• Title/Summary/Keyword: Ion gel

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Characterization of Selectively Absorbing Properties of Indium Tin Oxide Thin Films by UV-VIS-IR Spectroscopy (UV-VIS-IR 분광법에 의한 산화 인듐 주석 박막의 선택적 투과 흡수 특성 관찰)

  • Lee, Jeon-Kook;Lee, Dong-Heon;Cho, Nam-Hee
    • Analytical Science and Technology
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    • v.5 no.1
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    • pp.135-142
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    • 1992
  • Indium tin oxide(ITO) films coated on the window glass selectively transmit the solar energy and infrared. We call this system passive solar collectors. Selectively absorbing properties of sol gel dip coated ITO films were characterized by UV-VIS-NIR spectroscopy. The effects of heat treating temperature, time, atmosphere, substrate and barrier layers are concerned. Indium tin oxide films heat-treated at $500^{\circ}C$ in a reducing atmosphere show intrinsic properties. Efficiency of solar energy transmittance was enhanced by coating of $SiO_2-ZrO_2$ as an alkali ion barrier layer. Energy was saved by the double layers of $SiO_2-ZrO_2$ and ITO since solar energy is transmitted and heat generated inside(${\lambda}$ > 2700nm) is reflected.

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The Electrochemical Properties and Synthesis of V2O5 Xerogel using H2O2 (과산화수소를 이용한 V2O5 Xerogel의 합성 및 전기화학적 특성)

  • Park, Heai-Ku;Jung, Jae-Youb;Lee, Man-Ho
    • Applied Chemistry for Engineering
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    • v.16 no.1
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    • pp.107-111
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    • 2005
  • We have performed a study on the electrochemical characteristics and nuclear ($^7Li$) magnetic resonance of $V_2O_5$ xerogels that have been synthesized by the sol-gel reaction of $V_2O_5$ powder with hydrogen peroxide. NMR measurements revealed that chemical shift of $Li^+$ ions varied as lithium ions were inserted into $V_2O_5$ xerogel and that several different sites for $Li^+$ ions existed in the $V_2O_5$ xerogel structure. The electrochemical properties of the xerogel electrodes did not depend much upon the concentration of $V_2O_5$ and HCl that were used for the synthesis of $V_2O_5$ gels. The specific capacity of $V_2O_5$ xerogels were about 140 mAh/g, similar to that of the xerogels prepared by the ion exchange method.

Significance of Urease Distribution across Helicobacter pylori Membrane

  • Gang, Jin-Gu;Yun, Soon-Kyu;Choi, Kyung-Min;Lim, Wang-Jin;Park, Jeong-Kyu;Hwang, Se-Young
    • Journal of Microbiology and Biotechnology
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    • v.11 no.2
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    • pp.317-325
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    • 2001
  • For heuristic purposes, the relative ratio of urease contents inside and outside cells was surveyed using nine ureB+ strains of Helicobacter pylori. the ratio of the enzyme specific activity appeared to vary greatly between the various H. pylori strains, ranging from 0.5 to 2.5. Besides the above compartment, urease was also richly found in the membrane fraction, especially in either peripheral or integral form. The urease distribution across the H. pylori membrane was significantly influenced by the ambient pH; the specific activity of external urease was highest at pH 5.5 with a narrow plateau, whereas the internal specific activity was highest within a pH range of 4.5 to 6.5 with a broad plateau. These finding strongly suggest that H. pylori urease is secretory and responded to the external pH. However, at pH 4.0 or below, no urease activity was detected in either the internal or external compartment, although an increase in the color development with 2,4,6-trinitrobenzene sulfonate (TNBS) was observed. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that these phenomena may be related to a specific proteolysis in certain proteins, including urease or ${\gamma}$-glutamyl transpeptidase. Interestingly, the effect of ammonium ions n alleviating the enzyme inactivation inside the H. pylori cells was remarkably similar to that of D-glucose. In addition, it would appear that the cation acted as a surrogate of not only $Na^+$ but also $K^+$ thereby increasing the H. pylori P-type ATPase activity. This is of great interest, as it implies that the urease action in H. pylori is indispensible at any locus.

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Removal of Skin from Filefish Using Enzymes (효소를 이용한 말쥐치의 탈피)

  • KIM Se-Kwon;BYUN Hee-Guk;CHOI Kwang-Duck;ROH Ho-Seok;LEE Won-Hee;LEE Eung-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.26 no.2
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    • pp.159-172
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    • 1993
  • Collagenase existed in the internal organs of filefish Novoden modestrus was isolated with ammonium sulfate and was purified by ion exchange column chromatography with DEAE-Sephadex A-50 and gel filtration with Sephadex G-150. The activity of the purified enzyme was increased 92.4 folds than that of the crude one and the yield of the purified one was $10.9\%$. The optimum conditions showing the maximum activity of the crude enzyme to digest insoluble collagen(Type I) were $55^{\circ}C$ and pH 8.0, while those showing the maximum activity of the purified one were $55^{\circ}C$ and pH 7.75. However, the use of the crude enzyme for skinning of filefish was more profitable because the yield was 800 folds higher than that of the purified one and the cost was also able to economy. When hydrolysis for skinning of filefish was conducted with $0.3\%$(w/w) crude collagenase at $50^{\circ}C$ and pH 8.0 for 3hrs, there was some problem to cause a damage on muscle of the fish by heat. To solve such problem for the skinning, the hydrolysis at $18^{\circ}C$ for 4hrs with $0.3\%$ (w/w) crude enzyme after pretreated with 0.5M acetic acid for 10 min provided a good result for skinning of filefish.

