• Proceedings of the Korea Concrete Institute Conference
• /
• 1992.04a
• /
• pp.90-94
• /
• 1992

ACI318-89 Recommened that when the specified compressive strength of concrete in a column is greater than 1.4 times that specified for a floor system, top surface of the column concrete shall extend 2ft (600mm) into the slab from the face of column to avoid unexpected brittle failure. The major variables are extension distance, compressive strength of concrete (f'c), shear confinement ratio(Vs), and loading types. The test results showed that the load capacity of the specimen subjected to monotonic loading had more than that of the specimen subjected to one way cyclic loadings. The failure models of specimens under cyclic loading were concentrated at 5∼20cm apart region from beam-column joint face. Ducility index(μf) are increased with increasing of shear confinement ratio. The specimen with 2ft extension distance shows more ductility than specimen with lft extension distance.

• Microbiology and Biotechnology Letters
• /
• v.7 no.3
• /
• pp.149-155
• /
• 1979

Streptomyces sp. 115-5 was selected as the most active microorganism of about 200 strains for the production of chitinase. The enzyme was purified by (NH$_4$)$_2$SO$_4$ treatment, 1st-Sephadex G-100, DEAE-Cellulose, 2nd-Sephadex G-100 column chromatography, and evidence for homogenity was obtained from CM-Sephadex C-50 column chromatography and polyacylamide gel electrophoresis. The purified enzyme hydrolyzed chitin (N-acetyl glucosamine polymer) and chitosan (glucosamine polymer) but not cellulose. And with chitin as the substrate, a Km value of 3.6 mg of chitin per ml and a Vmax of 100 $\mu$mo1e fer hr were found. The activation of the chitinase was 3.66 kcal per mole. The molecular weight of the enzyme was esti-mated about 56,000 daltons by Sephadex G-100 chromatography and isoelectric point as pH 3.0.

• Korean Journal of Food Science and Technology
• /
• v.28 no.3
• /
• pp.600-603
• /
• 1996

The methanol extract of Aralia elata bark showed antimicrobial activities against bacteria, yeast and fungi. The active components were successively purified with solvent fractionation, silica gel adsorption column chromatography, Sephadex LH-20 column chromatography, silica gel partition column chromatography and HPLC. The active substances were separated with HPLC where 1% acetic acid-MeOH (60 : 40, v/v) was used as mobile phase. The isolated active substance ($t_r$ 17.1 min) was identified as trans-3,4-dihydroxycinnamic acid by $MS,\;^1H-NMR\;and\;^13C-NMR$.

• Analytical Science and Technology
• /
• v.5 no.4
• /
• pp.389-399
• /
• 1992

Liquid Chromatographic behavior of Pd(II) in Isonitrosoethylacetoacetate lmine, $Pd(IEAA-NR)_2$ (R=H, $CH_3$, $C_2H_5$, $n-C_3H_7$, $C_6H_5-CH_2$, $n-C_4H_9$) chelates were investigated by reversed-phase HPLC on Micropak MCH-5 column using methanol/water as mobile phase. The optimum conditions for the separation of $Pd(IEAA-NR)_2$ chelates were examined with respect to the effect of the flow rate, sample solvent, mobile phase strength and column temperature. It wass found that metal chelates were properly eluted in an acceptable range of capacity factor value($0{\leq}log\;k^{\prime}{\leq}1$). The dependence of the logarithm of capacity factor(k') on the volume fraction of water in the binary mobile phase was examined. Also, the dependence of k' on the liquid-liquid extration distribution ratio($D_c$) in methanol-water/n-alkane extration system was investigated. Both kinds of dependence are linear, which susggests that the retention of the electroneutral metal chelate is largely due to the solvophobic effect. Standard adsorption enthalpy changes (${\Delta}H^{\circ}$) and standard adsorption entropy changes (${\Delta}S^{\circ}$) of Pd(II) Isonitrosoethylacetoacetate imine chelates on Micropak MCH-5 column were calculated by measuring capacity factor with changing temperature of the column.

• Journal of Environmental Science International
• /
• v.4 no.3
• /
• pp.295-301
• /
• 1995

Continuous deodorization of malodorous sulfur compounds by Thiobaillus neapolitanusts R-10 immobilized onto a polypropylene pellet was studied using a column reactor at 30$^{\circ}$C. The maximum amounts of immobilized cells was 5.3 gall polypropylene with 5$\times$7.5mm in pellet size, and the amounts of immobilized cells in the higher part of the column was as twice as in the lower part. The optimum pH and temperature for removal of dimethyl sulfide were 6.0 and 30$^{\circ}$C, respectively. When 5-20 ${mu}ell$/l of hydrogen sulfide and methylmercaptan were employed 98% of removal efficiency were achieved. In contrast, lower concentrations of dimethyl sulfide and dimethyldisulfide should be supplied to meet satisfactory deodorization efficiency. The immobilized cell column was successfully operated for the deodorization of mixture of sulfur compounds over 15 days without significant loss of initial activity achieving high efficiency.

