• Mycobiology
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• 제39권2호
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• pp.103-108
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• 2011

Amylases and cellulases are important enzymes that can be utilized for various biological activities. Ten different wild Nigerian mushrooms (Agaricus blazei, Agaricus sp., Corilopsis occidentalis, Coriolus versicolor, Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, Podoscypha bolleana, Pogonomyces hydnoides, and Nothopanus hygrophanus) were assayed for production of these secondary metabolites. The results revealed that most of the tested wild fungi demonstrated very good amylase and cellulase activities. With the incorporation of carboxymethyl-cellulose (a carbon source) into the culture medium, Agaricus blazei had the highest amylolytic activity of 0.60 unit/mL (at $25^{\circ}C$, pH 6.8). This was followed in order by P. tuber-regium and Agaricus sp. with 0.42 and 0.39 unit/mL, respectively ($p {\leq} 0.05$). Maltose and sucrose supplementation into the submerged liquid medium made N. hygrophanus and P. hydnoides to exhibit very low amylase activities of 0.09 and 0.11 unit/mL, respectively. Introducing peptone (an organic nitrogen source) into the basal medium enhanced the ability of C. versicolor to produce a cellulase value of 0.74 unit/mL. Other organic nitrogen sources that supported good cellulase activities were yeast extract and urea. Sodium nitrate (inorganic nitrogen source) generally inhibited cellulase production in all mushrooms. The best carbon source was carboxymethyl-cellulose, which promoted very high cellulase activity of 0.67 unit/mL in C. versicolor, which was followed in order by P. tuber-regium, T. chypeatus, and C. occidentalis ($p {\leq} 0.05$). Sucrose was the poorest carbon compound, supporting the lowest values of 0.01, 0.01, and 0.14 unit/mL in P. hydnoides, A. blazei, and Agaricus sp., respectively.

• 미생물과산업
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• 제11권1호
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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.

• 미생물학회지
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• 제37권3호
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• pp.214-220
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• 2001

축산 분뇨의 퇴비화에 관련되는 세균들을 분리하고 이들이 생산하는 효소들 중 퇴비화에 관련되는 것으로 사료되는 amylase, cellulase, protease 및 lipase의 특성을 연구하였다. 발효 중에 있는 축산 분뇨로부터 24주의 균주를 분리하여 이중 protease, cellulase, amylase, 그리고 lipase의 활성을 모두 가진 6개의 균주들을 선별하였다. 분리한 6개의 균주들을 동정해본 결과 Corynebacterium varibilis, Bacillus spp., Pseudomonas spinosa, Acetobacter calcoaceticus 및 Athrobacter cumminsii 등으로 밝혀졌다. 이들이 분비하는 효소들의 특징은 중성에서 알칼리성에 이르는 광범위한 pH에서 효소들이 높은 활성을 보였으며, cellulase를 제외한 대부분의 효소들의 최대 활성 온도가 $60^{\circ}C$ 정도 였으나, cellulase의 경우 $37^{\circ}C$가 최적 활성 온도였다. 이는 발효가 진행되어 축산 분뇨에 고온의 열이 발생할 때, 이 환경하에서 유기물을 분해함으로써 발효과정을 원활히 진행시키는 것으로 생각된다. 다만 cellulase 생산 세균의 경우 축산 분뇨의 초기 발효시에 관여하여 균주의 성장 및 유기물의 분해에 관여하는 것으로 사료된다. 이와같은 결과는 축산분뇨 발효초기와 발효후기의 온도가 상승된 환경에서 작용하는 세균의 균총이 다름을 암시하고 있다.

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

• 미생물학회지
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• 제14권2호
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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.

• Journal of Microbiology and Biotechnology
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• 제4권1호
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• pp.49-55
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• 1994

A fungal strain capable of producing extracellular cellulase was isolated from farmland. It was identified as Aspergillus niger, and named Aspergillus niger KKS. Production of cellulase and xylanase by the A. niger KKS was studied through a shake-flask culture. The effects of culture conditions such as inoculum size, temperature, pH, and medium composition on the cellulase and xylanase production were examined. The optimum temperature and pH for the enzyme production were $30^{\circ}C$ and pH 7.0, respectively. The optimized medium was composed of 2.0% (w/v) rice straw, 0.5% (w/v) proteose peptone, 0.5% (w/v) $KH_2 PO_4$, 0.05% (w/v) yeast extract, 0.01% (w/v) $CoSO_4 \cdot 7H_2O$, and 0.05% (w/v) $CuSO$_4$\cdot 5H_2O$. When the strain was incubated with the optimized medium, it gave the activities of endoglucanase, $\beta$-glucosidase, $\beta$-xylosidase, xylanase were 3.80, 4.20, 4.00, 80.0 (IU/mL), respectively. Filter paper and cotton activities were 0.68 and 0.045 (IU/mL), respectively. The results of this study show that A. niger KKS is a potential organism with a wide spectrum of enzyme activities, such as those of $\beta$-glucosidase, $\beta$-xylosidase, and xylanase.

