16 research outputs found

    Coconut Shell Activated Carbon Supported Quaternary Ammonium for Continuous Cycloaddition of CO<sub>2</sub> and Biogas Upgrading in a Packed Bed

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    Quaternary ammonium was successfully prepared on coconut shell activated carbon (CSAC) granules. The samples were characterized by FT-IR, N<sub>2</sub> adsorption–desorption, XPS, TG, and EA. The immobilized quaternary ammonium was thermally stable below 320 °C. The amount of immobilized quaternary ammonium on the CSAC was 0.957 mmol/g. Continuous cycloaddition of CO<sub>2</sub> to epichlorohydrin (ECH) was carried out in a packed-bed reactor without using solvent or cocatalyst. When the reaction conditions were 130 °C and 1.4 MPa, the conversion of ECH and the corresponding turnover frequency (TOF) were 43.5% and 64.6 h<sup>–1</sup>, respectively. The selectivity to epichlorohydrin carbonate (ECHC) reached ∼100%. In biogas upgrading, grafting of quaternary ammonium was demonstrated to enhance CO<sub>2</sub> capture capacity of the CSAC. The saturated CO<sub>2</sub> capture capacities of the CSAC and the quaternary ammonium functionalized CSAC were 1.82 and 2.40 mmol/g at 20 °C and 0.5 MPa, respectively. The adsorption selectivities of CO<sub>2</sub> over CH<sub>4</sub> were ∼67% and 85% for the CSAC and the supported quaternary ammonium, respectively. The adsorption heat was 20–30 kJ/mol for the adsorbents. The supported quaternary ammonium also exhibited a relatively stable cyclability in a packed bed

    Development of Coconut Shell Activated Carbon-Tethered Urease for Degradation of Urea in a Packed Bed

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    Coconut shell activated carbon (AC)-tethered urease (from jack bean) was successfully developed to degrade urea in a packed bed reactor. The loading capacity of urease in AC was 78.8 mg/g. The tethered enzyme showed a maximum activity at 70 °C and pH 7.2. For higher than 75% of the maximum activity, the tethered urease showed a broader temperature range of 42–80 °C compared to 45–75 °C for the free enzyme. Similarly, the tethered urease had an increased stability against the changes of pH. The <i>K</i><sub>m</sub> value of the free urease was 0.271 mol/L and 0.345 mol/L for the tethered one. This may be caused by the conformational changes of the enzyme. The <i>V</i><sub>max</sub> values were 0.215 and 0.110 mol/min for the tethered and free ureases, respectively, which is reflected by an increase in catalytic activity. The catalytic degradation of urea was performed in a packed bed reactor. The remaining activity of the tethered urease was over 80% after 50 h of operation

    Dynamics of <i>kdr</i> allele frequency in response to deltamethrin selection.

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    <p><b>A</b>: wildtype L1014 allele frequency was significantly decreased under deltamethrin selection, but significantly increased in the absence of selection; <b>B</b>: L1014F allele frequency was significantly increased under selection, but significantly decreased when no insecticide selection pressure was available; and <b>C</b>: L1014S allele frequency was decreased regardless of deltamethrin selection.</p
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