• Journal of Microbiology and Biotechnology
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• v.7 no.5
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• pp.305-309
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• 1997

Bacillus stearothermophilus No. 236, an effective xylanolytic bacterium, produced an extracellular carboxymethyl cellulase when the strain was grown on xylan. The carboxymethyl cellulase was purified to homogeneity as judged by SDS-PAGE and zymogram, The carboxymethyl cellulase had a pI of 4.0, and a molecular mass of 95 kDa. The highest level of enzyme activity was observed at pH 6.5 and $60^{\circ}C$. The $K_m$, and $V_{max}$ values of the enzyme to carboxymethyl cellulose were 20.8 mg/ml and $0.63 {\mu}mole$/min/mg protein, respectively, The enzyme was found to act also on filter paper and xylan as well as carboxymethyl cellulose. Therefore, it is expected that this xylanolytic strain isolated from soil could be efficiently used for xylan biodegradation.

• 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.30 no.2
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• pp.113-118
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• 2002

A Carboxymethyl Cellulase (CMCase) has been isolated and purified from the edible mushroom, Stropharia rugosoannulata. The molecular weight of CMCase was estimated to be 54 kDa by SDS polyacryl amide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $40^{\circ}C$, and stable for pH 3.0 to 11.0 to maintain 40% activity. The CMCase activity was activated by $AgNO_{3},\;MgSO_{4},\;and\;KCl$. However, its activity was inhibited by 1,10-phenanthroline, KCN and L-cysteine. Also, the enzyme activity was decreased by the addition of EDTA, suggesting that the purified CMCase is metalloenzyme.

• 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.

• Journal of Microbiology
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• v.34 no.4
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• pp.305-310
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• 1996

A microorganism producing carboxymethyl-cellulase (CMCase) was isolated from 300 soil and compost samples. The isolate was identified as Bacillus sp. by $Biolog^{TM}$ test and fatty acid analysis, and named as Bacillus sp. KD1014. The isolate could degrade, in addition to CMC, various kinds of polysaccharides such as levan, xylan, starch, and filter paper but hardly degrade microcrystalline Avicel. The optimum growth and CMCase production of the isolate was observed between 16-and 25 hr-culture at 45$^{\circ}C$ and pH 5.0. The maximum CMCase activity was observed at pH 4.5 and 6$0^{\circ}C$. The CMCase was found to bind to Avicel. The CMCase was internally cleaved as growth continued. When crude supernatant was used for activity staining, three major bands were detected on a native gel, however, only one major band was detected on a denaturating gel after removal of the detergent.

• Journal of Applied Biological Chemistry
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• v.43 no.2
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• pp.74-78
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• 2000

A strain that produces a high level of carboxymethyl cellulase was isolated from rotten leaves. The isolated strain was revealed to be gram-negative, oxidase-positive, and catalase-negative. From the electron microscopic features, it was identified as a rod-shaped bacterium with peritrichous flagella and did not form spores. Morphological and biochemical characteristics of the strain were found to be similar to the Pseudomonas species. However, carbon utilization test showed different results. Based on the results, this new strain was identified as Pseudomonas sp. CMC-50. CMCase produced by this strain showed a strong activity in neutral and weak acidic conditions and maximum activity at $50^{\circ}C$.

• The Microorganisms and Industry
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• v.11 no.1
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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.

• The Korean Journal of Mycology
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• v.25 no.2 s.81
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• pp.91-100
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• 1997

Production of alkaline carboxymethyl cellulase (CMCase) and xylanase by batch and fed-batch cultures of alkalophilic Cephalosporium sp. RYM-202 was investigated. Of carbon sources tested, wheat bran gave the highest production of those enzymes. The high levels of CMCase on carboxymethyl cellulose and xylanase on birchwood xylan suggest that the biosynthesis of CMCase and xylanase in Cephalosporium sp. RYM-202 is regulated separately at the level of enzyme induction. The temperature and pH for maximal production of those enzymes was $20^{\circ}C$ and 9.0, respectively. High concentration of wheat bran in batch fermentation resulted in the lower and delayed production of the enzymes by catabolite repression. In fed-batch fermentation with controlled feeding of 5% final wheat bran concentration, the highest activities of CMCase and xylanase were 0.39 and 9.2 units/ml, respectively, and 1.22 and 1.36 times higher respectively than those in batch fermentation on 5% wheat bran.

• Korean Journal of Agricultural Science
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• v.24 no.2
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• pp.275-282
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• 1997

The prcx.iuction of extracellular 1,4-${\beta}$-glucanase by Cellulomonas sp. CS1-1 on microcrystalline cellulose, sigmacell was maximal after 5-day cultivation as 280 units/mL, which was three times higher than the level produced on carboxymethyl cellulose. A carboxymethyl cellulase containing the carbohydrate of 8.2% was purified from the culture filtrate by successive procedures of column chromatographies. Purification factor was calculated as 22-folds with the specific carboxymethyl cellulase activity of 31.9 units/mg. The molecular weight and isoelectric point of the purified enzyme were 54,000 and pI 5.4, respectively. The optimal pH and temperature were 6.0 and $45^{\circ}C$, and the enzyme was stable between pH 6.5 and 7.5 and below $50^{\circ}C$. The estimated Km and Vmax were 10 mg/mL and $6.25{\mu}mol/min$ for carboxymethyl cellulose and 30.3 mg/mL and $2.85{\mu}mol/min$ for sigmacell, respectively. The enzyme was partially inhibited by $Ag^+$, $Zn^{+{+}}$, $Fe^{+{+}}$ and EDTA, while completely inhibited by $Cd^{+{+}}$ and $Hg^{+{+}}$ at 1 mM concentration.

• Korean Journal of Microbiology
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• v.45 no.3
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• pp.257-262
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• 2009

Carboxymethyl celluase (cellulase) was purified from cell-free extract of the recombinant Escherichia coli carrying a Bacillus licheniformis WL-12 cellulase gene by DEAE-Sepharose and phenyl-Sepharose column chromatography with specific activity of 163 U/mg protein. The molecular mass of the purified enzyme was estimated to be approximately 49.5 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme had a pH optimum at 5.5 and a temperature optimum at $55^{\circ}C$. The activity of the enzyme was completely inhibited by SDS (5 mM), and slightly enhanced by $Cu^{2+}$ (5 mM). The cellulase was active on CMC, konjac, barely glucan and lichenan, while it did not exhibit activity towards xylan, locust bean gum, and p-nitrophenyl-$\beta$-glucopyranoside. The predominant products resulting from the cellulase hydrolysis were cellobiose and cellotriose for cellooligosaccharides including cellotriose, cellotetraose and cellopentaose. The enzyme could hydrolyze cellooligosaccharides larger than cellobiose.