• Microbiology and Biotechnology Letters
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• v.19 no.1
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• pp.52-56
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• 1991

Inulin degradation was examined using patially puriiied enzyme mixtures of the Exo-inulinase from a Bacillus spp. and the Endo-inulinase from a Pseudomonas spp.. The highest synergistic xtion of the two cnzymcs was observcd when the Exo- and the Endo-inulinase werc mixed at the ratio of 1 to 13, and the rate of hydrolysis of the above process was enhanced approximately 1.6 times I1ight.1- than that of the reaction catalysed with a single enzyme of the same units. The enzymc mixture showed the maximal activity at pH 6.0 and $55^{\circ}C$, and in the prescncc of 0.5 mM each of $CO^{2+}$ and $Mn^{2+}$. Under the optimal condition described above fructosu was accumulated with the overitll concentration of 84% after 36 hours of the reiiction.

• Applied Chemistry for Engineering
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• v.26 no.3
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• pp.366-371
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• 2015

The kinetic behavior of tetrahydrotricyclopentadiene (THTCPD) isomerization was studied by using two kinds of chloroaluminate ionic liquid (IL) catalyst with different Lewis acidity. THTCPD isomerization pathway was discussed under the different temperature and time as reaction parameters using IL catalysts consisting of 1-butyl-3-methylimidazolun chloride $(BMIC)/AlCl_3$ with low acidity and pyridine hydrochloride $(PHC)/AlCl_3$ with high acidity. The conversion of THTCPD isomerization increased with increasing Lewis acidity of IL catalyst. The THTCPD isomerization pathway changed as a function of reaction temperature and catalyst acidity. In the case of $BMIC/AlCl_3$ IL catalyst, THTCPD isomerization pathway was similar to that of using conventional $AlCl_3$ catalyst. However, two different types of additional pathways (endo, exo, endo-NB ${\rightarrow}$ exo, exo, endo-NB ${\rightarrow}$ exo, exo, exo-NB and endo, exo, endo-NB ${\rightarrow}$ exo, exo, endo-NB ${\rightarrow}$ exo, exo, exo-CP) were appeared when using $PHC/AlCl_3$ IL catalyst.

• Korean Journal of Microbiology
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• v.38 no.4
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• pp.241-246
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• 2002

A gene coding for endo-$\beta$-1,3-1,4-glucanase of Bacillus circulans was subcloned into Escherichia coli Ml5 using pQE30 as an expression vector. Endo-$\beta$-1,3-1,4-glucanase produced by the recombinant expression plas-mid pLQ43 was intactly purified to a single protein through a nickel-nitrilotriacetic acid (Ni-NTA) metal-affinity chromatography method. The molecular mass of the purified enzyme was estimated to be 28 kDa by SDS-PAGE. The optimum pH and temperature of the enzyme activity were pH 6.8 and $60^{\circ}C$, respectively. This enzyme was fairly stable in the pH ranging 5.5~7.5 and at the temperatures lower than $55^{\circ}C$. The enzyme appeared to be sensitive to most of the metal ions, especially to $Hg^{2＋$, and also to methanol, ethanol, isopropanol or 1-butanol at a concentration of 10%(v/v).

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.20-24
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• 1992

In order to reuse inulinase effectively, a method for immobilizing both endo- and exoinulinase to vinylsulfone activated agarose via covalent bond was investigated. The immobilized enzyme preparation had, respectively, 400 U for exoinulinase activity and 80 U for endoinu- Iinase activity per gram gel. A thermal stability by immobilization had increased in the case of exoinulinase. Optimum pHs for two immobilized enzymes were 4.4 to 5.0. Synergistic effect which depends on mixed ratio of two immobilized enzymes was the best when the mixed ratio of endo/exo lay between 0.1 and 0.5, and its activity of the mixed enzyme increased 1.7 times as compared to that of each immobilized enzyme. Inulinase activities of both of the immobilized enzymes did not change during 20 times experimental runs in a batch reactor.

