• Title/Summary/Keyword: monomeric organic additive

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Effects of Additives on Soil Washing Efficiency for Mixed Surfactants (혼합 계면활성제에 적용된 각종 첨가제가 토양세척 효율에 미치는 영향)

  • Choi, Sang-Il;Jang, Min;Hwang, Kyung-Yub;Ryoo, Doo-Hyun
    • Journal of Korea Soil Environment Society
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    • v.3 no.1
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    • pp.65-74
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    • 1998
  • To enhance the washing efficiency of soil polluted by hydrophobic organic compounds, the effects of electrolytes and monomeric organic additives on micelle formation and washing efficiency of mixed surfactant solutions were investigated in this study. The surface tensions and critical micelle concentrations(CMCs) of the single and mixed surfactant solutions[$POE_5$/SDS] supplemented by NaCl were measured to investigate the effects on washing efficiency, and the composition ratios of surfactants and NaCl were optimized for the efficient soil washing system. As the mixing ratio of $POE_5$/SDS was increased to 80%, the mixed surfactant with 0.01M NaCl showed more proportional increase of washing efficiency than the mixed surfactant without any salts. The 3% solution of $POE_5$ and SDS(80%/2o%) with 0.01M NaCl showed the washing efficiency of 90%. However, the washing efficiency was not enhanced by NaCl addition to the single surfactant solution of $POE_5$. The CMC of SDS(0.049%) was higher than that of $POE_5$(0.016%), but the CMCs of mixed surfactants were decreased as the mixing ratio of $POE_5$ was increased. Alcohols having longer chain and branched carbon chain were found to be desirable for the soil washing additives.

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Cloning, High-Level Expression, Purification, and Properties of a Novel Endo-${\beta}$-1,4-Mannanase from Bacillus subtilis G1 in Pichia pastoris

  • Vu, Thi Thu Hang;Quyen, Dinh Thi;Dao, Thi Tuyet;Nguyen, Sy Le Thanh
    • Journal of Microbiology and Biotechnology
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    • v.22 no.3
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    • pp.331-338
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    • 2012
  • A novel gene coding for an endo-${\beta}$-1,4-mannanase (manA) from Bacillus subtilis strain G1 was cloned and overexpressed in P. pastoris GS115, and the enzyme was purified and characterized. The manA gene consisted of an open reading frame of 1,092 nucleotides, encoding a 364-aa protein, with a predicted molecular mass of 41 kDa. The ${\beta}$-mannanase showed an identity of 90.2-92.9% ${\leq}95%$) with the corresponding amino acid sequences from B. subtilis strains deposited in GenBank. The purified ${\beta}$-mannanase was a monomeric protein on SDS-PAGE with a specific activity of 2,718 U/mg and identified by MALDI-TOF mass spectrometry. The recombinant ${\beta}$-mannanase had an optimum temperature of $45^{\circ}C$ and optimum pH of 6.5. The enzyme was stable at temperatures up to $50^{\circ}C$ (for 8 h) and in the pH range of 5-9. EDTA and most tested metal ions showed a slightly to an obviously inhibitory effect on enzyme activity, whereas metal ions ($Hg^{2+}$, $Pb^{2+}$, and $Co^{2+}$) substantially inhibited the recombinant ${\beta}$-mannanase. The chemical additives including detergents (Triton X-100, Tween 20, and SDS) and organic solvents (methanol, ethanol, n-butanol, and acetone) decreased the enzyme activity, and especially no enzyme activity was observed by addition of SDS at the concentrations of 0.25-1.0% (w/v) or n-butanol at the concentrations of 20-30% (v/v). These results suggested that the ${\beta}$-mannanase expressed in P. pastoris could potentially be used as an additive in the feed for monogastric animals.