• The Journal of the Korean Society for Microbiology
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• v.35 no.5_6
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• pp.360-360
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• 2000

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.660-661
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• 2001

Pseudomonas sp. GRC3 produced extracellular chitinase(s) and ${\beta}$-1,3-glucanase(s), possible biocontrol agents. Both of enzymes appeared to inhibit the growth of plant phathogens, especially Phytophthora capsici. Antifungal activities of Pseudomonas sp. GRC3 determined was more than 78% inhibition rate against P. capsici.

• Proceedings of the Zoological Society Korea Conference
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• 1999.10b
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• pp.273.2-273
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• 1999

No Abstract, See Full Text

• KSBB Journal
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• v.18 no.5
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• pp.352-355
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• 2003

${\beta}$-(1,6)-Branched ${\beta}$-(1,3)-D-glucans are known to enhance the immune system in human body, and in most cases have higher molecular weights over 1 MDa. In order to enhance the efficacy of glucans by decreasing their molecular weights, sonication, acid treatment, and enzymatic hydrolysis were tested and compared in this work. Treatment of sonication was effective to decrease the molecular weight to the extent of several dozens of kilo-daltons, but have a risk to disorder the triple helical structure of the glucans. Acid treatment was also an effective method to degrade polysaccharides, but ${\beta}$-(1,6)-branched of the glucan molecules was found to be also hydrolyzed. Treatment of ${\beta}$-(1,3)-glucanase was an effective method to decrease the molecular weight in mild conditions, but could not hydrolyse the highly ${\beta}$-(1,6)-branched ${\beta}$-(1,3)-glucans efficiently.

• Journal of the Korean Wood Science and Technology
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• v.38 no.6
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• pp.547-560
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• 2010

The optimum culture condition of Schizophyllum commune for the cellulase production and its enzymatic characteristics for saccharification of cellulosic biomass were analyzed. S. commune secrets ${\beta}$-1,4-xylosidase (BXL) and cellulases, including endo-${\beta}$-1,4-glucanase (EG), cellobiohydrolase (CBH), and ${\beta}$-glucosidase (BGL). The optimum reaction temperature for all cellulases was $50^{\circ}C$ and the thermostable range was $30{\sim}40^{\circ}C$C. The optimum reaction pH for all cellulases was 5.5 in a range of temperature from $0^{\circ}C$ to $55^{\circ}C$. The best nutritions for the cellulase production of S. commune among tested nutrients were 2% cellulose for the carbon source and corn steep liquor or peptone/yeast extract for the nitrogen source without vitamins. The environmental culture condition for the cellulase production was 5.5~6.0 for pH at $25{\sim}30^{\circ}C$. The enzyme activities of EG, BGL, CBH, and BXL were 3670.5, 631.9, 398.5, and 15.2 U/$m{\ell}$, respectively, after concentration forty times from the culture broth of S. commune which was grown at the optimized culture condition. Alternative filter paper unit assay showed 11 FPU/$m{\ell}$ enzyme activity. The saccharification tests using cellulase of S. commune showed the low saccharification rate on tested hardwoods but a high value of 50.5% on cellulose, respectively. The saccharification rate (50.5%) of cellulose by cellulase produced in this work is higher than 45.7% in the commercial enzyme (Celluclast 1.5L, 30 FPU/g, glucan).

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.7
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• pp.945-951
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• 2013

In vitro studies were undertaken to develop an appropriate fibrolytic enzymes cocktail comprising of cellulase, xylanase and ${\beta}$-D-glucanase for maize stover with an aim to increase its nutrient utilization in sheep. Cellulase and xylanase added individually to ground maize stover at an increasing dose rates (0, 100, 200, 400, 800, 1,600, 3,200, 6,400, 12,800, 25,600, 32,000, 38,400, and 44,800 IU/g DM), increased (p<0.01) the in vitro dry matter digestibility and in vitro sugar release. The doses selected for studying the combination effect of enzymes were 6,400 to 32,000 IU/g of cellulase and 12,800 to 44,800 IU/g of xylanase. At cellulase concentration of 6,400 IU/g, IVDMD % was higher (p<0.01) at higher xylanase doses (25,600 to 44,800 IU/g). While at cellulase doses (12,800 to 32,000 IU/g), IVDMD % was higher at lower xylanase doses (12,800 and 25,600 IU/g) compared to higher xylanase doses (32,000 to 44,800 IU/g). At cellulase concentration of the 6,400 to 32,000 IU/g, the amount of sugar released increased (p<0.01) with increasing levels of xylanase concentrations except for the concentration of 44,800 IU/g. No effect of ${\beta}$-D-glucanase (100 to 300 IU/g) was observed at lower cellulase-xylanase dose (cellulase-xylanase 12,800 to 12,800 IU/g). Based on the IVDMD, the enzyme combination cellulase-xylanase 12,800 to 12,800 IU/g was selected to study its effect on feed intake and rumen fermentation pattern, conducted on 12 rams (6 to 8 months; $20.34{\pm}2.369$ kg body weight) fed 50% maize stover based TMR. The total volatile fatty acids (p<0.01) and ammonia-N concentration was higher in enzyme supplemented group, while no effect was observed on dry matter intake, ruminal pH and total nitrogen concentration.

