• 한국의류학회지
• /
• 제21권2호
• /
• pp.471-481
• /
• 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.

• 한국생활과학회지
• /
• 제9권4호
• /
• pp.483-489
• /
• 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.

• 미생물학회지
• /
• 제42권4호
• /
• pp.313-318
• /
• 2006

가정에서 제조된 된장으로부터 cellulase 생산균으로 분리된 고온성 WL-12는 형태적 특성, 생화학적 성질 및 16S rRNA의 염기서열에 근거하여 Bacillus licheniformis로 동정되었다. B. licheniformis WL-12의 cellulase 유전자를 클로닝하여 그 염기서열을 결정한 결과 cellulase 유전자(celA)는 517 아미노산으로 구성된 단백질을 코드하며 1,551 뉴클레오티드로 이루어졌다. 아미노산 잔기배열을 분석한 결과 WL-12의 cellulase는 활성영역과 cellulose 결합영역으로 구성되어 있었으며, glycosyl hydrolase (GH) family 5에 속하는 B. licheniformis, B. subtilis와 B. amyloliquefaciens의 cellulase와 높은 상동성을 보였다. 클론된 celA를 발현용 vector에 도입하여 B. subtilis에서 발현시켜 cellulase 최대생산성이 7.0 units/ml에 이르렀다.

• 미생물학회지
• /
• 제14권2호
• /
• pp.75-83
• /
• 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.

• KSBB Journal
• /
• 제13권5호
• /
• pp.593-598
• /
• 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.

• 한국미생물·생명공학회지
• /
• 제15권5호
• /
• pp.346-351
• /
• 1987

Clostridium thermocellum의 cellulase 유전자를 pBR322를 이용하여 Escherichia coli에 cloning하였다. 삽입된 Hind III 분해 DNA 단편의 크기는 약 1. 8kb였으며 이미 알려진 C. themocellum의 cellulase gene과는 다른 제한효소 분해위치를 가진 새로운 cellulase gene으로서 E, coli에서 CMCase와 FPase 활성을 나타내었다. 이 유전자는 생육의 전시기를 통해 표현되었고 고온성 cellulase의 구조적, 기능적 특성이 그대로 유지되었을 뿐만 아니라 상당량이 세포밖으로 분비되었다.

• 한국균학회지
• /
• 제12권2호
• /
• pp.59-64
• /
• 1984

볏짚배지(培地)에서 Pleurotus sajor-caju의 배양조건(培養條件)을 달리하여 섬유소분해효소(纖維素分解酵素) 생산(生産)에 미치는 영향(影響)을 검토(檢討)하여 다음과 같은 결과(結果)를 얻었다. 1) 효소생산(酵素生産)의 최적(最適) 수분함양(水分含量), pH 및 온도(溫度)는 $C_1-cellulase$가 60%, 7.0, $35^{\circ}C$ 이었고 $C_x-cellulase$는 60%, 5.0, $25^{\circ}C$이었으며 ${\beta}-glucosidase$는 60%, 7.0, $20^{\circ}C$이었다. 2) 균사배양기간(菌絲培養期間) 중에 광(光)을 조사(照射)하므로서 $C_1-cellulase$와 ${\beta}-glucosidase$생산(生産)은 감소(減少)하였으나 $C_x-cellulase$는 $500{\sim}1,000\;lux$에서 오히려 증가(增加)되었다. 3) 배양기간(培養期間) 중에 $C_1-cellulase$가 감소(減少)하면 $C_x-cellulase$와 ${\beta}-glucosidase$가 증가(增加)하는 상반관계(相反關係)를 나타내었다. 4) 부원료(副原料) 중에서 $C_1-cellulase$는 미강(米糠), $C_x-cellulase$는 면실박(綿實粕)과 미강(米糠), ${\beta}-glucosidase$는 대두박(大豆粕)과 어분(魚粉)을 첨가(添加)했을 때 가장 양호(良好)했으며 $C_1-cellulase$와 ${\beta}-glucosidase$는 미강(米糠) 20%, $C_x-cellulase$ 10%는 첨가(添加)했을 때 양호(良好)하였다.

• 미생물학회지
• /
• 제13권3호
• /
• pp.85-90
• /
• 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.

• 한국식품영양과학회지
• /
• 제22권3호
• /
• pp.340-348
• /
• 1993

Penicillium funiculosum과 Trichoderma viride cellulase의 정제효소들을 사용하여 cross-synergism을 조사하였다. Exo-exo형 상승작용이 Avicel을 분해하는데 가장 효과적이었으며 exo-endo형은 다소 효과가 떨어졌다. 정제효소성분과 이종의 조효소를 혼합하여 70시간 이상 Avicel을 가수분해하며 생성된 total sugar를 측정한 결과, P. funiculosum cellulase에서 분리정제한 $\beta$-glucosidase 성분효소는 T. viride cellulase와 상승작용을 크게 나타내며 Avicel을 가수분해하였다. 또한, T. viride cellulase에서 분리정제한 exoglucanase 성분효소도 P. funiculosum cellulase의 가수분해능을 크게 향상시켰다. 이와같은 결과로 미루어 볼 때, 이종의 cellulase로 부터 부족한 성분효소를 보충시켜 효소성분비율을 변화시킴으로써 Avicel의 가수분해도를 향상시킬 수 있을 것으로 사료된다. 이 때 최대한 높은 가수분해를 얻기 위하여 여러 형식의 상승작용이 같이 이루어져야할 것이다.

• 한국미생물·생명공학회지
• /
• 제21권6호
• /
• pp.549-555
• /
• 1993

The production of cellulase by Pseudomonas sp. LBC505 isolated was under the strict genetic and biochemical control mechanisms such as catabolit repression and induction. These biochemical control reduced cellulase production. Thus LBC505 was mutated to increase enzyme yields. Cells growth and cellulase production were inhibited by the addition of 2-deoxy glucose (2-DG), which is presumed to function as repressor for the selection of high cellulase yielding mutant.