RESUMEN
The availability of microbially-safe drinking water is a challenge in many developing regions. Due to the well-known antibacterial effect of silver ions, materials used for their controlled release have been widely studied for point-of-use water disinfection. However, even if it is in principle known that chloride anions can suppress the antibacterial efficiency of silver, the majority of previous studies, surprisingly, have not focused on chloride concentrations relevant for freshwaters and thus for practical applications. Here, we prepared low-cost nanocellulose-aluminium oxyhydroxide nanocomposites functionalized with silver nanoparticles. Field samples obtained from Chennai, India were used as a guideline for choosing relevant chloride concentrations for the antibacterial studies, i.e., 10, 90, and 290 ppm. The antibacterial performance of the material against Escherichia coli and Bacillus subtilis was demonstrated and the influence of chloride concentration on the antibacterial effect was studied with E. coli. A 1 h contact time led to bacterial reductions of 5.6 log10, 2.9 log10, and 2.2 log10, respectively. This indicates that an increase of chloride concentration leads to a substantial reduction of antibacterial efficiency, even within chloride concentrations found in freshwaters. This work enables further insights for designing freshwater purification systems that utilize silver-releasing materials.
RESUMEN
Membrane-bound pyrophosphatases (M-PPases) are enzymes that enhance the survival of plants, protozoans and prokaryotes in energy constraining stress conditions. These proteins use pyrophosphate, a waste product of cellular metabolism, as an energy source for sodium or proton pumping. To study the structure and function of these enzymes we have crystallized two membrane-bound pyrophosphatases recombinantly produced in Saccharomyces cerevisae: the sodium pumping enzyme of Thermotoga maritima (TmPPase) and the proton pumping enzyme of Pyrobaculum aerophilum (PaPPase). Extensive crystal optimization has allowed us to grow crystals of TmPPase that diffract to a resolution of 2.6 Å. The decisive step in this optimization was in-column detergent exchange during the two-step purification procedure. Dodecyl maltoside was used for high temperature solubilization of TmPPase and then exchanged to a series of different detergents. After extensive screening, the new detergent, octyl glucose neopentyl glycol, was found to be the optimal for TmPPase but not PaPPase.