• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.31 no.3
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• pp.68-76
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• 1999

Coprinus cinereus 2249 producing alkaline-active cellulase was screened from 29 species of Corpinaceae and constitutively produced alkaline carboxymethyl cellulase (CMCase) and filter paper cellulase (Fpase). When cultivated at pH 9.0, 25$^{\circ}C$ and 5 days, copnnus cinereus 2249 produced higher alkaline activity on 0.5% CMC, 2% wheat bran as carbon source and 0.5% peptone, 0.05% yeast extract as nitrongen source compared with other culture conditions. The level of cellulase production was higher in the presence of wheat bran than in the presence of CMC. The optimum temperature and pH for alkaline -active cellulase activity weas 50$^{\circ}C$ and 9, 0, respectively.

• 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.

• Korean Journal of Agricultural Science
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• v.3 no.2
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• pp.235-243
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• 1976

As an investigation on the catabolite repression system in cellulase production by Cellulomons sp. CS1-1, the organism was tested on the avicel overlay plates containing glucose or cellobiose at a range of concentration and was grown in continuous culture vessel, supplied by cellobiose medium, aiming the enhanced production of extracellular CM-cellulase at low dilution rates. Product inhibition of cellulase action by cellobiose was also tested. The results obtained are: i) no inhibition of CM-cellulase was observed up to 10 mM(3.4mg/ml) cellobiose in the reaction mixture, however 30% inhibition was observed at 20mM and 55% at 50mM, ii) the tests of catabolite repression on the solid media were successful, and avicel degradation was markedly repressed by glucose or cellobiose, iii) at low concentrations of cellobiose, dilution rate 0.05 and $1.0hour^{-1}$, no significant increase was observed in the production of either intra or extracellular CM-cellulase.

• Journal of Microbiology and Biotechnology
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• v.22 no.11
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• pp.1501-1509
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• 2012

A novel bacterial strain, MG7, with high cellulase activity was isolated and identified by morphological characteristics and molecular phylogeny analysis as Paenibacillus barcinonensis. Maximum production of cellulase by MG7 was observed at pH 7.0 and $35^{\circ}C$. The enzyme was purified with a specific activity of 16.88 U/mg, the cellulase activity was observed in a zymogram, and its molecular mass (58.6 kDa) was confirmed by SDS-PAGE. The purified enzyme showed maximum activity at pH 6.0 and $65^{\circ}C$ and degraded cellulosic substrates such as carboxy methyl cellulose (CMC), Avicel, filter paper, and ${\beta}$-glucan. The enzyme showed stability with 0.5% concentration of various surfactants. The $K_m$ and $V_{max}$ of cellulase for CMC and Avicel were found to be 0.459mg/ml and 10.46mg/ml/h, and 1.01 mg/ml and 10.0 mg/ml/h, respectively. The high catalytic activity and its stability to temperature, pH, surfactants, and metal ions indicated that the cellulase enzyme by MG7 is a good candidate for biotechnological applications.

• KSBB Journal
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• v.29 no.4
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• pp.239-243
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• 2014

Recently, there is a growing interest in efficient biomass pretreatment and saccharification processes to produce biofuels and biochemicals from renewable non-food biomass resources. In this study, glucose was produced from cellulose by immobilizing cellulase enzyme on chitosan beads which was reported to have high pH and temperature stability. The immobilized amounts of cellulase on chitosan beads linearly increased with increasing the concentrations of cellulase solution. The glucose production increased to 7.2 g/L from 1% carboxymethyl cellulose (CMC) substrate when immobilized at 20% cellulase solution. The maximum specific activity was 0.37 unit/mg protein when immobilized at 8% cellulase solution. At pH 7 and $37^{\circ}C$, the optimum reaction composition was 0.5 g beads/L from 1% CMC substrate. At this condition, the conversion to glucose completed at ca. 20 min.

