LED irradiated photo-Fenton for the removal of estrogenic activity and endocrine disruptors from wastewater treatment plant effluent.

The goal of this work was to evaluate the performance of the LED irradiated photo-Fenton process on the removal of (i) estrogenic activity and (ii) seven endocrine disruptors (EDs) (4-octylphenol, 4-nonylphenol, bisphenol A, estrone, 17ß-estradiol, 17α-ethinylestradiol, and estriol) from real wastewater treatment plant effluent (WWTPE). EDs are a group of contaminants of emerging concern present in WWTPE and which may be recognized by hormone receptors, thus harming animal and human health. The yeast estrogenic screen test (YES) was used to quantify estrogenic activity promoted by EDs in WWTPE samples before and after photo-Fenton treatment. Tests were performed following a factorial design with different iron (20, 40, and 60 mg L-1) and hydrogen peroxide (100, 200, and 300 mg L-1) concentrations in a laboratory scale LED photoreactor (λ = 455 nm, 1.5 L, 1.6 × 10-6 Einstein s-1). EDs were analyzed by gas chromatography coupled to a mass spectrometer. Control experiments consisted of Fenton process, iron only, LED irradiation only, and H2O2 only. Optimum experimental conditions for LED photo-Fenton resulted in 62% removal of estrogenic activity and 59% mineralization. In addition, treated WWTPE was not toxic to Aliivibrio fischeri and more than 80% of EDs were removed during LED irradiated photo-Fenton. Although Fenton process showed similar efficiency to that obtained by LED photo-Fenton, a higher volume of sludge was generated in the dark. Finally, results obtained in this study confirm the applicability of LED irradiated photo-Fenton process for improving the quality of WWTPE as an alternative to solar photo-Fenton in case solar radiation is not available, thus reducing hazards associated to WWTPE reuse or discharge.

Molecular characterization of SUMO E2 conjugation enzyme: differential expression profile in Schistosoma mansoni.

SUMO-dependent post-translational modification is implicated in a variety of cellular functions including gene expression regulation, nuclear sub-localization, and signal transduction. Conjugation of SUMO to other proteins occurs in a similar process to ubiquitination, which involves three classes of enzymes: an E1 activating, an E2 conjugating, and an E3 target-specific ligase. Ubc9 is the unique SUMO E2 enzyme known to conjugate SUMO to target substrates. Here, we present the molecular characterization of this enzyme and demonstrate its expression profile during the S. mansoni life cycle. We have used bioinformatic approaches to identify the SUMO-conjugating enzyme, the SmUbc9-like protein, in the Schistosoma mansoni databases. Quantitative RT-PCR was employed to measure the transcript levels of SUMO E2 in cercariae, adult worms, and in vitro cultivated schistosomula. Furthermore, recombinant SmUbc9 was expressed using the Gateway system, and antibodies raised in rats were used to measure SmUbc9 protein levels in S. mansoni stages by Western blotting. Our data revealed upregulation of the SmUbc9 transcript in early schistosomula followed by a marked differential gene expression in the other analyzed stages. The protein levels were maintained fairly constant suggesting a post-transcriptional regulation of the SmUbc9 mRNA. Our results show for the first time that S. mansoni employs a functional SUMO E2 enzyme, for the conjugation of the SUMO proteins to its target substrates.