• Korean Journal of Microbiology
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• v.13 no.3
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• pp.85-90
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• 1975

Crude cellulases freshly prepared from cultures of Aspergillus niger, Prnicillum motatum, Trichoderma vride 16273 and Trichoderma viride 16374 were assayed on 4 different substrates including Na-CMC, cellulose powder, starch and sucrose. Enzyme prepared from A. niger contained highly active hydrolytic enzymes of the 4 substrates assayed. P. notatum [yielded relatively lower amount of cellulase but the extracts were also highly reactive on starch and sucrose. Trichoderma viride 16274 yielded very little cellulase and invertase, but the extracts showed a high degree of amylase activity. Trichoderma viride 16374, however, yielded collulase comparable to that of Penicillium notatum, but lower activities of amylase and invertase were seen. Commercial cellulases prepared from Penicillium notatum (cellulase[K]) and Trichoderma viride(cellulase[J]) indicated enzyme activities closely parallel to the crude enzymes freshly prepared from fungus cultures. The optimum pH's of cellulolytic activities of cellulase[K] and cellulase[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase[K] and cellualse[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase [K] and cellulase [J] were $60{\circ}C$ and $50{\circ}C$ respectively. Assuming the average molecular weight of Na-CMC is about 115,000, the Km values of cellulase [K] and cellulase[J] were found to be $3.3{\times}10^{-5}/nM$ and $3.3{\times}10^{-4}/nM$ respectively.

• Korean Journal of Microbiology
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• v.14 no.2
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• pp.49-49
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• 1976

Enzyme activities, such as glucoamylase dextrinogenic amylase, cellulase, acid protase and neutral protease, of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their enzyme activities are surveyed from taxonomical, ecological and physiological viewpoint. Effect of carbon sources and phytohormones on the amylalse production of Rhizopus are also measured. Among the 735 strains of Phizopus isolated, strain number 587 exhibiting most prominent dextrinogenic amylase and netral protease activity is selected as the best strain, and the strain number 673, 108, 329, 165 and 728 are seleted for their predominant cellulase, acid protease, glucoamylase, dextrinogenic amylase and neutral protease activities, respectively. R.acidus and R.nigricans which exhibited relatively higher callulalse activity, showed lower activities for both amylase. R.tritici exhibited higher protease activity. The relations between activities and various substrates of wild strains are not outstnading difference, although the strains isolated from inland region exhibited more or less higher amylase and cellulase activities, than those of coast region, generally. Lactose and dextrin are most effective carbon sources for glucoamylase and dextrinogenic amylase production of the Rhizopus niveus, respectively. Although all phytohormones tested are effective for production of amylase by the Rhizopus strains, except nicotinamide for glucoamylase production, biotin and ascorbate are most effective for dextrinogenic amylase and glucoamylase production, respectively.

• Korean Journal of Microbiology
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• v.14 no.2
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• pp.47-56
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• 1976

Enzyme activities, such as glucoamylase dextrinogenic amylase, cellulase, acid protase and neutral protease, of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their enzyme activities are surveyed from taxonomical, ecological and physiological viewpoint. Effect of carbon sources and phytohormones on the amylalse production of Rhizopus are also measured. Among the 735 strains of Phizopus isolated, strain number 587 exhibiting most prominent dextrinogenic amylase and netral protease activity is selected as the best strain, and the strain number 673, 108, 329, 165 and 728 are seleted for their predominant cellulase, acid protease, glucoamylase, dextrinogenic amylase and neutral protease activities, respectively. R.acidus and R.nigricans which exhibited relatively higher callulalse activity, showed lower activities for both amylase. R.tritici exhibited higher protease activity. The relations between activities and various substrates of wild strains are not outstnading difference, although the strains isolated from inland region exhibited more or less higher amylase and cellulase activities, than those of coast region, generally. Lactose and dextrin are most effective carbon sources for glucoamylase and dextrinogenic amylase production of the Rhizopus niveus, respectively. Although all phytohormones tested are effective for production of amylase by the Rhizopus strains, except nicotinamide for glucoamylase production, biotin and ascorbate are most effective for dextrinogenic amylase and glucoamylase production, respectively.

• Journal of Microbiology and Biotechnology
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• v.21 no.12
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• pp.1312-1321
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• 2011

Enzyme extracts of cellulase [filter paper cellulase (FPase) and carboxymethyl cellulase (CMCase)], chitinase, and chitosanase produced by Aspergillus niger NRRL-567 were evaluated. The interactive effects of initial moisture and different inducers for FP cellulase and CMCase production were optimized using response surface methodology. Higher enzyme activities [FPase $79.24{\pm}4.22$ IU/gram fermented substrate (gfs) and CMCase $124.04{\pm}7.78$ IU/gfs] were achieved after 48 h fermentation in solid-state medium containing apple pomace supplemented with rice husk [1% (w/w)] under optimized conditions [pH 4.5, moisture 55% (v/w), and inducers veratryl alcohol (2 mM/kg), copper sulfate (1.5 mM/kg), and lactose 2% (w/w)] (p<0.05). Koji fermentation in trays was carried out and higher enzyme activities (FPase $96.67{\pm}4.18$ IU/gfs and CMCase $146.50{\pm}11.92$ IU/gfs) were achieved. The nonspecific chitinase and chitosanase activities of cellulase enzyme extract were analyzed using chitin and chitosan substrates with different physicochemical characteristics, such as degree of deacetylation, molecular weight, and viscosity. Higher chitinase and chitosanase activities of $70.28{\pm}3.34$ IU/gfs and $60.18{\pm}3.82$ to $64.20{\pm}4.12$ IU/gfs, respectively, were achieved. Moreover, the enzyme was stable and retained 92-94% activity even after one month. Cellulase enzyme extract obtained from A. niger with chitinolytic and chitosanolytic activities could be potentially used for making low-molecular-weight chitin and chitosan oligomers, having promising applications in biomedicine, pharmaceuticals, food, and agricultural industries, and in biocontrol formulations.