• Applied Biological Chemistry
• /
• v.47 no.4
• /
• pp.379-383
• /
• 2004

For the elucidation of substrate specificity to the brown copra meal by Bacillus sp. ${\beta}-mannanase.$, the enzymatic hydrolysate after 24 hr of reaction was heated in a boiling water bath for 10 min, and then centrifuged to remove the insoluble materials from hydrolysates. The major hydrolysates composed of D.P 5 and 7 galactosyl mannooligosaccharides. For the separate of galactosyl mannooligosaccharides, the supernatant solution of 150 ml was put on a first activated carbon column. The column was then washed with 5 l of water to remove mannose and salts. The oligosaccharides in the column were eluted by a liner gradient of $0{\sim}30%$ ethanol, at the flow rate of 250 ml per hour. The sugar composition in each fraction tubes was examined by TLC and FACE analysis. The combined fraction from F3 was concentrated to 30 ml by vacuum evaporator. Then put on a second activated carbon column. The oligosaccharides in the column were eluted by a liner gradient of $0{\sim}30%$ ethanol (total volume: 5 l), at the flow rate of 250 ml per hour. The eluent was collected in 8 ml fraction tubes, and the total sugar concentration was measured by method of phenol-sulfuric acid. The major component of F2 separated by 2nd activated carbon column chromatography were identified $Gal^3Man_4(6^3-mono-{\alpha}-D-galactopyranosyl-{\beta}-mannotetraose)$. To investigate the effects of brown copra meal galactomannooligosaccharides on growth of Bifidobacterium longum, B. bifidum were cultivated individually on the modified-MRS medium containing carbon source such as $Gal^3Man_4$, compared to those of standard MRS medium.

• Journal of the Earthquake Engineering Society of Korea
• /
• v.3 no.4
• /
• pp.83-94
• /
• 1999

High-strength concrete has demonstrated characteristics of both increased strength and enhanced durability; hence its use has become more and more widespread. But, due to the lack of experimental evidance on the seismic performance of frame members constructed with high-strength concrete, the current codes of their design provisions are based on normal concrete test. The purpose of this study is to compare the response of the high-strength concrete beam-column-slab subassemblies with the response of a normal-strength concrete specimens. Four assemblies $(f_c'=240kg/\textrm{cm}^2, f_c'=700kg/\textrm{cm}^2)$ with 2/3 scale were designed and tested to investigate seismic behavior.

• Microbiology and Biotechnology Letters
• /
• v.33 no.2
• /
• pp.123-129
• /
• 2005

Isolation and identification of pathogens from slaughter and meat processing plant were investigated. Antimicrobial activity of Amaranthus lividus against isolated pathogens such as Aeromonas sobria, Escherichia coli, Escherichia coli O157, Listeria monocytogenes, Salmonella spp., and Staphylococcus aureus was investigated. Among the chloroform, ethyl acetate and buthanol fraction of amaranthus lividus showed inhibitory effect against Aeromonas sobria CLFM1 and Escherichia coli CLFM2. Antimicrobial substance in chloroform fraction was isolated by silica gel adsorption column chromatography, sephadex LH-20 column chromatography and silica gel partition column chromatography. The antimicrobial compound of amaranthus lividus was identified as diethyl phtalate by HPLC, GC-MS, H-NMR and C-NMR.

• Journal of the Korean Society of Food Culture
• /
• v.5 no.2
• /
• pp.269-274
• /
• 1990

This study was conducted to determine invertase activity in persimmon during the drying process and characterize the purified enzyme. As drying proceeded, invertase activity increased until 10 days and decreased gradually afterwards. Invertase in persimmon fruit was extracted with 250 mM potassium phosphate sulfate buffer at pH 7.4. The enzyme was purified by means of ammonium sulfate fractionation, column chromatography on DEAE-cellulose and gel filtration on Sephadex G-200 column. The optimal temperature of enzyme was $40^{\circ}C$ and optimal pH was 5.0 and 6.0 for sucrose and raffinose, respectively. The enzyme was stable up to $50^{\circ}C$ and pH 3-6. The Km value of the enzyme, with sucrose as a substrate, was 2.5mM. Electrophoretic pattern of purified enzyme solution showed a single band.

• Microbiology and Biotechnology Letters
• /
• v.2 no.3
• /
• pp.133-140
• /
• 1974

1) Two xylanase (designed as A and B) of Myriococcus albomyces were purified from an extract of wheat koji culture. Puriscation steps included first ammonium sulfate fractionation followed successively by SE-Sephadex column chromatgraphy. DEAE-Sephadex column chromatography and gel filtration on Sephadex G-100 repectively. 2) The optimum pH and pH stability for crude xylanse were found to be pH 5.0 and pH 4.0-7.0 respectively. 3) The optimium temperature was found to he 5$0^{\circ}C$ and for the thermal statbility of xylanase, the enryme incubated at $65^{\circ}C$ for 60min did not affect their stability. 4) The purised xylanase A and B were considered as liquefying xylanase and saccharogenic xylauase repectively. 5) The Bylanase A was most active at pH 4.0 and range of pH 3.0-8.0 at 3$0^{\circ}C$ for six hrs. The B was most active at pH 5.0 showing stability range of pH 4.0 to 8.5 at 3$0^{\circ}C$ for 6 hrs. incubation respectively. The Optimum temperature of xylanase A and B were found to be 7$0^{\circ}C$ and $65^{\circ}C$ for 60min repectively.