• Title/Summary/Keyword: acidic pH

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Development and Stability Evaluation of Enteric Coated Diclofenac Sodium Tablets Using AquaPolish E.

  • Zaid, A.N.;Fadda, A.M.;Nator, S.;Qaddumi, A.
    • Journal of Pharmaceutical Investigation
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    • v.41 no.4
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    • pp.211-215
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    • 2011
  • The aim of this study was to develop a stable enteric coated diclofenac sodium (DFS) tablets using Aqua-Polish E without using a subcoat. DFS uncoated tablets were manufactured through the non direct compression process. AquaPolish E white aqueous coating dispersion was used as enteric coating material. This film forming polymer is a mixture of selected polymethacrylic/ethylacrylate copolymers. The stability of the obtained enteric coated tablets was evaluated according to ICH guidelines. No signs of disintegration or cracking was observed when they placed in 0.1N HCl solution (pH1.2), but they were completely disintegrated within 10 minutes when they placed in buffered solution at pH6.8. Dissolution test was also conducted by placing tablets in 0.1 N HCl for 2 hours and then 1 hour in phosphate buffer at pH 6.8. Less than 0.9 % of drug was released in the acidic phase and up to 97% in the basic medium. These findings suggest that aqueous enteric coating with AquaPolish E system is an easy and economical approach for preparing stable DFS enteric coat without the use of a subcoating layer.

Adsorption of Dyes Reactive Blue 221, N Blue RGB and Acid Blue MTR on Two Different Samples of Activated Carbon

  • Kant, Rita;Rattan, V.K.
    • Carbon letters
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    • v.11 no.3
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    • pp.206-210
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    • 2010
  • Removal of dyes Reactive Blue 221, N Blue RGB and Acid Blue MTR using two different samples of activated carbon by static batch method was studied. Experimental data on optical density of solutions at different concentrations ranging from 10 to 100 mg/L and of solutions after adsorption on activated carbon samples were measured. Calibration curves were plotted and the amount of dye $q_e$ adsorbed was calculated. The data was fitted to Langmuir and Freundlich isotherms for two different carbon samples and different concentration and pH values. Constants were calculated from the slope and intercept values of the isotherms. Coefficient of correlation $R_2$ and Standard Deviation SD were also noted. The data fitted well to the isotherms. Carbon sample $C_1$ showed higher potential to adsorb all the three dyes. Adsorption was higher at lower concentrations. Carbon sample $C_2$ showed better adsorption in acidic pH as compared to in alkaline pH. From the analysis of the data capacity of $C_1$ and $C_2$ to remove the dyes from water have been compared.

Purification and Characterization of Carboxymethyl Cellulase from Stropharia rugosoannulata (독청버섯아재비 균주가 생산하는 Carboxymethyl Cellulase의 정제 및 효소학적 특성)

  • Yoo, Kwan-Hee;Chang, Hyung-Soo
    • The Korean Journal of Mycology
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    • v.30 no.2
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    • pp.113-118
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    • 2002
  • A Carboxymethyl Cellulase (CMCase) has been isolated and purified from the edible mushroom, Stropharia rugosoannulata. The molecular weight of CMCase was estimated to be 54 kDa by SDS polyacryl amide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $40^{\circ}C$, and stable for pH 3.0 to 11.0 to maintain 40% activity. The CMCase activity was activated by $AgNO_{3},\;MgSO_{4},\;and\;KCl$. However, its activity was inhibited by 1,10-phenanthroline, KCN and L-cysteine. Also, the enzyme activity was decreased by the addition of EDTA, suggesting that the purified CMCase is metalloenzyme.

Purification and Properties of Glucoamylase from Schwanniomyces castellii (Schwanniomyces castellii Glucoamylase의 정제 및 성질)

  • Bai, Suk;Park, Jong-Chun;Kim, Dong-Ho;Kim, Kang-Hwa;Chun, Soon-Bai
    • Korean Journal of Microbiology
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    • v.29 no.2
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    • pp.104-110
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    • 1991
  • The glucoamylase of Schwanniomyces castellii was purified to homogeneity from the culture filtrate. the purified enzyme was a glycoprotein with a molecular mass of about 145 KDa, which was monomeric protein with an isoelectric point of 4.3. The pH and temperature optima were 5.5 and 40.deg.C, respectively. The enzyme was fairly stable up to 50.deg.C and at acid pH range (pH 4.5-6.0). The apparent Km of the enzyme toward soluble starch, isomaltose and pullulan were 3.84, 0.51 and 13.7 mg/ml, respectively. The analysis of amino acid composition on this enzyme was found to be acidic protein like other fungal glucoamylase. The amino acid sequence of N-terminal peptide consisted of Ala-Pro-Ala-Asp-Gly-Ile-Gly-Asp-X-Ala-X-Ala.