• 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.

• Korean Journal of Microbiology
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• v.15 no.3
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• pp.113-121
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• 1977

The 685 strains of Korean Sspergilli are isolated, cultured purely, and their Avicelase, CMCase and Salicinase activities are measured, in order to select the best strains exhibiting predominant cellulase activities, and to survey their cellulase activities in taxonomical and ecological viewpoints. Strains No.175, 255 and 254 are selected as the best Avicelase producing strains, strains No.131, 151 and 116 are selected as the best CMCase producing strains, and strains nO.456, 457 and 253 are selected as the best Salicinase producing strains. A niger group and A, clavatus group exhibited the highest activities of Avcelase and Salicinase, respectively. A.iniger group and A, clavatus groups are showed the highest activites of CMCase. Among the different species tested, the activities of Avicelase, CMCase andSalicinase are highest in A.phoenicis, A.clavatus, and A. japonicus and A.giganteus, respectively. Cellulase activities of Aspergilli from the inland regions of Korea are higher, more or less, than those of the strains from the other regions. Avicelase and CMCase activities of Aspergilli isolated from bread and Korean cake are relatively higher, and Salicinase activities of the strains isolated from the cereals are higher than those of the strains from the other habitat substrate.

• Journal of Plant Biology
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• v.36 no.4
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• pp.327-335
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• 1993

The active sites, intracellular transport, function of cellulase in association with the disintegration of the storage materials of the endosperm cells during seed maturation and after-ripening of Panax ginseng C.A. Meyer seeds were studied by electron microscopy. Cytochemical activities of the cellulase occurred in protein bodies and vesicles of endosperm cells in seed with red seed coat. In after-ripening seed, the activities were strongly found in the cell wall of endosperm near the umbiliform layer and on neighbouring vesicles, so it is assumed that these cells begin to be decomposed. Cellulase activities were initiated before the decomposition of storage materials. But, no activity was observed in the umbiliform layer, so it is suggested that cellulase lose its activity after the completion of lysis process.

• Applied Biological Chemistry
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• v.24 no.4
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• pp.260-266
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• 1981

Some properties of cellulase and xylanase produced from Pleurotus ostreatus 301 and Lentinus edodes 3-1 during its growth in rice straw medium were investigated. The cellulase activities of P. ostreatus 301 and L. edodes 3-1 were increased in proportion to substrate concentration within 0.6% and 0.8%, respectively, and xylanase activities of two strains were increased within 1%. The reducing sugar production of cellulase and xylanase in two strains were proportionaly increased until 30 min. and 60 min. respectively. The opium pH for cellulase activities of P. ostreatus 301 and L. edodes 3-1 were pH 4.0 and pH 4.5, respectively, and xylanase activities of two strains were pH 5.0. The stable pH range for cellulase activities of P. ostreatus 301 was within 4.0 to 6.0 and L. edodes 3-1 was within 3.0 to 5.0, Xylanase activities of P. ostreatus 301 was within 4.5 to 6.0 and L. edodes 3-1 was within 3.5 to 6.0. The optium temperature for cellulase activities of P. ostraeatus 301 and L. edodes 3-1 were $40^{\circ}C$ and $50^{\circ}C$, respectively, but xylanase activities of P. ostreatus 301 and L. edodes 3-1 were $50^{\circ}C$ and $45^{\circ}C$, respectively. Thermal stability of enzymes were below of optimum temperature and these were mostly inactivate at $70^{\circ}C$ for 10 min of the metalic ions tested, cellulase activities of L. edodes 3-1 was increased by $Co^{++},\; Mg^{++}$ at the concentration of $10^{-2}M$, but were greatly inhibited by $Hg^{++},\;Cu^{++}$ in two strains. Xylanase activities were increased by $Ca^{++},\;Co^{++},\;Mg^{++}$ and $Cd^{++}$ but was greatly inhibited by $Hg^{++}$.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1196-1199
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• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.

• Journal of Microbiology and Biotechnology
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• v.13 no.1
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• pp.35-42
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• 2003

A 1,3 kb cellulase gene encoding novel bifunctional cellulase-chitosanase activity was cloned from biopolymer-producing alkali-tolerant B. lichenformis NBL420 in E. coli. A recombinant cellulase-chitosanase, named CelA, was expressed and purified to homogeneity. The activity staining and the enzymatic characterization of the purified CeIA revealed bifunctional activities on carboxymethyl cellulose (CMC) and glycol-chitosan. The similar characteristics of the enzymatic activities at the optimum pH, optimum temperature, and thermostability Indicated that CelA used a common catalytic domain with relaxed substrate specificity. A comparison of the deduced amino acids in the N-terminal region revealed that the mature CelA had a high homology with the previously identified bifunctional cellulase-chitosanase of Myxobacter sp. AL- 1.