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Fractionation and Enzymatic Characterization of Endoprotease and Exopeptidase from Crude Extracts of Cuttlefish Sepia officinalis Hepatopancreas

  • Kim, Min Ji;Kim, Hyeon Jeong;Kim, Ki Hyun;Heu, Min Soo;Lee, Jung Suck;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • v.15 no.4
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    • pp.283-291
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    • 2012
  • This study examines the optimal fractionation method and conditions for the isolation of endoprotease- and exopeptidase-active fractions from crude extracts of cuttlefish hepatopancreas (HP) using four fractionation methods: ammonium sulfate fractionation (ASF), polyethylene glycol fractionation (PGF), ion exchange chromatography (IEC), and gel filtration chromatography (GFC). Total endoprotease activity highest in the fraction II (concentrate of fractions 34-42; 842.60 U) of GFC, followed by fraction III (40-60% ammonium sulfate fraction; 670.25 U) of ASF, fraction I (concentrate of fractions 8-12; 436.89 U) of IEC, and fraction II (10-20% polyethylene glycol; 307.31 U) of PGF. Total exopeptidase activity of these fractions was highest in fraction II (2,704.70 U) of GFC, fraction III (2,110.50 U) of ASF, fraction III (1,605.60 U) of PGF, and fraction II (concentrate of fractions 38-44; 1,196.22 U) of IEC. These results showed that fraction II of GFC had the highest activity toward both exopeptidase and endoprotease, with exopeptidase activity being 3.21 times higher than of endoprotease. These results suggest cuttlefish HP could be used as a potential source for the extraction of exopeptidase, an enzyme capable of catalyzing the cleavage of N- and C-terminal amino acids in polypeptides, Like endoprotease, the most efficient method for separating exopeptide-active fractions was GFC.

Characteristics of Heavy Metal Ion Adsorbent Extracted from Crab Shell (Crab Shell로부터 추출한 중금속 흡착제들의 특성)

  • 현근우;이찬기;이해승
    • Journal of environmental and Sanitary engineering
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    • v.14 no.2
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    • pp.46-55
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    • 1999
  • This study compared the adsorption characteristics of heavy metal ions by crab shell, treated crab shell with 2N-HCl, treated crab shell with 4%-NaOH, chitin and chitosan.Using crushed crab shell, the heavy metal ions removal rates of $Cd^{2+}$ and $Zn^{2+}$ were about 70-80% in 45minutes, but the removal rates of $Cu^{2+}$, $Cr^{6+}$ and $Pb^{2+}$ was less than 10%, 10% and 30%, respectively. For the by-products crab shell by 2N-HCl treatment, it was shown that the removal rates of $Cu^{2+}$ and $Pb^{2+}$ were about 70-80% in 45minutes reaction. But, some problems were observed, that the contained protein in crab shell was changed into gel in the mixing solution after a few hours. For the by-products of crab shell by 4%-NaOH treatment, the removal rates of Pb and Zn were about 90% in 45 minutes, and those of capacity of chitin and chitosan powder was better than those of the other by-products. The more adding to the adsorbent dosages increased the removal rates, and the adsorption reaction was rapidly occurred in a few minute. Using 1.0 wt% chitin powder, the heavy metal removal rates were ordered $Cu^{2+}$(94%) > $Zn^{2+}$(89%) > $Cd^{2+}$(88%) > $Pb^{2+}$(77%) > $Cr^{6+}$(58%) in 45 minutes. Using 1.0 wt% chitosan powder, the heavy metal removal rates were ordered $Cu^{2+}$(99%) > $Pb^{2+}$(96%) > $Cd^{2+}$(79%) > $Zn^{2+}$(71%) > $Cr${6+}$(46%) in 45minutes. The degree of degree of deacetylation by prepared chitosan was 91%.The Freundlich adsorption isotherm of $Cu^{2+}$, $Cd^{2+}$ and $Zn^{2+}$, when it was applied to 1.0 wt% chitosan powder in minutes, can be acceptable very strictly. The equation constant (1/n) for $Cu^{2+}$, $Cd^{2+}$ and $Zn^{2+}$ were 0.54 0.41 and 0.23 respectively.