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Peroxidase Activity Boosting by Various Nitrogenous Compounds

  • Lee, Dong-Joo;Kim, Soung-Soo;Lee, Mi-Young
    • BMB Reports
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    • v.33 no.4
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    • pp.312-316
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    • 2000
  • Effects of various nitrogenous compounds on the peroxidative activity of Korean radish (Rophanus sativus L.) isoperoxidase $A_1$ were examined by using anilino substrates, such as dianisidine and phenylenediamine. We also used phenolic substrates such as guaiacol, chlorogenic acid, caffeic acid, ferulic acid and esculetin. The peroxidation of dianisidine was stimulated by adenine and imidazole as much as 5 fold and 11 fold, respectively at pH 8. Moreover, about 4.8 fold and 8 fold stimulation of phenylenediamine peroxidation occurred by adenine and imidazole, respectively at pH 8. The stimulation by adenine and imidazole did not occur at the acidic pH range. The peroxidations of phenolic substrates, such as guaiacol, chlorogenic acid, caffeic acid, ferulic acid and esculetin, were not boosted greatly by any of the nitrogenous compounds tested. Notably, ammonium salt, which has been known for the excellent booster of horseradish peroxidase, did not affect the peroxidation of the Korean radish isoperoxidase $A_1$. The kinetic studies of dianisidine peroxidation with imidazole, as a model of boosting reaction, showed that neither the affinity of imidazole against dianisidine, nor the activation energy of dianisidine peroxidation changed during the activity boosting of isoperoxidase $A_1$.

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Purification and Properties of Alcohol Oxidase Produced by Hnasenula sp. MS-364 (Hansenula sp. MS-364가 생산하는 Alcohol Oxidase 의 정제 및 성질)

  • 김병호;김형만;권태종
    • Microbiology and Biotechnology Letters
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    • v.23 no.1
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    • pp.60-67
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    • 1995
  • Methanol assimilating yeast, Hansenula sp. MS-364 that has high productivity with methanol as carbon and energy source has been preserved at dept. of Microbiological engineering. Purification and properties of alcohol oxidase (E.C.1.1.3.13: oxygen oxidoreductase) were investigated in the methanol assimilating yeast, Hansenula sp. MS-364. Alcohol oxidase is related to the catalytic reaction that degrades alcohol to aldehyde and peroxide. The methanol oxidizing enzyme was purified by ammonium sulfate precipitation, DEAE-Sephadex A-50 chromatography and gel filtration on Sepharose 6B from cell-free extract. The purified enzyme preparation gave a single band in the sodium dodesyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of the enzyme was calculated to be about 576,000 and molecular weight of subunit was also calculated to be 72,000. The optimal pH and temperature of the enzyme reaction were pH 7.5 and 37$\circ$C, respectively. The enzyme was unstable in acidic pH and higher temperature. The enzyme was not specific for methanol and also oxidized lower primary alcohols. The Km value for methanol was 2.5 mM and that for ethanol was 1.66 mM. The enzyme was heavily inhibited by metal ions such as Hg$^{2+}$, Ag$^{2+}$, Cu$^{2+}$. The high concentration of EDTA and sulfhydryl reagents strongly inhibited the enzyme activity. The component of coenzyme was determined to flavin adenine dinucleotide.

