Reduced formation of brominated trihalomethanes during chlorination of bromide-containing waters in the presence of Mn(II).

Manganese(II) (Mn(II)) and bromide (Br-) are common in natural waters. This study investigated the effect of in-situ Mn(II) oxidation and preformed MnOx on the brominated trihalomethane (Br-THM) formation during chlorination of bromide-containing waters. The results showed Br-THM formation could be substantially inhibited by in-situ Mn(II) oxidation, but the addition of preformed MnOx had limited influence on Br-THM formation during chlorination of bromide-containing waters. Analysis of bromine species showed that about 30 % bromine species were incorporated into the MnOx particles and formed MnOx-Br during the in-situ Mn(II) oxidation process. Consequently, the availability of reactive bromine species for the reaction with dissolved organic matter (DOM) reduced, leading to less Br-THM formation. X-ray diffraction (XRD) analysis of in-situ Mn(II) oxidation product indicated the presence of Br- decreased the crystallinity of Mn oxides, verifying the bromine species entered MnOx crystal. However, the adsorptive uptake of bromine species by preformed MnOx was negligible and had no impact on Br-THM formation. Inhibition rate of Mn(II) oxidation on THM formation decreased with increasing specific ultraviolet absorbance (SUVA254) value of filtered water, showing SUVA254 could be a good indicator of DOM competition ability for oxidant with Mn(II). In addition, Excitation/Emission Matrix indicated that Mn(II) could form complexes with humic substances, which might also retard the reaction between humic substances and oxidant to form Br-THMs. This study highlighted the inhibiting effect of in-situ Mn(II) oxidation on Br-THM formation during chlorination of bromide-containing waters.

Enhanced disinfection byproducts formation by fine iron particles intercepted in household point-of-use facilities.

To cope with the demand for good-quality potable water, household point-of-use (POU) facilities such as polypropylene cotton filters (PCFs) are widely used. However, the behaviors of new and used PCFs under discoloration are unclear. In this study, we found that new PCF did not effectively intercept particles under discoloration within the initial 5 d of inflow. In addition, the particles, especially the fine ones, accumulated in the long-used PCF exacerbated the risks of disinfection byproducts (DBPs) and microbes. The concentrations of trihalomethanes (THMs) and haloacetonitriles (HANs) in the effluent run through the PCF all increased over time; interestingly, all sharply increased after 5 d in accordance with the decrease in effluent iron particles. During this stage, maximum increases rate of 117.89% in THMs and 75.12% in HANs were observed. For haloacetic acids (HAAs), it served as the dominant contaminants, with concentrations approximately 10-fold greater than those of THMs and HANs. The increase showed that used PCFs could exacerbate the risks in DBPs exposure. Adenosine triphosphate (ATP) also showed a similar trend, with a maximum increase from 0.0033 to 0.0055 nmol/mL. Thus, PCFs can act only as pretreatment units and should be replaced after yellow water events. This study offers important guidance for PCF usage in drinking water purification, especially under discoloration.

In vivo and in vitro characterization of TEV protease mutants.

Tobacco etch virus protease (TEVp) is frequently applied in the cleavage of fusion protein. However, production of TEV protease in Escherichia coli is hampered by low yield and poor solubility, and auto-cleavage of wild type TEVp gives rise to the loss-of-function. Previously it was reported that TEVp S219V displayed more stability, and TEVp variant containing T17S/N68D/I77V and double mutant L56V/S135G resulted in the enhanced production and solubility, respectively. Here, we introduced T17S/N68D/I77V in TEVp S219V to generate TEVpM1 and combined five amino acid mutations (T17S/L56V/N68D/I77V/S135G) in TEVp S219V to create TEVpM2. Among TEVp S219V, and two constructed variants, TEVpM2 displayed highest solubility and catalytic activity in vivo, using EmGFP as the solubility reporter, and the designed fusion protein as in vivo substrate containing an N-terminal hexahistidine tagged GST, a peptide sequence for thrombin and TEV cut and E. coli diaminopropionate ammonia-lyase. The purified TEVp mutants fused with double hexahistidine-tag at N and C terminus showed highest yield, solubility and cleavage efficiency. Mutations of five amino acid residues in TEVpM2 slightly altered protein secondary structure conformed by circular dichroism assay.