• Journal of Life Science
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• v.18 no.3
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• pp.323-328
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• 2008

In this study we evaluated the method to develop red ginseng oil containing high content of phytochemicals by enzymes treatment. To select the optimum extraction process of red ginseng with oils, the antioxidant activities of red ginseng using various enzymes were measured. Red ginseng after 0.5% cellulase treatment for 1 hr at $50^{\circ}C$ had higher antioxidant activity than the other conditions. We found that red ginseng/soybean oil extracted for 15 days at $40^{\circ}C$ after 0.5% cellulase treatment increased DPPH radical scavenger activity and decreased the TBA and POV values. However, red ginseng/olive oil had little functional activities compare to the red ginseng/soybean 0il. We also analyzed vitamin A and E by HPLC and found that vitamin E was increased by 0.5% cellulase treatment in the oil. This is the first report that red ginseng oil extracted by enzyme treatment has various beneficial effects.

• Food Science and Preservation
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• v.24 no.1
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• pp.60-67
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• 2017

In this study, we tried to establish the best method for fresh blueberry beverage production using enzyme treatment as well as low temperature extraction. During extraction of physiologically functional materials, we used low temperature to prevent nutritional loss by heat. In addition, we investigated optimal blueberry extraction conditions using various enzyme treatments (cellulase, pectinase, cellulase:pectinase (1:1) mixture) to increase extraction efficiency and reduce turbidity. A variety and ratio of enzymes, extraction temperature, extraction time, and shaking speed were considered for the best extraction efficiency rate. We observed high extraction efficiency rates of 85.72-86.55% and 87.06-87.93%, respectively, upon cellulase or pectinase treatment. In addition, a mixture of cellulase:pectinase (1:1) showed an extraction efficiency rate of 86.84-88.14%. The best extraction efficiency rate was observed when crude blueberry was treated at $45^{\circ}C$ (87.91%), for 3 h (87.88%), in a 90 rpm shaker (89.19%). Sugar content and acidity of blueberry extract were not affected by the various treatments. However, total phenolic compounds were detected upon pectinase treatment (18.62 mg/g). Only fructose and glucose as free sugars were found in all samples regardless of treatments and extraction conditions.

• Asian-Australasian Journal of Animal Sciences
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• v.10 no.6
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• pp.575-580
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• 1997

Two experiments were carried out to evaluate the effects of cellulase and brewers' grains addition on improvement of the fermentation quality and the nutritive value of barley straw silages made from dried or fresh straw. In Exp. I : 1 kg dried barley straw + 2 kg wet brewers' grains + 0 (I-0), 2 (I-2), 4 (I-4), 6 (I-6), and 8 (I-8) g of cellulase. In Exp. II : 2 kg fresh barley straw + 2 kg wet brewers' grains + 0 (II-0), 2 (II-2), 4 (II-4), 6 (II-6), and 8 (II-8) g of cellulase. Each prepared material was ensiled into vinyl bag silos (5 L capacity) and stored for 10 (Exp. I) or 7 (Exp. II) months at $21^{\circ}C$. The fermentation quality and nutritive value of barley straw silages produced were markedly improved by mixing them with wet brewers' grains, on the other hand the effect of cellulase addition on the fermentation and reduction of the cell wall components in the silos at ensiling more effectively occurred at low dry matter silages rather than at the high ones. All silages in both Exp. I and II were found well preserved as indicated by their low pH and high lactic acid concentration. Cellulase treated silages had a lower pH (p<0.05) and a higher lactic acid concentration (p<0.05) than those of without cellulase addition. NDF, ADF, and (Hemi)cellulose contents of cellulase treated silages reduced (p<0.05) compare to those of the corresponding silage without cellulase. Increasing levels of cellulase addition caused an increase in fermentation quality and reduction of cell wall components. In vitro dry mater digestibility was found similar in all silages. Fermentation quality and nutritive value of barley straw silages were improved by both wet brewers' grains and cellulase addition. Cellulase addition reduced the cell wall components silages, but did not improve the digestibility.

• 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.

• Microbiology and Biotechnology Letters
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• v.19 no.4
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• pp.331-336
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• 1991

In order to utilize natural cellulosic materials as a fermentative substrate, saccharification of a various kind of native cellulosic materials was performed by using cellulase from the isolated strain, Pseudomonas sp. LBC-505 which potently produced cellulase complex and xylanase. Cellulase complex production was repressed by the low concentration of glucose, induced by cellulosic compounds such as CMC, wheat bran and rice straw et al. and showed to be highest on the PY-CMC medium containing 5% (w/v) wheat bran instead of CMC. Optimal temperature for enzyme reactions of CMCase and xylanase was $50^{\circ}C$, and $55^{\circ}C$ for $\beta$-glucosidase. Optimal pH for these enzyme reaction was 6.6. Rate of saccharification for natural cellulose was low by the treatment of crude enzyme. Among their substrates, rice straw was the most effective substrate of enzymatic reaction in this work. After treating rice straw with 5% (v/v) HC1 and hydrolysing with crude enzyme, rate of saccharification was 18.4% (w/w) on dry substrate. Sugars of cellulosic hydrolyzate mainly contained glucose, xylose and cellobiose.

