• Journal of the Korean Wood Science and Technology
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• v.36 no.6
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• pp.138-146
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• 2008

The chemical compositions, cell wall biopolymers and non-isothermal behavior of the stem biomass of Nicotiana Tabacum originated from tobacco industry were investigated in depth. On a weight basis, the contents of total ash and total sugar are 19.1% and 20.7% respectively. Lignin content was around 3% of tobacco stem biomass while pectin was over 7%. The holo-cellulose content in cell wall biopolymer was around 13% and the $\alpha$-cellulose constitutes 60% of the total holo-cellulose. The thermal behavior of stem biomass showed different patterns depending on either inert (nitrogen) or oxidizing (air) atmospheric condition. In the air atmosphere, the rapid thermal decompositions at around $473^{\circ}C$ and $581^{\circ}C$ were recorded as the peaks in DTG curve, while the peaks were not shown in the nitrogen atmosphere condition. The thermal analysis of the freeze dried soluble obtained from hot water extraction of tobacco stem biomass showed that the rapid thermal decomposition at around $581^{\circ}C$ in the air atmosphere was due to the residual char originated from the soluble fraction. The distinct difference in thermal decomposition between hemicellulose and cellulose were easily found in the DTG curve obtained in the nitrogen atmosphere.

• Korean Journal of Veterinary Research
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• v.22 no.2
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• pp.115-119
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• 1982

Total protein levels of 60 bovine bull sera were treasured with refractometer and the strum proteins were fractionated by cellulose acetate membrane electorphoresis and the relative amount of each fraction was measured with automatic scanning densitometer. The sixty bovine bulls consisted of 17 Charolais bulls, 28 Holstein bulls and 15 Korean bulls. Mean total serum protein level of the total bulls was $7.50{\pm}0.50(Mean{\pm}SD)$, with the mean of Charolais $7.04{\pm}0.37g/dl$, the mean of Holstein $7.62{\pm}0.40g/dl$ and the mean of Korean $7.81{\pm}0.43g/dl$. As barbital-calcium buffer was used in fractionating the bovine serum protein with cellulose acetate membrane, electric current of 0.4 mA per centimeter width of the membrane for an hour resulted in more clear separation between ${\alpha}_1$-globulin and ${\alpha}_2$-globulin than electric current of 0.6 or 1.0 mA for an hour. However ${\alpha}_1$-globulin and ${\alpha}_2$-globulin could not be measured separately with automatic scanning densitometer. Mean serum albumin level of total bulls was $3.54{\pm}0.42g/dl$, with the mean of Charolais $3.42{\pm}0.26g/dl$, the mean of Holstein $3.69{\pm}0.38g/dl$ and the mean of Korean $3.39{\pm}0.55g/dl$. Mean serum ${\alpha}$-globulin level of the total bulls was $0.62{\pm}0.14g/dl$, with the mean of Charolais $0.61{\pm}0.07g/dl$, the mean of Holstein $0.60{\pm}0.11g/dl$ and the mean of Korean $0.67{\pm}0.23g/dl$. Mean ${\beta}$-globulin level of the total bulls was $0.85{\pm}0.21g/dl$, with the mean of Charolais $0.74{\pm}0.11g/dl$, the mean of Holstein $0.83{\pm}0.14g/dl$ and the mean of Korean $1.02{\pm}0.30g/dl$. Mean serum ${\gamma}$-globulin level of the total bulls was $2.48{\pm}0.45g/dl$ with the mean of Charolais $2.27{\pm}0.37g/dl$, the mean of Holstein $2.48{\pm}0.44g/dl$ and the mean of Korean $2.72{\pm}0.47g/dl$.

