• Journal of Microbiology and Biotechnology
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• v.6 no.1
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• pp.1-6
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• 1996

A bacterial strain NS70 producing an alkaline protease was isolated from soil samples taken near a hot spring and identified as Bacillus licheniformis by its morphological and physiological properties and cellular fatty acid analysis. The isolated alkaline protease was purified by ammonium sulfate fractionation, DEAE-, CM-, and Phenyl-Sepharose column chromatography. The molecular weight of the purified enzyme was estimated to be 32, 000 Da by sodium dodecylsulfate polyacrylamide gel electrophoresis. Its optimal pH and temperature for proteolytic activity against Hammarsten casein were 12 and $65^{\circ}C$, respectively. The enzyme was stable at alkaline pH range from 6.0 to 12.0, and fairly stable up to $65^{\circ}C$. The enzyme was inhibited by phenylmethylsulfonyl fluoride but not by EDTA and N-ethylmaleimide indicating that the enzyme is serine protease. Enzyme activity was markedly inhibited by $Hg^{2+}$ and $Cu^{2+}$. Autolytic phenomena were observed on purified protease NS70 but autolysis was reduced by the addtion of $Ca^{2+}$ ion or bovine serum albumin.

• Journal of Microbiology and Biotechnology
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• v.23 no.7
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• pp.942-952
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• 2013

Monoliths are functional porous materials with a three-dimensional continuous interconnected pore structure in a single piece. A monolith with uniform shape based on poly(${\gamma}$-glutamic acid) (PGA) has been prepared via a thermally induced phase separation technique using a mixture of dimethyl sulfoxide, water, and ethanol as solvent. The morphology of the obtained monolith was observed by scanning electron microscopy and the surface area of the monolith was evaluated by the Brunauer Emmett Teller method. The effects of fabrication parameters such as the concentration and molecular mass of PGA and the solvent composition have been systematically investigated. The PGA monolith was cross-linked with hexamethylene diisocyanate to produce the water-insoluble monolith. The addition of sodium chloride to the phase separation solvent affected the properties of the cross-linked monolith. The swelling ratio of the cross-linked monolith toward aqueous solutions depended on the buffer pH as well as the monolith fabrication condition. Copper(II) ion was efficiently adsorbed on the cross-linked PGA monolith, and the obtained copper-immobilized monolith showed strong antibacterial activity for Escherichia coli. By combination of the characteristic properties of PGA (e.g., high biocompatibility and biodegradability) and the unique features of monoliths (e.g., through-pore structure, large surface area, and high porosity with small pore size), the PGA monolith possesses large potentials for various industrial applications in the biomedical, environmental, analytical, and separation fields.

• Journal of the Korean Applied Science and Technology
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• v.31 no.1
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• pp.92-100
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• 2014

Hydrophobic magnesium hydroxide [$Mg(OH)_2$] was modified by hydrothermal method using non-ionic sorbitol surfactant with Span series. Mganesium chloride [$MgCl_2$] and sodium hydroxide [NaOH] were used for synthesis of $Mg(OH)_2$. Also non-ionic surfactant were added as a stabilizer, dispersant and surface modifier. Addition of non-ionic surfactant was favourable to obtain small sized $Mg(OH)_2$ particles with better dispersibility and hydrophobic property of $Mg(OH)_2$ particles. The obtained product were characterized by particle size analysis(PSA), scanning electron microscope(SEM), energy dispersive spectroscopy(EDS), x-ray diffraction(XRD) and fourier transform infrared spectroscopy(FT-IR). The results show that the product are prepared with this method has a well hydrophobic properties and dispersity compared with unmodified $Mg(OH)_2$ particles. The improve properties of surface modified $Mg(OH)_2$ particles were also verified by similarity synthesizing under slightly different conditions.

• The Korean Journal of Zoology
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• v.36 no.3
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• pp.433-438
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• 1993

In the previous paper (Choi et al., 1992), we found that a large but transient elevation in intracellular cGMP levels occur concomitant with the myoblast fusion. To establish the physiological significance of the elevation of cGMP levels, the change in guanylate cyclase activity dudng myoblast fusion and the correlation hetween various chemicals that may affect guanylate cyclase adivity and myoblast fusion were examined. Sodium nitroprusside, a nitric oxide-forming compound, induced a precocious fusion and increased guanylate cyclase activity compared to the control. Furthermore, L-NG-monomethyl arginine, specific inhibitor of L-arginine: nitric oxide synthase, inhibited the cell fusion in a dose-dependent manner, without affecting biochemical differentiation. On the basis of our present findings, we propose that the onset of myoblast fusion is somehow correlated with the rise in cellular cGMP levels that is regulated by the activation or inhibItIon of soluble guanylate cyclase, via as yet undefined mechanism but possibly through L-arginine: nitric oxide pathway.

