Variance in heavy metal leachability of Pb-, Ni-, and Cr-contaminated soils through red brick sintering procedure.

The technology for remediating heavy metal-contaminated soil is considerably limited because heavy metals do not undergo decomposition. Off-site reuse has emerged as the main technique for treating heavy metal-contaminated soil. Soil is the primary material in red brick making; and in the sintering procedure, heavy metals could solidify and stabilize within bricks. In this study, lead-, nickel-, and chromium-contaminated soils were collected from multiple agricultural fields. The sintering process was performed using a kiln that was for making red bricks. The sintering temperature was approximately 1000 °C. Soil and brick samples, before and after sintering, were analyzed for metal extraction concentration and binding form distribution. After sintering, the concentrations of Pb, Ni, and Cr determined through X-ray fluorescence approximated the concentrations in the soil. However, in the bricks, the bioavailability concentration of Pb, Ni, and Cr is less than 1% of that in the soil; the toxicity characteristic leaching procedure (TCLP) leaching concentration of Pb in the bricks was only 4% of that in the soil, and the leaching concentrations of Ni and Cr were lower than the detectable concentration. For the aqua regia extraction method, in the bricks, the Pb, Ni, and Cr were extracted and the concentrations accounted for 4.6%, 8.8%, and 9.4% of the concentrations in the soil, respectively. After sintering, more than 95% of Ni and Cr in the bricks were in residual fractions. The sintering process has the ability to stabilize the heavy metals in the contaminated soil.

Recombinant Passenger Proteins Can Be Conveniently Purified by One-Step Affinity Chromatography.

Fusion tag is one of the best available tools to date for enhancement of the solubility or improvement of the expression level of recombinant proteins in Escherichia coli. Typically, two consecutive affinity purification steps are often necessitated for the purification of passenger proteins. As a fusion tag, acyl carrier protein (ACP) could greatly increase the soluble expression level of Glucokinase (GlcK), α-Amylase (Amy) and GFP. When fusion protein ACP-G2-GlcK-Histag and ACP-G2-Amy-Histag, in which a protease TEV recognition site was inserted between the fusion tag and passenger protein, were coexpressed with protease TEV respectively in E. coli, the efficient intracellular processing of fusion proteins was achieved. The resulting passenger protein GlcK-Histag and Amy-Histag accumulated predominantly in a soluble form, and could be conveniently purified by one-step Ni-chelating chromatography. However, the fusion protein ACP-GFP-Histag was processed incompletely by the protease TEV coexpressed in vivo, and a large portion of the resulting target protein GFP-Histag aggregated in insoluble form, indicating that the intracellular processing may affect the solubility of cleaved passenger protein. In this context, the soluble fusion protein ACP-GFP-Histag, contained in the supernatant of E. coli cell lysate, was directly subjected to cleavage in vitro by mixing it with the clarified cell lysate of E. coli overexpressing protease TEV. Consequently, the resulting target protein GFP-Histag could accumulate predominantly in a soluble form, and be purified conveniently by one-step Ni-chelating chromatography. The approaches presented here greatly simplify the purification process of passenger proteins, and eliminate the use of large amounts of pure site-specific proteases.