2 research outputs found

    An investigation of heavy metal adsorption by hexa-dentate ligand-modified magnetic nanocomposites

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    <p>Advancement of an efficient and cost-effective method for heavy metal removal from contaminated water utilising Fe<sub>3</sub>O<sub>4</sub>–APTES–EDTA (FAE) nanocomposite, a productive reusable adsorbent, is explained in this study. The novel FAE nanocomposite was prepared and characterised using different techniques such as FTIR, XRD, TEM, EDS, BET, TGA, EDX and Zeta potential techniques. FAE is found to be a good adsorbent for Pb<sup>2</sup><sup>+</sup>, Cd<sup>2</sup><sup>+</sup>, Ni<sup>2</sup><sup>+</sup>, Co<sup>2</sup><sup>+</sup> and Cu<sup>2</sup><sup>+</sup> removal with a higher adsorption capacity. The maximum adsorption capacity of Pb<sup>2</sup><sup>+</sup>, Cd<sup>2</sup><sup>+</sup>, Ni<sup>2</sup><sup>+</sup>, Co<sup>2</sup><sup>+</sup> and Cu<sup>2</sup><sup>+</sup> are found to be 11.31, 13.88, 7.64, 4.86 and 78.67 mg/g, respectively. The adsorption and desorption cycle was studied for five cycles with minimal loss of efficiency.</p

    Impact of imidazolium-based ionic liquids on the structure and stability of lysozyme

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    <p>Various types of water-miscible aprotic ionic liquids (ILs) with different cations (1-ethyl-3-methylimidazolium, 1-butyl-3-methylimidazolium, 1-octyl-3-methylimidazolium) and anions (ethylsulfate and chloride) were used as co-solvents to investigate the stability of lysozyme. Different techniques such as fluorescence, thermal absorption, and circular dichroism (CD) spectroscopy have been used for the study. Fluorescence results reveal that the addition of ILs (1-ethyl-3-methylimidazolium ethyl sulfate and 1-ethyl-3-methylimidazolium) increases the hydrophobicity around the tryptophan environment in lysozyme. CD analysis and temperature-dependent studies were done to investigate the stability of the protein. From the CD analysis, it was observed that the ILs keep the native structure of protein intact. Thermal denaturation studies depicted that the melting temperature of the protein increased in the presence of ILs (1-ethyl-3-methylimidazolium ethyl sulfate and 1-ethyl-3-methylimidazolium), which indicates the stabilization of the protein.</p
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