• Journal of Life Science
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• v.25 no.6
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• pp.680-685
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• 2015

Previously, cellulase and xylanase producing microorganism, Bacillus subtilis NC1, was isolated from soil. Based on the 16S rRNA gene sequence and API 50 CHL test the strain was identified as Bacillus subtilis, and named as B. subtilis NC1. We cloned and sequenced the genes for cellulase and xylanase. Plus, the deduced amino acid sequences from the genes of cellulase and xylanase were determined and were also identified as glycosyl hydrolases family (GH) 5 and 30, respectively. In this study to optimize the medium parameters for cellulase production by B. subtilis NC1 the RSM (response surface methodology) based on CCD (central composite design) model was performed. Three factors, tryptone, yeast extract, and NaCl, for N or C source were investigated. The cellulase activity was measured with a carboxylmethyl cellulose (CMC) plate and the 3,5-dinitrosalicylic acid (DNS) methods. The coefficient of determination (R²) for the model was 0.960, and the probability value (p=0.0001) of the regression model was highly significant. Based on the RSM, the optimum conditions for cellulase production by B. subtilis NC1 were predicted to be tryptone of 2.5%, yeast extract of 0.5%, and NaCl of 1.0%. Through the model verification, cellulase activity of Bacillus subtilis NC1 increased from 0.5 to 0.62 U/ml (24%) compared to the original medium.

• Korean Journal of Microbiology
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• v.9 no.1
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• pp.32-38
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• 1971

In solid culture of Endomycopsis fibuliger No.55, Eudomuopsis javanensis No.112 and Candida tropicalis No.340, the conditions of enzyme (protease, anylase and cellulase) production and the influence of addition of $(NH_4)_2;SO_4$ were examined, and the results obtained were as follows. 10 Wheat bran medium is found to be the best on the enzyme production in case of simple material. The optimum conditions ; are water content added 100 to 120%, temperature 25 to $80^{\circ}C$ and incubation times 2 to 3 days. 2) The cellulase production was scarely produced in the case of Endomyopsis fibuliger No.55, as well as, the amylase production was scarely producted in the case of Endomycopsis javanensis No.112 and Candida tropicalis No.340. 3) The enzyme production was remarkably increased when 5% of$(NH_4)_2;SO_4$ as inorganic nitrogen sources was admixed to wheat bran. 4) When 5% of $(NH_4)_2;SO_4$ was admixed to medium, the ratio of protein increase was 10.2 to 17.7% in wheat bran medium and 10.6 to 17.9% in sweet potato cake medium.

• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.229-233
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• 2001

Trichoderma reesei Rut C-30 produced high levels of ${\beta}$-glucosidase, endo-${\beta}$-glucosidase, endo-${\beta}$-1,4-glucanase, and exo-${\beta}$-1,4-glucanase. In pilot-scale production (50-1 fermentor), productivity and yield of CMCase (carborymethyl cellulose) and FPase (filter paper activity) were 273 U/ml and 35 U/ml, and 162 FPU/l.h and 437 FPU/g, respectively. The fed-batch techniques were used to improve enzyme activities with constant cell concentration. The acidity was an important parameter and controlled at pH 3.9 and 5.0 by automatic addition of ammonium hydroxide. Cellulase powder was prepared by ammonium sulfate precipitation and its CMCase and FPase activities were 3,631 U/g and 407 U/g, respectively.

• 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.

• Journal of Microbiology and Biotechnology
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• v.25 no.7
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• pp.1101-1107
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• 2015

The role of CRE1 in a thermophilic fungus, Myceliophthora thermophila ATCC42464, was studied using RNA interference. In the cre1-silenced strain C88, the filter paper hydrolyzing activity and β-1,4-endoglucanase activity were 3.76-, and 1.31-fold higher, respectively, than those in the parental strain when the strains were cultured in inducing medium for 6 days. The activities of β-1,4-exoglucanase and cellobiase were 2.64-, and 5.59-fold higher, respectively, than those in the parental strain when the strains were cultured for 5 days. Quantitative reverse-transcription polymerase chain reaction showed that the gene expression of egl3, cbh1, and cbh2 was significantly increased in transformant C88 compared with the wild-type strain. Therefore, our findings suggest the feasibility of improving cellulase production by modifying the regulator expression, and an attractive approach to increasing the total cellulase productivity in thermophilic fungi.