• 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.

• Korean Journal of Food Science and Technology
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• v.30 no.2
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• pp.245-252
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• 1998

The chitosanolytic capabilities of cellulases, glucosidases, proteases and commercial enzymes were evaluated, and effective chitosanolytic cellulases from T. viride, T. reesei and Celluclast, a commercial enzyme from T. reesei were characterized. The reaction of cellulase from T. viride, T. reesei and Celluclast was optimal at pH 5. 0 and $45{\sim}55^{\circ}C$. Max. chitosanolytic activities of cellulases from both T. viride and T. reesei were observed at the enzyme/chitosan ratio=0.1 and chitosan concentration=3.0%. For the possible application of commercial Celluclast to chitosan oligosaccharides production, 3%(w/v) chitosan was reacted with 1%(v/v) Celluclast at pH 5.0 and $55^{\circ}C$. The apparent viscosity decreased by 98% within 30 minutes reaction and Max. contents of 50% EtOH solubles were 70% at 15 hrs reaction. Total reducing sugars were also increased with reaction time and maintained approx. 13.5% after 2hrs reaction. In 15 hrs treated chitosan hydrolyzates, various kinds of chitosan oligosaccharides were produced and contents of chitosan hexamer, known for its antitumor activities, were about 8.0%, about 4 times higher values compared with acid hydrolysis method. The results suggested that chitosan oligosaccharides could be produced with low-cost cellulases from T. reesei.

• Journal of Marine Bioscience and Biotechnology
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• v.2 no.2
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• pp.108-112
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• 2007

A cellulase (endo-${\beta}$-1,4-D-glucanase(E.C.3.2.1.4)) was isolated from the hepatopancreas of abalone Haliotis discus hannai by EST analysis. The abalone cellulase named HdEG compassed 1977 bp, including 195 bp in the 5'untranslated region, 1680 bp in the open reading frame which encodes 560 amino acid residues, and 92 bp in the 3'-untranslated region. The C-terminal region of the HdEG showed 44-52% identity to the catalytic domains of glycoside hydrolase family 9 (GHF9)-cellulases from arthropods and bacteria. The recombinant cellulase, pEHdEG was produced in E. coli with being fused with C-terminal His-tag. The expressed protein showed a single band (~62 kDa) on Western blotting which was consistent with the value (61,878 Da) calculated from the DNA sequence.

• 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.

• The Korean Journal of Mycology
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• v.21 no.1
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• pp.28-37
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• 1993

An endo-type cellulase, carboxymethyl cellulase(CMCase) IV, was purified from culture filtrate of cellulolytic fungus Penicillium verruculosum. The CMCase IV was acidic glycoprotein having carbohydrate of 13% as glucose and pI value of 4.0. The CMCase IV was 52 KDa of molecular weight in SDS-polyacrylamide gel electrophoresis and have optimum temperature and pH of $50^{\circ}C$ and 5.0 for enzyme activity. The CMCase IV liberated glucose and cellobiose as major products of the enzyme against carboxymethyl cellulose(CMC) and seemed to has transglycosylation activity simultaneously. Cellulase activity staining(zymogram) showed that the cellulase components of P. verruculosum were not aggregated in the medium. P. vrttuculosum mRNA was translated in vitro and translation product by the mRNA coding for CMCase IV was identified by immunoprecipitation.

• The Korean Journal of Mycology
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• v.24 no.2 s.77
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• pp.149-154
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• 1996

Effects of various kinds of sawdusts, supplements and culture conditions on activities of several enzymes such as protease, phenoloxidase and cellulase produced from mycelium of P. ostreatus grown on sawdust medium were studied and the results are as follows; Higher specific activity of these enzymes was observed when oak tree sawdust and poplar tree sawdust were supplemented with rice bran or wheat bran at rate of 30%, 20% and 10% in total volume respectively. Higher total activities of protease, phenoloxidase and cellulase were observed at 70% of the moisture contents of culture media, while lower activity of these enzymes was observed with 40% moisture contents of sawdust culture medium. The pH 4 and 9 of the sawdust media appeared to be optimum pH for the. production of protease while pH 5 and 7 were optimal for the production of phenoloxidase. The pH 6 of the sawdust medium was optimal for the production of cellulase. The optimum incubating temperature for the production of protease, phenoloxidase and cellulase was $25^{\circ}C$. Higher total activities of protease and phenoloxidase were observed when culture medium was added with wood vinegar at the control, and 0.5% for cellulase.

• Journal of Life Science
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• v.17 no.7 s.87
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• pp.983-989
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• 2007

Bacillus lichemiformis Kll, a plant growth promoting rhizobacterium was reported as a producer of auxin, siderophore, as well as antifungal cellulase under some culture conditions. In vitro test, B. licheniformis Kll represented excellent antagonistic ability against Fusarium oxyspoum (KACC 40037), and showed broad spectrum against other phytopathogenic fungi. B. licheniformis Kll had cellulolytic activity toward not only carboxymethyl-cellulose (CMC) but also insoluble cellulose, such as fungal cell wall cellulose, filter paper (Whatman No. 1), and Avicel. In addition, we confirmed antifungal substance production by butanol-extract methods. The strain produced optimally the antifungal substance when it was cultivated at pH 9.0, 30${\circ}$C for 4 days on nutrient medium. The biological control mechanisms of B. lichemiformis Kll were caused by antifungal substance, cellulase and siderophore against phytopathogenic fungi.

• Korean Journal of Microbiology
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• v.23 no.1
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• pp.25-33
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• 1985

The cell-free cellulolytic enzyme was separated into 3 different enzyme proteins by gel-filtration and ion-exchange chromatography. These fractions were named enzyme A, enzyme B and enzyme C. The mode of action of each of the separated enzymes on crystalline cellulose was examined using infrared spectroscopy and X-ray crystallography. It was concluded that enzyme B is of the $C_1-type$ and reduces the crystallinity of the subatrate by generation an unstable glucopyranose ring structure, whilst enzymes A and C are of the $C_x-type$ and hydrolyse the reaction product of enzyme B to constituent sugars. A reaction scheme for this cellulase system is proposed and discussed.

• Korean Journal of Microbiology
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• v.25 no.4
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• pp.297-297
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• 1987

A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be 60.deg.C and 6.0, respectively.

• Journal of the Korean Society of Tobacco Science
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• v.7 no.1
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• pp.75-84
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• 1985

A strain of Trichoderm sp. J-30 which strongly products cellulase to reduce the content of cellulose in the stem of leaf tobacco was isolated from leaf tobaco. The Trichoderma sp. J-30 was identified as Trochoderma voride. The cellulase from this strain was purified with the physico-chemical methods and treated in the culled stem of leaf tobacco. The results obtained were summarized as follows. 1. Optimal pH of the enzyme was at pH 5.0. 2. The enzyme shooed a higher activity at $40^{\circ}C$ and its thermal stability began to decrease at $60^{\circ}C$. 3. The enzyme activity was promoted by the metal ions such as $Ca^{2+}, Mg^{2+}, Pb^{2+}and\;Zn^{2+}.$ 4. When the culled stem of leaf tobacco was applied with the 3% of the enzyme solution at $40^{\circ}C$ for 3 days. 15 to 17% of cellulose contents decreased, 12 to 13% of total sugar increased and the filling power was increased by 10-13% in the sample.