• Journal of Pharmaceutical Investigation
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• v.31 no.3
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• pp.151-160
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• 2001

The purpose of this study is to investigate the interaction of progesterone with various cyclodextrins (CDs) in the aqueous solution and in solid state, and finally to formulate a parenteral aqueous formulation. CDs used were ${\alpha}-$, ${\beta}-$, and ${\gamma}-CD$, $2-hydroxypropyl-{\beta}-CD$ (HPCD), sulfobutyl $ether-{\beta}-CD$ (SBCD), $dimethyl-{\beta}-CD$ (DMCD) and $trimethyl-{\beta}-CD$ (TMCD). The solubility studies of progesterone were performed in the presence of various CDs as a function of concentration or temperature. The solubility of progesterone increased in the rank order of ${\alpha}-CD$ < ${\beta}-CD$ < ${\gamma}-CD$ < TMCD$ < HPCD < DMCD < SBCD. Addition of SBCD (200 mg/ml) in water increased the aqueous solubility $(9.36\;{\mu}g/ml)$ about 3,200 times, and lowering the temperature facilitated the solubilization of progesterone. However, the addition of HPCD and SBCD in 20:80 (v/v) polyethylene glycol 300-water and propylene glycol-water cosolvents markedly decreased the solubility of progesterone, compared with solubilizing effects in water. Physical mixtures and solid dispersions of progesterone with HPCD or SBCD were prepared, and evaluated by differential scanning calorimetry (DSC), Fourier-transform infrared spectroscopy (FT-IR), near IR spectroscopy and dissolution studies. By DSC and IR studies, it was found that progesterone was dispersed in HPCD in monotectic state and dissolved rapidly from both solid dispersions. Based on solubility studies, new aqueous progesterone fonnulations (5 mg/ml) containing SBCD (200 mg/ml) could be prepared and did not form precipitates even after 2 months at $4^{\circ}C$. The solution was transparent when mixed with normal saline and 5% dextrose injection at 1: 1, 1:10 and 1:20 (v/v) even after 7 days. Permeation rates of progesterone through a cellulose membrane from 20% PEG 300 solution $(50\;{\mu}g/ml)$ containing HPCD or SBCD were compared with oily formulation. Permeation of progesterone from oily formulation did not occur up to 8 hr, but aqueous formulations showed fast permeation rates from early stage of permeation study. The addition of HPCD or SBCD retarded the permeation rates of progesterone with the increase of CD concentrations, suggesting the possibility of a controlled absorption from the site administered intramuscularly. These results demonstrate that it is feasible to develop a new progesterone parenteral aqueous injection (5 mg/ml) using SBCD.

• Korean Journal of Food Science and Technology
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• v.37 no.5
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• pp.776-782
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• 2005

The effects of purification using ${\alpha}-amlyase$ (Termamyl 120L) on physicochemical properties of ${\beta}-glucan$ from oat bran were studied. Four fractions were selected as fraction A ($55^{\circ}C$, 15%, pH 6), fraction B ($45^{\circ}C$, 15%, pH 6), fraction C ($50^{\circ}C$, 0%, pH 7), and fraction D ($50^{\circ}C$, 10%, pH 5) from the result of physiological test, and three consecutive subfractions were obtained by repeated ${\alpha}-amlyase$ treatments on the each fractions. The contents of ${\beta}-glucan$, protein, and ash after purification were in 81.4-88.2%, 4.1-6.3% and 2.6-6.2%, respectively. The apparent viscosities of purified ${\beta}-glucan$ aqueous solutions were similar to those of hydroxy methyl cellulose. Glucose was a major monosaccharide of ${\beta}-glucan$ extracts, and xylose and arabinose were also detected as minor constituents on TLC. The average molecular weight ranged $2.0{\times}10^6-5.1{\times}10^6$ and was decreased after purification. From the result of the differential scanning calorimetry, the melting point ranged $130-140^{\circ}C$ with purification step and thermal transition enthalpy was increased. The ratio of ${\beta}-(1{\rightarrow}3)\;to\;{\beta}-(1{\rightarrow}4) $ linkages were 1:2.22-1:2.52, and increased up to 1:5.50 after purification.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2005.06a
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• pp.245-247
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• 2005

