• Korean Journal of Microbiology
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• v.26 no.2
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• pp.88-92
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• 1988

The isolation and characterization of a new type II methylase, BmaI methylase, from Bacillus macerans ATCC 8244 were described. BmaI methylase was isolated by procedures of ammonium sulfate fractionation, DEAE-cellulose chromatography and phosphocellulose chromatography. Two types of methylases were present in this strain and only one of the two was a site specific BmaI methylase. The pBR322 DNA methylated by BmaI methylase was not cleaved by BmaI endonuclease, and pBR322 DNA cleaved by BmaI endonuclease was not methylated by BmaI methylase. The optimal pH for the BmaI methylase activity was 7.5, and optimal NaCl concentration was about 50 mM. BmaI methylase could methylate single-stranded M13mp18 DNA.

• Korean Journal of Microbiology
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• v.26 no.1
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• pp.1-5
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• 1988

The esolation and characterization of a new type II restriction endounclease, BamI, from Bacellus macerans ATCC 8244 were described. BmaI endonuclease was partially purified by procedures of ammonium sulfate fractionation, DEAE-cellulose and phosphocellulose chromatographies. This enzume recognized one site on pBR322 DNA, two sites on Bluescribe DNA, three sites on $\lambda$DNA and no site on SV 40 DNA. The same cleavage patterns for vareius DNAs as PvuI indicated that BamI is an isoschisomer of PvuI whose recognition sequence is 5'-CGATCG-3'. The optimal pH for the BmaI endonuclease activity was about 7.0 and optimal NaCl concentration was about 100mM. Manganese ion could partially replace magnesium as a cofactor, but calcium could not at all.

• Journal of the Korean Wood Science and Technology
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• v.25 no.4
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• pp.45-50
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• 1997

This research was studied for dissolving pulp preparation as the raw material of viscose rayon from woody biomass by solvolysis pretreatment. In the change of pulp characteristic after solvolysis pretreatment, the following results were obtained. In the case of solvolysis pretreatment, we have obtained pulp that high purity cellulose, and degree of polymerization was inclined to decrease less than 440 on the phosphoric acid as catalyst. Comparing phosphoric acid and formic acid as catalyst in the solvolysis pretreatment, using on formic acid catalyst is superior to phosphoric acid catalyst for making dissolving pulp.

• Biomedical Science Letters
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• v.6 no.4
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• pp.261-268
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• 2000

Fibrinolytic enzyme (FE-2) was purified from the fruiting bodies of Tricholoma saponaceum using DEAE-Cellulose chromatography and Mono-S column chromatography, The enzyme has a molecular weight of 18.23 kDa and include Zn$^{2+}$ ion as found by ICP/MS. The N-terminal amino acid sequence of the enzyme was A-L-Y-V-G-X-S-P-X-Q-Q-S-L-L-V It has a pH optimum at pH 7.5, suggested that FE-2 was a neutral pretense. The activity of FE-2 was highly inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme is a metalloprotease. The activity of FE-2 was increased by $Mg^{2+}$, Zn$^{2+}$, Fe$^{2+}$, and Co$^{2+}$, but the enzyme activity was totally inhibited by Hg$^{2+}$. No inhibition was found with PMSF, E-64, pepstatin and 2-mercaptoethanol. The enzyme hydrolyzed both $A\alpha$ and B$\beta$ chains of human fibrinogen. The $\gamma$ chain was resistant to hydrolysis by FE-2.

• Korean Journal of Soil Science and Fertilizer
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• v.34 no.5
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• pp.333-341
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• 2001

The Compost-decomposing-bacteria was isolated from livestock compost containing sawdust. The isolated bacteria was identified as Bacillus subtilis LYH201 by the method of the composition of the fatty acid with MIDI system and Bergey's manual. Cloning of CMCase encoding gene was accompanied by shotgun method. The pLK100 have yellow activity ring on CMC medium, that was carried 2.2 kb insert DNA in pBluescript II $SK^+$ vector, named BglC gene. The BglC was very similar to Pectobacterium carotovorum Gun_CLOAB(P15704) with score of 57% identity and 71% homology over 508 aa. The BglC was measured molecular weight 56 kDa by CMC-SDS-PAGE. Optimum cellulase activity Bacillus subtilis LYH201 was temperature $50^{\circ}C$ and pH 7.