• KSBB Journal
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• v.11 no.6
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• pp.718-725
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• 1996

Old newsprint was deinked with endoglucanase, exoglucanase and their various compositions from Trichoderma viride. The yield decreased with an increase in enzyme concentration. Especially, it was the lowest in the treatment of endo-exo mixture(1:1). It may be regarded as a synergistic actions of the cellulase components. The brightness was the highest in pulp deinked with endo-exo mixture(1:1). Maximum brightness was observed when 0.5mg/mL of the endo-exo mixture was used. The physical strength increased with increasing concentration in exoglucanase. But, it decrease with increasing concentration in endoglucanse and endo-exo mixture(1:1). Also, we investigated the yield, brightness and physical strength of endoglucanase in combination with exoclucanase(12:1, 8:1, 4:l, 1:1, 1:4, 1:8, 1:12). Maximal deinking conditions, obtained at a specific optimal ratio of endoglucanase to exoglucanse are as follow ; 12:1 for yield, 12:1 for brightness, 4:1 for tensile strength, 12:1 for bursting strength, and 8:1 for tearing strength. These results indicated that the deinking depended largely upon the action of endoglucanase. Exoglucanase was occupying more than 60% of the total crude cellulase contents. Therefore, the most effective deinking must repress the action of exoglucanase.

• Journal of Microbiology and Biotechnology
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• v.16 no.10
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• pp.1583-1590
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• 2006

T4 endonuclease V (T4 endo V) [EC 3. 1. 25. 1], found in bacteriophage T4, is responsible for excision repair of damaged DNA. The enzyme possesses two activities: a cyclobutane pyrimidine dimer DNA glycosylase (CPD glycosylase) and an apyrimidic/apurinic endonuclease (AP lyase). T4 denV (414 bp cDNA) encoding T4 en do V (138 amino acid) was synthesized and expressed using either an expression vector, pTriEx-4, in E. coli or a baculovirus AcNPV vector, pBacPAK8, in insect cells. The recombinant His-Tag/T4 endo V (rHis-Tag/T4 endo V) protein expressed from bacteria was purified using one-step affinity chromatography with a HiTrap Chelating HP column and used to make rabbit anti-His-Tag/T4 endo V polyclonal antibody for detection of recombinant T4 endo V (rT4 endo V) expressed in insect cells. In the meantime, the recombinant baculovirus was obtained by cotransfection of BacPAK6 viral DNA and pBP/T4 endo V in Spodoptera frugiperda (Sf21) insect cells, and used to infect Sf21 cells to overexpress T4 endo V protein. The level of rT4 endo V protein expressed in Sf21 cells was optimized by varying the virus titers and time course of infection. The optimal expression condition was set as follows; infection of the cells at a MOI of 10 and harvest at 96 h post-infection. Under these conditions, we estimated the amount of rT4 endo V produced in the baculovirus expression vector system to be 125 mg/l. The rT4 endo V was purified to homogeneity by a rapid procedure, consisting of ion-exchange, affinity, and reversed phase chromatographies, based on FPLC. The rT4 endo V positively reacted to an antiserum made against rHis-Tag/T4 endo V and showed a residual nicking activity against CPD-containing DNA caused by UV. This is the first report to have T4 endo V expressed in an insect system to exclude the toxic effect of a bacterial expression system, retaining enzymatic activity.

• Korean Journal of Agricultural Science
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• v.12 no.2
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• pp.324-332
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• 1985

Aspergillus niger B-15 with strong Endo-polygalacturonase (Endo-PG) activities was selected out from a total of 1,573 fungal strains isolated from various testing materials. A mutant strain, U-46, was obtained from the Aspergillus niger B-15 by repeated irradition of ultra-violet light. The objectives of the study were to investigate the fungal properties of the parental and mutant strains obtained and to study the condition of enzyme production and reaction. The results obtained are summarized as follows: 1. The size of conidial head of the U-46 mutant was smaller than that of the parental strains, B-15 and the length of the conidiophore was also shorter than that of the parental strains. 2. The optimum conditions for the Endo-PG production of the parental B-15 strain in the wheat bran Koji were obtained when 40% of water was added to the wheat bran and the temperature was 30 to $35^{\circ}C$. However, the best condition for the mutant U-46 strain was attained when 60 to 70% of water was added and the temperature was $35^{\circ}C$. The optimum growing periods were two to three days for both parental and mutant strains. 3. Under the optimum producing conditions of each strains, the enzymatic activity of the mutant U-46 was 20 times higher than the Endo-PG of the parental strain, B-15. 4. When both strains were cultured in the wheat bran Koji containing 60% of water at $35^{\circ}C$ for three days, the mutant strain. U-46, was about 46 times higher in the Endo-PG activity and about 18 times greater in Exo-PG activity than the parental strain, B-15. The activities of cellulase, $\alpha$-amylase, and glucoamylase were also highly increased in the mutant strain. 5. The mutant strain, U-46, increased its Endo-PG activity up to 20% over that of ordinary case when 1.2 to 1.5% of ammonium sulphate was added to the wheat bran. 6. The optimum condition for Endo-PG activity of crude enzyme of the mutant strain, U-46, was attained when pH of reaction solution was 4.0 to 4.5 and the temperature was $50^{\circ}C$.

