Search

In this study, recycled acrylonitrile-butadiene-styrene terpolymer (ABSr) was reused to produce polyamide 6 (PA6)-based blends. This was achieved through reactive compatibilization using styrene-acrylonitrile-maleic anhydride (SAN-g-MA) copolymer with a high degree of functionalization (6–10% MA). The PA6/ABSr and PA6/ABSr/SAN-g-MA blends were prepared through melt processing and injection molding and then analyzed for their rheological, mechanical, thermomechanical, thermal, and structural properties, as well as morphology. The torque rheometry revealed a maximum reactivity of the PA6/ABSr (70/30 wt%) blend with low SAN-g-MA (5 phr—parts per hundred resin) content, while above this threshold, torque began to decline, indicating compatibilizer saturation in the interface. These findings were further substantiated by the increase in complex viscosity and the lower melt flow index (MFI) of the PA6/ABSr/SAN-g-MA (5 phr) blend. The 5 phr SAN-g-MA reactive compatibilization of the PA6/ABSr blends significantly enhanced its impact strength, elongation at break, tensile strength, and heat deflection temperature (HDT) by 217%, 631%, 12.6%, and 9.5%, respectively, compared to PA6/ABSr. These findings are promising for the plastic recycling field, paving the way for the production of new tailor-made materials at a reduced price. [ABSTRACT FROM AUTHOR]

Avian pathogenic Escherichia coli (APEC) belonging to extraintestinal pathogenic E. coli (ExPEC) can cause severe infections in extraintestinal tissues in birds and humans, such as the lungs and blood. MprA (microcin production regulation, locus A, herein renamed AbsR, a blood survival regulator), a member of the MarR (multiple antibiotic resistance regulator) transcriptional regulator family, governs the expression of capsule biosynthetic genes in human ExPEC and represents a promising druggable target for antimicrobials. However, a deep understanding of the AbsR regulatory mechanism as well as its regulon is lacking. In this study, we present a systems-level analysis of the APEC AbsR regulon using ChIP-Seq (chromatin immunoprecipitation sequencing) and RNA-Seq (RNA sequencing) methods. We found that AbsR directly regulates 99 genes and indirectly regulates 667 genes. Furthermore, we showed that: 1) AbsR contributes to antiphagocytotic effects by macrophages and virulence in a mouse model for systemic infection by directly activating the capsular gene cluster; 2) AbsR positively impacts biofilm formation via direct regulation of the T2SS (type II secretion system) but plays a marginal role in virulence; and 3) AbsR directly upregulates the acid tolerance signaling system EvgAS to withstand acid stress but is dispensable in ExPEC virulence. Finally, our data indicate that the role of AbsR in virulence gene regulation is relatively conserved in ExPEC strains. Altogether, this study provides a comprehensive analysis of the AbsR regulon and regulatory mechanism, and our data suggest that AbsR likely influences virulence primarily through the control of capsule production. Interestingly, we found that AbsR severely represses the expression of the type I-F CRISPR (clustered regularly interspaced short palindromic repeats)-Cas (CRISPR associated) systems, which could have implications in CRISPR biology and application.

Amorphous ferric hydroxide (AFH) sorbents are commonly used for removal of arsenate from water. When disposed in microbially active, reducing environments, such as landfills, Fe(II) will be generated by reductive dissolution of the AFH surface and arsenate will be desorbed. However, the observed ratio of arsenate (and, in fact, total arsenic) to total iron in the leachate is not consistent with the original ratio of arsenate to iron on the AFH. Work to determine if ferrous iron re-adsorption to the AFH can partially explain this inconsistency is described. As pH increases above 7, Fe(II) increasingly sorbs onto the AFH surface. This sorption is largely independent of ionic strength and somewhat irreversible at high pH. In contrast, arsenate partitioning to AFH decreases with increasing pH. However, over the pH range from 5 to 9, the presence of Fe(II) sorbed to the AFH surface increases the capacity for arsenate sorption. In addition, when no Fe(II) is present, arsenate binding is largely to surface sites inaccessible to Fe(II) binding. The results are also consistent with Fe(II) sorption to AFH sites, otherwise unfavorable to arsenate binding and transformation of those sites into arsenate-amenable binding sites. [ABSTRACT FROM AUTHOR]