A "Heavy Metal Sponge" for Selective Removal and Recovery of Lead and other Toxic Metals from Water Sources
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The development of a "heavy metal sponge" protein for the removal and/or recovery of toxic and precious metal, especially in aqueous environments, was the focus of this experiment. Metal recovery and metal remediation are needed for efficient and safe methods for cleaning up water. Hazardous waste in water is a continuing environmental and business concern. Metal contaminants are continuing environmental and business concern due to their toxicity and potential risk to human health. Metallothionein (MT) is a protein that has an unique ability to selectively bind a number of toxic and precious metals, such as lead and mercury. The SUMO-MT is a fusion protein that degrades a system, yet the histidine-tag gives the protein functionality by expressing the solubility of MT. The breaking of cells from the protein SUMO-MT was needed in order to proceed affinity purification using Ni2+-NTA resin. Metals/metal salts, such as lead, cadmium, and copper sulfate, run into the columns to determine the metal binding to SUMO-MT linked to the Ultralink Iodoacetyl Resin. Gel filtration chromatography was used to rinse sodium arsenate and potassium arsenate solutions with MT to separate the molecules according to their size. ICPMS was used to detect the concentration of specific metals in fragmentations. The purpose of this experiment was to determine if the SUMO-MT protein could bind effectively with metals in aqueous environments. The SUMO-MT protein did not elute at the expected fraction number from both forms of chromatography; therefore, new techniques of removing heavy metal from water are needed to avoid adverse effects on human health.
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