• Journal of the Korean Wood Science and Technology
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• v.22 no.2
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• pp.30-36
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• 1994

Steam explosion process is one of the most efficient, pretreatment method for the utilization of lignocellulosic biomass. The carbxymethyl-cellulose(CMC) was prepared with steam exploded wood(EXW), pine(Pinus densiflora) and oak(Quercus mongolica), by standard method using isopropyl alcohol and monochloroacetic acid. The range of water solubility of carboxymethylated pine exploded wood was 45.2~66.8 % and those of oak was 60.7~84.7 %. The degree of substitution(D.S) of carboxymethylated pine exploded wood was 0.11~0.33 and oak exploded wood was 0.48~0.76. The color of carboxymethylated pine and oak exploded wood was brown-black. When carboxymethylated EXW was purified by sulfuric acid, the yield of carboxymethylated wood was lower than non-treated one. However, the color was still brown-black although after delignification. In carboxymethylated EXM prepared after delignification, the water solubility and degree of substitution(D.S) of pine were 81.4~95.9 % and 0.71~0.79, and those of oak were 76.2~89.5 % and 0.79~1.05. The values were higher than non-treated. The degree of substitution of purified carboxymethylated wood prepared with delignified EXM, pine and oak were 0.50~0.71 and 0.70~0.88. The color of carboxymethylated wood was white. In carboxymethylated wood preparde after delignification of EXM, swelling ratio and water retention value of pine were 95.9~96.5 and 580.0~751.2, those of oak were 76.2~89.5 and 124.3~307.6.

• Korean Journal of Food Science and Technology
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• v.14 no.1
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• pp.1-5
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• 1982

An invertase from Korean ginseng (Panax ginseng C. A. Mayer) was purified by means of DEAE-cellulose column chromatography and gel-filtration through Sephadex G-75. The homogeneity of the purified invertase was proved by polyacrylamide gel disc electrophoresis. The enzyme was separated into two subunits by SDS-polyacrylamide gel electrophoresis, showing its molecular weights as 48,000. The enzyme preparation showed a characteristic protein UV-spectra.

• Polymer(Korea)
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• v.31 no.5
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• pp.436-441
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• 2007

In this work, the multiwalled carbon nanotubes(MWNTs) were functionalized with sodium dodecylbenzene sulfonate(SDBS) and then MWNTs/Lyocell composite fibers were prepared. The properties of MWNTs, the functionlization on the surface of MWNTs and their dispersion in the cellulose matrix were characterized by TEM, SEM, WAXD and FT-IR. The results showed that SDBS has been coated successfully onto the surface of the MWNTs by functionlization. This can improve effectively the dispersion uniformity of MWNTs in NMMO aqueous solution and is helpful to prepare a spinnable spinning dope. Moreover, the resultant MWNTs/Lyocell composite fibers still have cellulose II crystal structure, and their tensile strength and initial modulus increased with the increasing draw ratio and reached the optimal value with adding 1 wt% MWNTs. The thermal stability of the composite fiber was also improved by the addition of the MWNTs.

• Korean Journal of Microbiology
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• v.24 no.1
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• pp.18-23
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• 1986

A new type II restriction endonuclease, Bdi I, has been isolated from Brenibacterium divaricatum FERM 5948 by procedures of ammonium sulfate fractionation, DEAE-cellulose chromatography and heparin agarose chromatography. The purified Bdi I restriction endonudlease had the same cleavage patterns of Cla I whose recognition sequence is 5' ATCGAT 3'. From the result that ${\lambda}-Cla$ I DNA frahment could be cloned in pBR 322 digested with Bdi I, it has been proven that Bdi I cuts between T and C(5' AT/CGAT3') within the recognition sequence and produces 5'pCG cohesive end. The optimal temperature for the Bdi I restriction endonuclease activity was $37^{\circ}C$, and optimal salt (NaCl) concentration was 50-100 mM.

• Parasites, Hosts and Diseases
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• v.21 no.1
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• pp.49-57
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• 1983

The distribution and Properties of branched chain amino acid aminotransferase (EC 2.6. 1.42) was investigated in adult Fasciola hepatica. Fascicla hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of branched chain amino acid aminotransferase was measured by the method of Ichihara and Koyama (1966) . Isozyme patterns of this enzyule was also examined by DEAE-cellulose column chromatography. The results obtained were as follows; 1. The activity in homogenate was found to be 12.69 units/g wet tissue. The activity of this enzyme was relatively high compared with those in rat tissues. 2. The distribution of branched chain amino acid aminotransferase in the subcellular organelles showed that 87.8% of the activity was in cytosolic, 10.9% in mitochondrial and 1.3% was in nuclear fraction. 3. Cytosolic fraction of Fasciola hepatica contained Enzyme I, but not Enzyme II and III, of branched chain amino acid aminotransferase. Ensyme I was eluted by 50mM phosphate buffier from DEAE-cellulose column and catalyzed the transamination of all three branched chain amino acids. 4. The Enzyme I was purified about 22-folds increase in specific activity after chromatography on DEAE-cellulose. 5. The best substrate among three amino acids (leucine, isoleucine and valise) was L-isoleucine. 6. The optimal temperature of Enzyme I was $45^{\circ}C$ and the optimal pH was 8.2. 7. The Km value for leucine of Enzyme I was 4.17 mM. 8. The Km values for a-ketoglutarate and pyridoxal phosphate of Enzyme I were 0.41mM and $4.76{\times}10^{-3}{\;}mM$, respectively.