• Mycobiology
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• v.39 no.2
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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.

• Asian Journal of Turfgrass Science
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• v.12 no.4
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• pp.211-220
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• 1998

Cellulose-degrading fungi were idenfied as Rhizoctonia solani AG2-2(IV), T. harzianum and C. cochliodes. Rhizoctonia solani AG2-2(IV) grows better in the acidified media of pH 4 and 5 than pH 6 and 7. Mycelial growth of T. harzianum and C. cochliodes was also higher in pH 4 and 5 than in pH 6 and 7. In order to relate the above findings to nutrient utilization, mycelial growth of R. solani AG2-2(IV) are evaluated with various carbon sources. R. solani AG2-2(IV) grows well in the order of mannose, cellobiose, glucose, xylose and arabinose. However, mycelial dry weights of T. harzianum were 98.7, 78.0, 72.3, 43.7 and 32.3mg in glucose, mannose, cellobiose, xylose, and arabinose, respectively. Mycelial dry weight of C. cochilodes was 118, 65, 57, 49, and 16mg in mannose, cellobiose, xylose, glucose, and arabinose, respectively. Result of cellulase assay of R. solani AG2-2(IV) and soil fungi was reffered as, R. solani AG2-2(IV) produced more cellulase on CMC substrate than on CEL and secretes more enzyme in floated condition than in water-immersed condition. T. harzianum secreted less amount of cellulase than R. solani AG2-2 and C. cochliodes. T. harzianum produced no enzyme on CEL under water-immersed condition. C. cochliodes produced similar amounts of cellulase on either CMC or CEL under both water-immersed and floated condition.

• 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.

• Journal of Microbiology and Biotechnology
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• v.10 no.6
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• pp.770-775
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• 2000

Several process parameters were studied to ascertain the effect on degradation of sugar cane bagasse in relation to the production of cellulase enzyme and reducing sugars by Solid Substrate Fermentation (SSF) and Submerged Culture Fermentation (SCF) of Aspergillus terreus SUK-1. The effect of air-flow rate (0-1.3 v/v/m), of different ratios of substrate weight to liquid volume (1:6, 1:10, 1:20, and 1:30 w/v, g/ml), scale-up effect (10, 20, and 100 times of 1:10 ration, w/v) and the effect of temperature (30, 40, 50, and $60^{\circ}C$) in SSF were studied. Air-flow rate of 1.0 v/v/m gave the highest enzyme activity (FPase 0.25 IU/ml, CMCase 1.24 IU/ml) and reducing sugars concentration (0.72 mg/ml). Experiment using 1:10 ratio (w/v) was found to support maximum cellulase activity (FPase 0.58 IU/ml, CMCase 1.97 IU/ml) and reducing sugar concentration (1.23 mg/ml). Scaling-up the ratio of 1:10(w/v) by a factor of 20 gave the highest cellulase activity (FPase 0.71 IU/ml, CMCase 2.25 IU/ml) and reducing sugar concentration (3.67 mg/ml). The optimum temperature for cellulase activity and reducing sugar production was $50^{\circ}C$(FPase 0.792 IU/ml, CMCase 2.25 IU/ml and 3.85 mg/ml for reducing sugar concentration). For SCF, the activity of cellulase enzyme and reducing sugar concentration was found to be lower than that obtained for SSF. The highest cellulase activity obtained in SCF was 50% lower than the highest cellulase activity in SSF, while for reducing sugar concentration, the highest concentration obtained in SCF was 90% lower than that obtained in SSF.

• Journal of Life Science
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• v.22 no.7
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• pp.912-919
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• 2012

A Bacillus sp. strain producing celluase and xylanase was isolated from environmental soil with LB agar plate containing carboxymethylcellulose (CM-cellulose) and beechwood xylan stained with trypan blue as substrates, respectively. Based on the 16S rRNA gene sequence and API 50 CHL test, the strain was identified as B. subtilis and named B. subtilis NC1. The cellulase and xylanase from B. subtilis NC1 exhibited the highest activities for CM-cellulose and beechwood xylan as substrate, respectively, and both enzymes showed the maximum activity at pH 5.0 and $50^{\circ}C$. We cloned and sequenced the genes for cellulase and xylanase from genomic DNA of the B. subtilis NC1 by the shot-gun cloning method. The cloned cellulase and xylanase genes consisted of a 1,500 bp open reading frame (ORF) encoding a 499 amino acid protein with a calculated molecular mass of 55,251 Da and a 1,269 bp ORF encoding a 422 amino acid protein with a calculated molecular mass of 47,423 Da, respectively. The deduced amino acid sequences from the genes of cellulase and xylanase showed high identity with glycosyl hydrolases family (GH) 5 and 30, respectively.