• Journal of the Korean Chemical Society
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• v.37 no.3
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• pp.317-326
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• 1993

The acid catalytic reactions of toluene with n-propylalcohol were investigated and the adsorption experiments of dialkylbenzene isomers were carried out at 100$^{\circ}C$ over modified HZSM-5 zeolites. ZSM-5 zeolite was synthesized by the hydrothermal reaction using 4-propylammonium ion, sodium aluminate and colloidal silica etc., and several zeolite catalysts, including H-, K-, Sr-, P-Mg-HZSM-5, H-Y and H-mordenite, were prepared by conventional methods. The main reaction products of toluene with n-propylalcohol over HZSM-5 catalyst include not only xylenes, propyltoluenes, but also ethyltoluenes and high para-selectivity among dialkylbenzene isomers was observed on P-Mg-HZSM-5 zeolite. The diffusion coefficients of various p-dialkylbenzenes are nearly the same, about 1 ${times}$ 10$^{-10}$ cm$^2$/sec and that of m-xylene was about one tenth of o-xylene. These reaction and adsorption characteristics were interpreted in the light of the shape-selectivity related to related to the zeolite pore structure and the zeolitic acidity.

• Membrane and Water Treatment
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• v.7 no.1
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• pp.55-70
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• 2016

Microfiltration/ultrafiltration (MF/UF) Adsorptive polyamide-6 (PA-6) membranes were prepared using wet phase inversion process. The prepared PA-6 membranes are characterized by scanning electron microscopy (SEM), porosity and swelling degree. In this study, the membranes performance has examined by adsorptive removal of copper ions from aqueous solutions in a batch adsorption mode. The $PA-6/H_2O$ membranes display sponge like and highly porous structures, with porosities of 41-73%. Under the conditions examined, the adsorption experiments have showed that the $PA-6/H_2O$ membranes had a good adsorption capacity (up to 120-280 mg/g at the initial copper ion concentration ($C_0$) = 680 mg/L, pH7), fast adsorption rates and short adsorption equilibrium times (less than 1.5-2 hrs) for copper ions. The fast adsorption in this study may be attributed to the high porosities and large pore sizes of the $PA-6/H_2O$ membranes, which have facilitated the transport of copper ions to the adsorption. The results obtained from the study illustrated that the copper ions which have adsorbed on the polyamide membranes can be effectively desorbed in an Ethylene dinitrilotetra acetic acid Di sodium salt ($Na_2$ EDTA) solution from initial concentration (up to 92% desorption efficiency) and the PA-6 membranes can be reused almost without loss of the adsorption capacity for copper ions. The results obtained from the study suggested that the $PA-6/H_2O$ membranes can be effectively applied for the adsorptive removal of copper ions from aqueous solutions.

• YAKHAK HOEJI
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• v.30 no.3
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• pp.149-156
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• 1986

Many experiments have showed that the sodium and potassium ion transporting system and the Na, $^+K^+$-ATPase activity of membrane fragments are inhibited by digitalis glycosides and that the pump may be associated with the pharmacological receptor for the drugs. The aim of our investigation is to elucidate the ouabain binding sites occupation in heart following infusion of ouabain to intact animals by the $^3H$-ouabain binding assay. Lethal dose and 26 percent of lethal dose of ouabain were infused to intact rabbit through ear vein. Microsomal fraction was fractionated from ouabain treated rabbit heart. $^3H$-ouabain binding to these fraction in vitro was studied by the Schwartz's method. $^3H$-ouabain binding to heart microsomal fraction was also studied following infusion of ginseng ethanol extract and caffeine to rabbits respectively. 1) The infusion of lethal dose ouabain (113$\mu\textrm{g}$/kg) inhibited the specific $^3H$-ouabain binding to rabbit heart microsomal fraction to the level of 60% (p<0.01) of control group and the infusion of 26% of lethal dose of ouabain led to the level of 79% (p<0.01) of the control group. 2) Time course of binding of 0.4$\mu{M}$ $^3H$-ouabain to microsomal fraction from rabbit heart following infusion of lethal and 26% of lethal dose of ouabain showed dose dependence at various incubation time. 3) Compared with control, only slight change of $K_d$ and $B_{max}$ was detected in in vitro $^3H$-ouabain binding after infusion of ginseng ethanol extract (300mg/kg) to rabbit. 4) In caffeine infusion group, $^3H$-ouabain binding yielded nearly the same results as control group.