• Polymer(Korea)
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• v.39 no.3
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• pp.506-513
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• 2015

Ethylidene norbornene (ENB) and its blends with endo-dicyclopentadiene (endo-DCPD) were prepared and reacted via the ring-opening metathesis polymerization (ROMP) reaction with the $1^{st}$ and $2^{nd}$ generation Grubbs' catalysts. Dynamic exothermic behaviors during ROMP and tensile properties after ROMP were evaluated using a differential scanning calorimeter (DSC) and a universal testing machine (UTM) for the samples, respectively. It revealed that the ROMP rate was accelerated with the less contents of endo-DCPD and under the $2^{nd}$ generation catalyst. Also, the addition of endo-DCPD and the $1^{st}$ generation catalyst resulted in higher tensile modulus and strength but lower toughness. Gel fraction measurement and fracture surface observation were made to understand the tensile properties.

• Restorative Dentistry and Endodontics
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• v.23 no.1
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• pp.236-246
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• 1998

The purpose of this study was to compare the degree of micro- leakage of new glass ionomer root canal sealer, Ketac-Endo(ESPE Co., Seefeld, Germany) with that of AH-26(De Trey Co., Ltd., U.S.A.). Root canal treatment using K -file, H -file, Gate Glidden drill was conducted on 49 extracted single-rooted teeth. 45 teeth were randomly divided into 3 experimental groups(15 teeth per group) and 4 teeth were used as the control group. Group 1 was used AH -26 sealer with the lateral condensation method for canal filling, group 2 was used Ketac-Endo with the single cone method and group 3 was used Ketac-Endo with the lateral condensation method. The control group was obturated with the single cone method without sealer. The teeth were covered with two coats of nail varnish after 48 hours of obturation. The teeth were immersed in India ink for 1 week and cleaned with methyl salicylate and then the degree of dye penetration were measured with stereomicroscope. The data were analyzed statistically by one-way ANOVA. The results were as follows: 1. 7 teeth in group 1, 5 in group 2, and 3 in group 3, were showed evidence of microleakage implying appropriate canal filling. 2, The mean average of microleakage was $0.17{\pm}0.32mm$ in group 1, $0.30{\pm}0.37mm$ in group 2. $0.10{\pm}0.21mm$ in group 3, showing that canal filling using the lateral condensation canal filling method with Ketac-Endo showed the least microleakage and using the single cone method with Ketac-Endo showed the largest amount of microleakage, 3. There were no statistically significant difference in the variation of microleakage among groups. From the results above, Ketac-Endo which has the advantage of glass ionomer, whether using the single cone method or the lateral condensation method, showed similar results as AH-26, but for clinical application it is thought that were studies on the properties of Ketac-Endo should be followed.

• Korean Journal of Food Science and Technology
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• v.16 no.1
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• pp.41-46
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• 1984

The pectic enzymes produced from Aspergillus niger were separated into three fractions (F-A, F-I and F-II) by means of Sephadex and DEAF-Sephadex column chromatography. Each enzyme fraction was characterized by determining viscosity change and reducing surgar of the pectic acid-enzyme mixture and analyzing thin layer chromatogram of the reaction products. F-I rapidly reduced the viscosity of pectic acid solution and released reducing groups in a random manner so that appeared to be an endo-polygalacturonase (endo-PG). The optimum pH of endo-PG for viscosity reducing activity was 4.2 and that for releasing reducing surgar was 4.7. In the thermal inactivation of endo-PG of $30-45^{\circ}C$, the enthalpy of activation was 217.3 kj/mole and z-value was $7.5^{\circ}C$. F-II and F-A were determined as endo-polymethylgalacturonase and exo-polygalacturonase, respectively.