recovery by affinity method. the first recycling showed relatively high hydrolysis rate of 97.4%. Even at the third recycle. hydrolysis rate was 86.7 percents. In the case of cellulase recovery by ultrafiltration method, first 2 recycling treatments resulted very high hydrolysis rate(97.0-97.7%). Even the third recycling showed about 94.2%. Authoydrolysis of oak wood followed by 2-stage delignification with alkali and oxygen-alkali produced a substrate for enzymatic hydrolysis that allowed almost quantitative recycle of cellulase.

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Deinking of Used Paper by Modified Cellulase with Polymer (고분자 가공 셀룰라아제에 의한 고지의 탈묵에 관한 연구)

  • 박진원;박귀남;이주한;이병준
    • KSBB Journal
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    • v.13 no.5
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    • pp.593-598
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    • 1998
  • Biological deinking process of used papers was studied by the polymer modified cellulase. Cellulase was modified with copolymers which consist of polyoxyethylene derivative and maleic anhydride(MA). The MA functional groups of copolymer can react with amino acids groups of the cellulase without much loss of activity. Modified degree of amino acids was controlled by the added copolymer. The maximum modified degree was about 60% and it was obtained when the weight ratio of copolymer and cellulase was 4. The remained activity of the maximum modified cellulase(MMC) was higher than 80% of native cellulase. The MMC's concentration was 0.05-2.0 wt% relative to the dry paper. In mechanical pulping process, cellulase enhanced the detachment of the ink particle from the used paper by partial hydrolysis of the fiber. The polyoxyethylene of modified cellulase produced the forms which can float the separated ink particle. Compared to the convention deinking method with NaOH or organic chemicals, the new biological deinnking process improved the physical properties such as freeness, tearing strength and whiteness.

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Studies on the Enzymes Produced by Pleurotus sajor-caju(I) -The Production of Cellulolytic Enzymes- (Pleurotus sajo-caju가 생산(生産)하는 효소(酵素)에 관한 연구(硏究)(I) -섬유소(纖維素) 분해(分解) 효소(酵素)의 생산(生産)에 관하여-)

  • Hong, Jae-Sik;Uhm, Tai-Boong;Jung, Gi-Tae;Lee, Kang-Bae
    • 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 ${\beta}-glucosidase$.

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Investigation of the Hydrolysis of Polysaccharides by Crude Cellulases prepared from Several Species of Fungi (몇 종류의 곰팡이에서 분리되는 Crude Cellulase의 다당류 분해능력의 조사)

  • 김은수;김영민;이인규;최태주
    • 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.

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Cross-Synergistic Interactions between Trichoderma viride and Penicillium funiculosum Cellulase (Trichoderma viride와 Penicillium funiculosum Cellulase 성분효소 간의 상승작용에 관한 연구)

  • Hong, Jeong-Hwa
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.22 no.3
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    • pp.340-348
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    • 1993
  • Cross-synergistic interactions were evaluated with purified enzymes from Trichoderma viride and Penicillium funiculosum cellulase. Different synergistic patterns between enzyme components were observed. Exo-exo type synergism was found to be the most effective for degrading Avicel in all cases. Exo-endo type synergism was found to be slightly less effective. Extended hydrolysis of Avicel was carried out using mixtures of purified enzyme components with the crude cellulase from a different source. Addition of $\beta$-glucosidase from P. funiculosum cellulase to T. viride cellulase provided the great enhancement of Avicel hydrolysis. In addition, exoglucanase from T. viride cellulase was found to enhance P. funiculosum cellulase in degradation of Avicel. In conclusion, it was possible to enhance the hydrolysis of Avicel by altering the proportions of enzyme components by supplementing enzyme components from a different source. Different types of synergisms acted together to achieve maximum conversion.

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