A cellulolytic fungus isolated from Agave plantation in northeastern Thailand was identified as Acrophialophora nainiana. The fungus was capable of growing at pH between 3 - 7 and 25 - 45 $^{\circ}C$, with the optimum conditions at pH 5.0 and 40 $^{\circ}C$. The wild isolate produced cellulases, comprising of exoglucanase (0.019 U/mg protein), endoglucanase (0.366 U/mg protein), and ${\beta}$-glucosidase (0.001 U/mg protein). Mutations with UV and NTG produced the UV 10-2 mutant with cellulases activities including exoglucanase (0.093 U/mg protein), endoglucanase (0.585 U/mg protein), and ${\beta}$-glucosidase (0.013 U/mg protein). Purification of the enzymes with ultrafiltration, ammonium sulfate precipitation, and ion-exchange chromatography yielded the maximal cellulase specific activities of 2.736 U/mg protein (exoglucanase), 0.235 U/mg protein (endoglucanase), and 0.008 U/mg protein (${\beta}$-glucosidase). The mutant's cellulases were the most active at pH 5.0 and 60 $^{\circ}C$. Ion-exchange chromatography revealed that A. nainiana UV 10-2 cellulases were comprised of two peaks with one peak showing the single endoglucanase activity while the other peak showed a mixture of the three enzyme activities. Production of A. nainiana UV 10-2 cellulases using banana leaf stalk as the sole carbon source gave comparable yields to that of the pure ${\alpha}$-cellulose. The enzymes were used in the simultaneous saccharification and fermentation (SSF) of plant residue (Coix aquatica) along with Kluveromyces marxianus to produce ethanol. Moreover, when the enzymes were used in the bioscouring process of fabric, the desiravle traits of textile processing including immediate water absorbency, increased in whiteness and reduction of yellowness of the treated fabric were observed.

• Applied Biological Chemistry
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• v.28 no.2
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• pp.98-105
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• 1985

In the sheep and cattle's rumen, facultative anaerobic cellulolytic bacteria were isolated by using Hungate's roll tube technique. In the 21 isolated species, one was screened by its strong cellulolytic activity and identified as Cellulomonas fimi C-14 by investigate morphological, cultural, physiological characteristics and electron microgram. Optimum conditions of the cell growth and enzyme production were pH 6.5 an $30^{\circ}C$, Thiamine and biotin support a good growth of C. fimi C-14. In the enzyme activities, Crystalline cellulose hydrolyzing activity, CMCase activity and ${\beta}-glucosidase$ activity were 20.6, 226.6 and 0.56$(unit{\times}10^3/ml)$ at pH 6.0, $40^{\circ}C$. By addition of fungal cellulase, enzyme activity was increased. Simultaneous Saccharification Fermentation is better than two step fermentation in ethanol yield with Saccharomyces cerevisiae DY2.

• Journal of Microbiology and Biotechnology
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• v.20 no.10
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• pp.1378-1385
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• 2010

A novel agarolytic bacterium, KY-YJ-3, producing extracellular agarase, was isolated from the freshwater sediment of the Sincheon River in Daegu, Korea. On the basis of Gram-staining data, morphology, and phylogenetic analysis of the 16S rDNA sequence, the isolate was identified as Cellvibrio sp. By ammonium sulfate precipitation followed by Toyopearl QAE-550C, Toyopearl HW-55F, and MonoQ column chromatographies, the extracellular agarase in the culture fluid could be purified 120.2-fold with a yield of 8.1%. The specific activity of the purified agarase was 84.2 U/mg. The molecular mass of the purified agarase was 70 kDa as determined by dodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal temperature and pH of the purified agarase were $35^{\circ}C$ and pH 7.0, respectively. The purified agarase failed to hydrolyze the other polysaccharide substrates, including carboxymethyl-cellulose, dextran, soluble starch, pectin, and polygalacturonic acid. Kinetic analysis of the agarose hydrolysis catalyzed by the purified agarase using thin-layer chromatography showed that the main products were neoagarobiose, neoagarotetraose, and neoagarohexaose. These results demonstrated that the newly isolated freshwater agarolytic bacterium KY-YJ-3 was a Cellvibrio sp., and could produce an extracellular ${\beta}$-agarase, which hydrolyzed agarose to yield neoagarobiose, neoagarotetraose, and neoagarohexaose as the main products.