• The Korean Journal of Ecology
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• 제9권4호
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• pp.231-241
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• 1986

The annual decomposition of cellulose and hemicellulose by microorganism and distribution of soil microbial flora were investigated in the humus horizon of a Pinus rigida stand in Mt. Kwanak. The cellulase activity was the lowest, 142$\mu$g glucose/g/hr from Dec. 1985 to Mar. 1986 and the highest, 760~1, 072$\mu$g glucose/g/hr in Jul. and Aug. 1985. The xylanase activity was 47% higher than the cellulase activity and was the lowest, 211~275$\mu$g xylose /g/hr from Feb. to Mar. 1986 and the highest as 799~1, 322$\mu$g xylose/g/hr from Jun. to Aug. 1986. The vertical distribution of the enzyme activity was decreased with the order of F, H, L, and A1 in both enzymes and the activities were exponentially decreased below L horizon, which suggests that most decomposition be done in F and H horizons with lots of organic matters. The SEM study slowed that the main decomposers of litters were fungi and initial attack into litters was also made by them. The enzyme activities of soil had strong correlations with the temperature and the precipitation. The correlation coefficients were 0.813 and 0.886 in the cellulase, and 0.673 and 0.626 in the xylanase for the temperature and the precipitation, respectively.

• 미생물학회지
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• 제14권3호
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• pp.117-127
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• 1976

A cellulase fraction (F IV-1) purified to about 8-folds was obtained from crude cellulase prepared from the wheat bran culture of S.atra. The partial purification of the enzyme was made by DEAE Sephadex and Sephdex cloumn chromatography in conjuction with ammonium sulfate precipitation. After stading at various pH's for 22 hours at $20^{\circ}C$, F IV-1 was most stable at pH 5.0 but when the enzyme fraction was stood for 74 hours, the point of pH stability was raised to around pH 6.0-7.0. After heating at various temperatures for 1 hour, F IV-1 was most stable at $20^{\circ}C$. The optimal enzyme activities of F IV-1 were seen at pH 6.0 and $50^{\circ}C$. The optimal concentrations of $Zn^{++}\;and\;Ca^{++}$ for the activities of crude cellulase were 6 and 4 mM respectively, but $Ca^{++}$ inhibited the enzyme activity at concentrations below 2 mM and above 6mM. Both $Cu^{++}\;and\;Mn^{++}$ ions inhibited cellulase activities and a ocmplete inactivation of crude cellulase was achieved at concentratioins of 5 and 2 mM of ions respectively. When Na-CMC was used as substrate, the Km values of crude cellulase and F IV-1 were calculated to be $5{\times}10^{-4}\;and\;2{\times}10^{-5}mM$, and V values 32 and 1.35 mmoles/hour, respectively. The Ki values of $Mn^{++}$ for crude cellulase and F IV-1 were found to be $8{\times}10^{-2}\;and\;3{\times}10^{-2}\;mM\;while\;those\;of\;Cu^{++}\;were\;at\;2{\times}10^{-1}\;and\;1{\times}10^{-1}\;mM\;respectively.\;Both\;Mn^{++}\;and\;Cu^{++}$ showed competitive inhibition with substrate.

• Journal of Microbiology and Biotechnology
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• 제9권1호
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• pp.44-49
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• 1999

Cellulase production by fed-batch cultivation of Trichoderma reesei Rut C30 with various initial concentrations of Solka Floc in 1 % wheat bran-containing medium was investigated. The cellulase activity and productivity increased with initial Solka Floc concentration up to 5%. When a total Solka Floc concentration of 90 g/l was used for cellulase production, CMC (carboxymethyl cellulose) and FP (filter paper) activities, productivity, and yield were 359.7 U/ml, 30.61 U/ml, 161 FPU $L^{-1}$ $h^{-1}$, and 340 FPU $g^{-1}$, respectively. It was important to maintain a high cell concentration during cellulase production to obtain high cellulase activity and productivity. Cellulase powder was prepared by ammonium sulfate precipitation: FP activity was 396.7 U/g and CMC activity was 6481 U/g.

• Biotechnology and Bioprocess Engineering:BBE
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• 제3권1호
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• pp.44-47
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• 1998

Maximum cellulase production was sought by comparing the activities of the cellulases produced by different Trichoderma reesei strains and Aspergillus niger. Trichoderma reesei Rut-C30 showed higher cellulase activity than other Trichoderma reesei stains and Aspergillus niger that was isolated from soil. By optimizing the cultivation conditions during shake flask culture, higher cellulase production could be achieved. The FP(filter paper) activity of 3.7U/ml and CMCase (Carboxymethylcellulase) activity of 60U/ml were obtained from shake flask culture. When it was grown in 2.5L fermentor, where pH and DO levels are controlled, the enzyme activities were 133.35U/ml (CMCase) and 11.67U/ml(FP), respectively. Ammonium sulfate precipitation method was used to recover enzymes from fermentation broth. The dried cellulase powder showed 3074.9U/g of CMCase activity and 166.7U/g of FP activity with 83.5% CMCase recovery.