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The issue that the residual Cr(VI) in the reduced chromite ore processing residue (rCOPR) is slowly released during deposition has attracted increasing attention. However, the speciation and leaching behaviors of Cr(VI) in rCOPR are still not clear, which is essential for revealing the release mechanism of Cr(VI). In this study, ettringite was determined to be the host phase of Cr(VI) in ferrous sulfate-reduced COPR by scanning electron microscopy (SEM), microfocus X-ray fluorescence spectroscopy (μ-XRF) and aberration-corrected scanning transmission electron microscopy (Cs-STEM). This is because the channel structure of ettringite makes it relatively easy for sulfate to be replaced by chromate with similar structure and thermochemical radius. Furthermore, the investigation on the leaching behavior and mechanism of Cr(VI) in rCOPR eroded by environmental factors showed that carbonates, sulfates and acid can promote the release of Cr(VI). Among them, the erosion effect of HCl on rCOPR is weaker than that of NaCO and NaSO because rCOPR possesses a high buffering reserve of alkalinity. In addition, the erosion of rCOPR by NaCO and NaSO can change Cr(VI) speciation in rCOPR. The results implied that the environmental risk of Cr(VI) release during the deposition of rCOPR should deserve careful assessment.
This article was published in the following journal.
Name: Journal of hazardous materials
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Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.
An enzyme that catalyzes the activation of sulfate ions by ATP to form adenosine-5'-phosphosulfate and pyrophosphate. This reaction constitutes the first enzymatic step in sulfate utilization following the uptake of sulfate. EC 184.108.40.206.
An arylsulfatase that catalyzes the hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. A deficiency of this enzyme is responsible for the inherited lysosomal disease, Maroteaux-Lamy syndrome (MUCOPOLYSACCHARIDOSIS VI). EC 220.127.116.11.
A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC 18.104.22.168.
An enzyme that specifically cleaves the ester sulfate of iduronic acid. Its deficiency has been demonstrated in Hunter's syndrome, which is characterized by an excess of dermatan sulfate and heparan sulfate. EC 22.214.171.124.
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