• Journal of Microbiology and Biotechnology
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• v.28 no.12
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• pp.2036-2045
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• 2018

An endo-${\beta}$-1,4-glucanase gene, cel5L, was cloned using the shot-gun method from Bacillus sp.. The gene, which contained a predicted signal peptide, encoded a protein of 496 amino acid residues, and the molecular mass of the mature Cel5L was estimated to be 51.8 kDa. Cel5L contained a catalytic domain of glycoside hydrolase (GH) family 5 and a carbohydrate-binding module family 3 (CBM_3). Chromatography using HiTrap Q and CHT-II resulted in the isolation of two truncated forms corresponding to 50 (Cel5L-p50) and 35 kDa (Cel5L-p35, CBM_3-deleted form). Both enzymes were optimally active at pH 4.5 and $55^{\circ}C$, but had different half-lives of 4.0 and 22.8 min, respectively, at $70^{\circ}C$. The relative activities of Cel5L-p50 and Cel5L-p35 for barley ${\beta}$-glucan were 377.0 and 246.7%, respectively, compared to those for carboxymethyl-cellulose. The affinity and hydrolysis rate of pNPC by Cel5L-p35 were 1.7 and 3.3 times higher, respectively, than those by Cel5L-p50. Additions of each to a commercial enzyme set increased saccharification of pretreated rice straw powder by 17.5 and 21.0%, respectively. These results suggest CBM_3 is significantly contributing to thermostability, and to affinity and substrate specificity for small substrates, and that these two enzymes could be used as additives to enhance enzymatic saccharification.

• Mycobiology
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• v.30 no.3
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• pp.166-169
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• 2002

Protein productivity by the cellulolytic fungi, Trichoderma viride(MTCC 800), Chaetomium globosum and Aspergillus terreus was compared in co-culture and mixed culture fermentations of cashewnut bran. Co-cultures were more effective in substrate saccharification, which ranged between $85{\sim}88%$ compared to the $62{\sim}67%$ saccharification shown by the monocultures. Maximum saccharification was induced by T. viride and C. globosum co-culture resulting in the highest 34% release of reducing sugars. The maximum 16.4% biomass protein and the highest protein productivity(0.58%) were shown by T. viride and A. terreus co-culture. A. terreus performed better in co-culture in the presence of T. viride rather than with C. globosum. Among the cellulolytic enzymes, FPase(Filter Paper Cellulase) activity was significantly higher in all the co-cultures and in the mixed culture than in their respective monocultures. Mixed culture fermentation involving all the three fungi was not effective in increasing the per cent saccharification or the biomass protein content over the co-cultures.

• Journal of Life Science
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• v.8 no.3
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• pp.326-332
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• 1998

Cyclodextrin glucanotransferase from B. stearothermophilus KJ16 that can produce both cyclodextrin glucanotransferase and cyclodextrinase was purified by ammonium sulfate precipitation, DEAE-cellulose chromatography, Sephadex G-100 chromatography, and FPLC. The molecular weight of the purifice enzyme was about 65,000 dalton by SDS-PAGE. The optimal pH and temperature were 6.0 and $60^{\circ}C$, respectively. The enzyme was stable at $50^{\circ}C$ for 1 hr and in the pH range of 5.5 and 8.5. Mercaptoethanol and dithiothreitol inhibited the enzyme activity strongly. The enzyme produced 60% cyclodextrin(CD) from 5% soluble starch with the $^{\alpha}$, $^{\beta}$, $^{\gamma}$-CD ratio of 42:46:12. Amylopectin was the most suitable substrate with 67% conversion to CD.