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Studies on Antitumor Components of Cultured Basidiomycetes - Purification and Chemical Analysis of Antineoplastic Constituents of Cultured Mycelia of Laccaria laccata - (애기졸각버섯 배양(培養) 균사(菌絲)의 항암(抗癌) 성분(成分)의 정제(精製) 및 화학(化學) 분석(分析))

  • Kim, Yoo-Jin;Lee, Chong-Ock;Shim, Mi-Ja;Kim, Sung-Won;Choi, Eung-Chil;Kim, Byong-Kak
    • The Korean Journal of Mycology
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    • v.12 no.1
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    • pp.35-43
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    • 1984
  • To produce and characterize antineoplastic constituents in the submerged cultured­mycelia of Laccaria laccata, the mycelia were extracted with distilled water. Purification of the extract was carried out by acetone precipitation, by ion exchange chromatography using DEAE­Sephadex A-50, CM-Sephadex C-25 resins, and by gel filtration chromatography on Sephadex G-200. Each fraction obtained during the purification was examined for antineoplastic activity against sarcoma 180 in ICR mice. As the purification proceeded, the antineoplastic activity was markedly increased. The highly purified Fraction E showed 75% tumor inhibition ratio at a dose of 10mg/kg/day and contained 81% polysaccharide and 4% protein. The antitumor component of Fraction E stimulated an accumulation of peritoneal exudate cells including peritoneal macrophages, and is named laccaran.

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Micro Emulsion Synthesis of LaCoO3 Nanoparticles and their Electrochemical Catalytic Activity

  • Islam, Mobinul;Jeong, Min-Gi;Ghani, Faizan;Jung, Hun-Gi
    • Journal of Electrochemical Science and Technology
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    • v.6 no.4
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    • pp.121-130
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    • 2015
  • The micro emulsion method has been successfully used for preparing perovskite LaCoO3 with uniform, fine-shaped nanoparticles showing high activity as electro catalysts in oxygen reduction reactions (ORRs). They are, therefore, promising candidates for the air-cathode in metal-air rechargeable batteries. Since the activity of a catalyst is highly dependent on its specific surface area, nanoparticles of the perovskite catalyst are desirable for catalyzing both oxygen reduction and evolution reactions. Herein, LaCoO3 powder was also prepared by sol-gel method for comparison, with a broad particle distribution and high agglomeration. The electro catalytic properties of LaCoO3 and LaCoO3-carbon Super P mixture layers toward the ORR were studied comparatively using the rotating disk electrode technique in 0.1 M KOH electrolyte to elucidate the effect of carbon Super P. Koutecky-Levich theory was applied to acquire the overall electron transfer number (n) during the ORR, calculated to be ~3.74 for the LaCoO3-Super P mixture, quite close to the theoretical value (4.0), and ~2.7 for carbon-free LaCoO3. A synergistic effect toward the ORR is observed when carbon is present in the LaCoO3 layer. Carbon is assumed to be more than an additive, enhancing the electronic conductivity of the oxide catalyst. It is suggested that ORRs, catalyzed by the LaCoO3-Super P mixture, are dominated by a 2+2-electron transfer pathway to form the final, hydroxyl ion product.

Novel Purification and Characterization of Glucose oxidase from Aspergillus niger (Aspergillus niger Glucose oxidase의 새로운 정제 방법 및 특성)

  • 한상배;김광진
    • KSBB Journal
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    • v.9 no.1
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    • pp.55-62
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    • 1994
  • Glucose oxidase(EC 1.1.3.4) was purified to electrophoretic homogeneity from Aspergillus niger by a combination of ammonium sulfate fractionation, ion exchange chromatography, and ultrafiltration. Two active fractions A and B, of glucose oxidase were obtained from the hydrophobic chromatography on phenyl sepharose CL-4B. The enzyme A and B were glycoproteins with the same denatured molecular weight of 78, 000 and had specific activities of 2, 191 and 1, 273-units/mg proteins, respectively. But the two enzymes showed differences in native molecular weight that was measured by HPLC gel filteration, maximum absorbtion wavelength and isoelectric point. The enzyme A oxidized $\beta$-D-glucose only and was resistant to sodium dodecyl sulfate. Activity optimum was found at $30^{\circ}C$ and pH 3.5. Also the enzyme A was inhibited greatly by $Hg^{2+}$(10mM). The results of chemical modification experiments suggested that cysteine and cystine residues might be involved in the active site of the enzyme A.

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Studies on Producing Anti-microbial Factor from Human Promyelocytic Cells (인간 전과립 세포로부터 항미생물 인자의 생산에 관한 연구)

  • 박영식;김태호
    • KSBB Journal
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    • v.10 no.2
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    • pp.131-136
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    • 1995
  • 0.374(1/day) of specific growth rate and 0.435(mg/108 viable cells) of Anti-Microbial factor (AMF) productivity were obseaved for the batch cultivation of human promyelocytic cells in 10% serum containing medium. The crude protein was purified 10 folds by a serial purification steps of ion exchange chromatography, Bio-Rex 70 and gel filtration chromatography, Sephadex G-70 and 100. The ranges of MIC(Minimal Inhibitory Concentration) of commercially available antibiotics, penicillin G, streptomycin and ampicillin was estimated as 40 to ($70\mu\textrm{g}$/ml) on Gram (-) E. coli and Gram (+) Streptococcus aureus. The values of the MBC (Minimal Bactericidal Concentration) of Purified AMF was ($0.5\mu\textrm{g}$/ml) and 0.4($\mu\textrm{g}$/ml), respectively. The molecular weight of the AMF was estimated as 15,000 dalton by SDS-PAGE.

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