• Korean Journal of Food Science and Technology
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• v.29 no.2
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• pp.198-203
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• 1997

The ground persimmon puree was treated with two kinds of commercial polysaccharide hydrolyzing enzymes (Viscozyme and Celluclast) in order to study their effects on the extraction yield, viscosity, color, titratable acidity and sugars. Hydrolysis with Viscozyme which has enzymatic activity of arabinase, cellulase, xylanase, hemicellulase and ${\beta}-glucanase$ significantly increased the extraction yield, L-value and reducing sugar and decreased in viscosity by treatment for 10 min at $50^{\circ}C$. The extraction yield of the juice was increased from 42.7% to 80% by Viscozyme while the Celluclast to 73.3%. On the other hand, the sensory properties of persimmon-like flavor, scarlet and orange color were greatly improved for the juice hydrolyzed with Viscozyme for 60 min.

• The Korean Journal of Mycology
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• v.13 no.1
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• pp.1-10
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• 1985

This experiment was undertaken to investigate proper conditions for protoplast isolation from strains of Agaricus bisporus, Flammulina velutipes, Lentinus edodes, Pleurotus florida, Pleurotus ostreatus, Pleurotus sajor-caju and Volvariella volvacea. Combination of ${\beta}-D-glucanase$, novozym 234 and snail enzyme with 0.6M $MgSO_4$ in 0.05M Na-maleate buffer, pH 5.8 was the most effective for isolation of protoplasts. High yields of protoplasts were obtained from $4{\sim}5$ days old mycelia of P. florida and P. ostreatus on mushroom complete agar medium. Protoplasts were also obtained in good yield from other fungi but A. bisporus and V. volvacea. In the latter two cases protoplast release was observed; however, the yield was much lower than those of the other fungi.

• Journal of Microbiology and Biotechnology
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• v.14 no.2
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• pp.430-434
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• 2004

Three extracellular protease-deficient Bacillus subtilis strains were transformed with the plasmid pCK98 containing the endo-$\beta$-1,4-glucanase (Eng) gene of B. subtilis BSE616. The three transformants, B. subtilis DB104 (pCK98), WB600 (pCK98) and WB700 (pCK98), produced the same high level of enzyme activity and showed similar patterns of cell growth and enzyme production. When B. subtilis DB 104 (pCK98), a two-extracellular protease deficient strain, was cultured for 22 h, almost all the secreted enzyme was found to be in the completely cleaved form by both activity staining and Western blotting studies. B. subtilis WB600 (pCK98), a six-extracellular protease-deficient strain, produced a partially cleaved form in addition to the intact form of the enzyme, although the degree of internal cleavage of the enzyme was greatly reduced. With B. subtilis WB700 (pCK98), a seven-extracellular protease-deficient strain, almost all the enzyme was produced as the intact uncleaved form. This study illustrates that a role of the V pr protease is to degrade foreign proteins produced in B. subtilis and WB700 is a suitable expression system for producing the intact form of the Eng and other foreign proteins that may lose at least part of their efficacy due to internal proteolytic cleavage.

• Journal of Microbiology and Biotechnology
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• v.22 no.3
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• pp.407-415
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• 2012

An endophytic bacterium, Bacillus thuringiensis GS1, was isolated from bracken (Pteridium aquilinum) and found to have maximal production of chitinase (4.3 units/ml) at 5 days after culture. This study investigated the ability of B. thuringiensis GS1 to induce resistance to Rhizoctonia solani KACC 40111 (RS) in cucumber plants. Chitinase activity was greatest in RS-treated plants at 4 days. ${\beta}$-1,3-Glucanase activity was highest in GS1-treated plants at 5 days. Guaiacol peroxidase (GPOD) activity increased continuously in all treated plants for 5 days. Ascorbate peroxidase (APX) activity in RS-treated plants was increased 1.5-fold compared with the control at 4 days. Polyphenol oxidase (PPO) activity in RS-treated plants was increased 1.5-fold compared with the control at 3 days. At 5 days after treatment, activity staining revealed three bands with chitinase activity (Ch1, Ch2, and Ch3) on SDS-PAGE of cucumber plants treated with GS1+RS, whereas only one band was observed for RS-treated plants (Ch2). One GPOD isozyme (Gp1) was also observed in response to treatment with RS and GS1+RS at 4 days. One APX band (Ap2) was present on the native-PAGE gel of the control, and GS1- and GS1+RS-treated plants at 1 day. PPO bands (Po1 and Po2) from RS- and GS1+RS-treated plants were stronger than in the control and GS1-treated plants upon native-PAGE at 5 days. Taken together, these results indicate that the induction of PR proteins and defense-related enzymes by B. thuringiensis GS1 might have suppressed the damping-off caused by R. solani KACC 40111 in cucumber plants.