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The Purification and Properties of $\alpha$-Amylase from Schwanniomyces casrellii CBS 2863 (Schwanniomyces castellii CBS 2863(ATCC 26077)으로부터 $\alpha$-Amylase 정제 및 특성)

  • Park, Jong-Chun;Bai, Suk;Lim, Suhn-Young;Lee, Jin-Jong;Lee, Hyang;Chun, Soon-Bai
    • Microbiology and Biotechnology Letters
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    • v.21 no.6
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    • pp.582-587
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    • 1993
  • The extracellular alpha-amylase was purified to homogenity from the culture filtrate of starch grown Sch. castellii CBS 2863. The purified enzyme was glycoprotein with a molecular weight of about 56 kDa. The pH and temperature optimum were 5.5 and 40C, respectively. The enzyme was fairly stable up to 40C and at acid pH range (pH 4.0-7.0). The apparent Km and Vmax of the enzyme toward starch was 1.0mg/ml and 100U/mg protein, respectively. The analysis of amino acid composition was found to be acidic protein. The amino acid sequence of N-terminal peptide consisted of Asp-Val-Ser-Ser-Ala-X-X-Thr-Arg-Ser-Glu-Ser-Ile-Tyr.

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Purification and Characterization of Carboxymethyl Cellulase from Loweporus roseoalbus (Loweporus roseoalbus가 생산하는 Carboxymethyl Cellulase의 정제 및 특성)

  • Chang, Hyung-Soo;Kim, Jun-Ho;Yoo, Kwan-Hee
    • The Korean Journal of Mycology
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    • v.33 no.2
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    • pp.75-80
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    • 2005
  • A carboxymethyl cellulase (CMCase) has been purified from Loweporus roseoalbus. The molecular weight of the purified CMCase was estimated to be 28.5 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $30^{\circ}C$, and stable for pH 3 to 5 to maintain 60% activity. The CMCase activity was activated by SDS and inhibited by PMSF and 1,10-phenanthroline. The enzyme activity was also decreased by the addition of ethylene diamine tetraacetic acid (EDTA), suggesting that the purified CMCase is metalloenzyme.

Evaluating Cadmium Ion Removal in Aqueous Solutions and Cytotoxicity Evaluation of Carbon, Synthesized Layered Double Hydroxide, and Multi-wall Carbon Nanotube (활성탄, 합성 층상이중층 수산화물, 카본나노튜브를 이용한 수용액상의 카드뮴의 제거와 흡착제 독성 연구)

  • Kim, Tae-Gyung;Park, Bog-Soung;Jung, Yong-Jun
    • Journal of Korean Society on Water Environment
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    • v.33 no.2
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    • pp.211-218
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    • 2017
  • This experiment was carried out with the purpose of testing cadmium adsorption abilities of multi wall carbon nanotube (MWCNT), activated carbon, and synthesized layered double hydroxide (LDH). In the acidic condition, only MWCNT was effective for removing cadmium ion in the aqueous phase while other adsorbents rarely removed it. The MWCNT and cadmium ion adsorption reactions followed pseudo-first order kinetic. When the initial pH value was neutral (pH = 7), cadmium ion was rapidly removed by MWCNT and activated carbon in 4 hr (100% and 99.2%, respectively). Increasing adsorbent dosages affects the pH evolution and cadmium ion removal (0 to 99%). Cytotoxicity test showed that both MWCNT and LDH has low cytotoxic effects on three kind of human cells (A549, HS-294t, and HT-29).

Service Life Prediction of Concrete Structures Exposed to a Sulfuric Acid Environment

  • Jeon, Joong-Kyu;Moon, Han-Young;Jeon, Chan-Ki;Song, Jong-Hwa
    • Journal of the Korea Concrete Institute
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    • v.19 no.3
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    • pp.385-389
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    • 2007
  • In this study, it was investigated the resistance of OPC, 60% GGBS, 20% PFA and 10% SF mortar specimens against sulfuric acid corrosion. As an index for degree of acid corrosion, the corrosion depth was evaluated. Then, it was found that an increase in the duration of immersion and a decrease in the pH, as expected, resulted in a more severe corrosion irrespective of binders; 60% GGBS mortar specimen was the most resistant to sulfuric acid corrosion. From the laboratory testing of sulfuric acid corrosion, an empirical prediction model was suggested as a power function of time and the pH of sulfuric acid, and was applied to an assessment of concrete structures exposed to an acidic environment. It was found that the empirical model gave a more precise prediction of sulfuric acid deterioration of concrete rather than a conventional model, mostly used for predicting carbonation of concrete.