• Journal of Life Science
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• v.16 no.4
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• pp.653-658
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• 2006

An apple polygalacturonase-inhibiting protein (PGIP), that specifically inhibited endopolygalacturonase (PG, EC 3.2.1.15) from Botryosphaeria dothidea, was purified from B. dothidea infected apple (Malus domestica cv. Fuji) fruits. The apple PGIP was a mixed-type inhibitor of PG from B. dothidea. Optimal temperature for the maximum enzyme activity was $40^{\circ}C$, and optimum pH of the purified PGIP was pH 5.0. PGIP was stable up to temperature of $60^{\circ}C$ and was completely suppressed after heating at $70^{\circ}C$ for 10 min, PGIP was stable at pH between 4 and 8. Inhibition of PG by PGIP was reduced by $K^+$, $Cu^{2+}$, $Mg^{2+}$, $Ca^{2+}$ and $Zn^{2+}$ metal ion, sodium dodecyl sulfate (SDS) and 1,2-diaminocyclohexane tetra acetate (CDTA).

• Korean Journal of Microbiology
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• v.25 no.3
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• pp.180-183
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• 1987

Stu I, type II restriction endonuclease, has been purified to homogeneity from Streptomyces tubercidicus (ATCC 25502), and its catalytic properties have been studied. For the purification of Stu I endonuclease free of nonspecific nucleases, DEAE-Sephadex (A-50), QAE-Sephadex (A-50) and Heparin-agarose column chromatography have been performed after ammonium sulfate fractionation of the crude extract. The enzyme was further purified by gel filtration using Sephadex G-100 column to obtain homogeneous form of protein. The single polypeptide species of Stu I endonuclease has a subunit molecular weight of 34,000 $\pm$ 1,000 daltons as judged by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Stu I endonuclease requires $Mg^{2+}$ ion for its activity and is maximally active at neutral pH (7.0-8.0) in the absence of NaCl.

• Journal of Microbiology and Biotechnology
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• v.22 no.7
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• pp.930-938
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• 2012

High levels of xylanase activity (143.98 IU/ml) produced by the newly isolated Paenibacillus campinasensis G1-1 were detected when it was cultivated in a synthetic medium. A thermostable xylanase, designated XynG1-1, from P. campinasensis G1-1 was purified to homogeneity by Octyl-Sepharose hydrophobic-interaction chromatography, Sephadex G75 gel-filter chromatography, and Q-Sepharose ion-exchange chromatography, consecutively. By multistep purification, the specific activity of XynG1-1 was up to 1,865.5 IU/mg with a 9.1-fold purification. The molecular mass of purified XynG1-1 was about 41.3 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sequence analysis revealed that XynG1-1 containing 377 amino acids encoded by 1,134 bp genomic sequences of P. campinasensis G1-1 shared 96% homology with XylX from Paenibacillus campinasensis BL11 and 77%~78% homology with xylanases from Bacillus sp. YA-335 and Bacillus sp. 41M-1, respectively. The activity of XynG1-1 was stimulated by $Ca^{2+}$, $Ba^{2+}$, DTT, and ${\beta}$-mercaptoethanol, but was inhibited by $Ni^{2+}$, $Fe^{2+}$, $Fe^{3+}$, $Zn^{2+}$, SDS, and EDTA. The purified XynG1-1 displayed a greater affinity for birchwood xylan, with an optimal temperature of $60^{\circ}C$ and an optimal pH of 7.5. The fact that XynG1-1 is cellulose-free, thermostable (stability at high temperature of $70^{\circ}C{\sim}80^{\circ}C$), and active over a wide pH range (pH 5.0~9.0) suggests that the enzyme is potentially valuable for various industrial applications, especially for pulp bleaching pretreatment.