Pyrolysis of Dried Wastewater Biosolids Can Be Energy Positive

Pyrolysis is a thermal process that converts biosolids into biochar (a soil amendment), py-oil and py-gas, which can be energy sources. The objectives of this research were to determine the product yield of dried biosolids during pyrolysis and the energy requirements of pyrolysis. Bench-scale experiments revealed that temperature increases up to 500 °C substantially decreased the fraction of biochar and increased the fraction of py-oil. Py-gas yield increased above 500 °C. The energy required for pyrolysis was approximately 5-fold less than the energy required to dry biosolids (depending on biosolids moisture content), indicating that, if a utility already uses energy to dry biosolids, then pyrolysis does not require a substantial amount of energy. However, if a utility produces wet biosolids, then implementing pyrolysis may be costly because of the energy required to dry the biosolids. The energy content of py-gas and py-oil was always greater than the energy required for pyrolysis

In Vivo Evolution of Butane Oxidation by Terminal Alkane Hydroxylases AlkB and CYP153A6

Enzymes of the AlkB and CYP153 families catalyze the first step in the catabolism of medium-chain-length alkanes, selective oxidation of the alkane to the 1-alkanol, and enable their host organisms to utilize alkanes as carbon sources. Small, gaseous alkanes, however, are converted to alkanols by evolutionarily unrelated methane monooxygenases. Propane and butane can be oxidized by CYP enzymes engineered in the laboratory, but these produce predominantly the 2-alkanols. Here we report the in vivo-directed evolution of two medium-chain-length terminal alkane hydroxylases, the integral membrane di-iron enzyme AlkB from Pseudomonas putida GPo1 and the class II-type soluble CYP153A6 from Mycobacterium sp. strain HXN-1500, to enhance their activity on small alkanes. We established a P. putida evolution system that enables selection for terminal alkane hydroxylase activity and used it to select propane- and butane-oxidizing enzymes based on enhanced growth complementation of an adapted P. putida GPo12(pGEc47{Delta}B) strain. The resulting enzymes exhibited higher rates of 1-butanol production from butane and maintained their preference for terminal hydroxylation. This in vivo evolution system could be useful for directed evolution of enzymes that function efficiently to hydroxylate small alkanes in engineered hosts

The dual transcriptional regulator CysR in Corynebacterium glutamicum ATCC 13032 controls a subset of genes of the McbR regulon in response to the availability of sulphide acceptor molecules

Background: Regulation of sulphur metabolism in Corynebacterium glutamicum ATCC 13032 has been studied intensively in the last few years, due to its industrial as well as scientific importance. Previously, the gene cg0156 was shown to belong to the regulon of McbR, a global transcriptional repressor of sulphur metabolism in C. glutamicum. This gene encodes a putative ROK-type regulator, a paralogue of the activator of sulphonate utilisation, SsuR. Therefore, it is an interesting candidate for study to further the understanding of the regulation of sulphur metabolism in C. glutamicum. Results: Deletion of cg0156, now designated cysR, results in the inability of the mutant to utilise sulphate and aliphatic sulphonates. DNA microarray hybridisations revealed 49 genes with significantly increased and 48 with decreased transcript levels in presence of the native CysR compared to a cysR deletion mutant. Among the genes positively controlled by CysR were the gene cluster involved in sulphate reduction, fpr2 cysIXHDNYZ, and ssuR. Gel retardation experiments demonstrated that binding of CysR to DNA depends in vitro on the presence of either O-acetyl-L-serine or O-acetyl-L-homoserine. Mapping of the transcription start points of five transcription units helped to identify a 10 bp inverted repeat as the possible CysR binding site. Subsequent in vivo tests proved this motif to be necessary for CysR-dependent transcriptional regulation. Conclusion: CysR acts as the functional analogue of the unrelated LysR-type regulator CysB from Escherichia coli, controlling sulphide production in response to acceptor availability. In both bacteria, gene duplication events seem to have taken place which resulted in the evolution of dedicated regulators for the control of sulphonate utilisation. The striking convergent evolution of network topology indicates the strong selective pressure to control the metabolism of the essential but often toxic sulphur-containing (bio-)molecules

Living in Peace: Host-Microbiota Mutualism in the Skin

Commensal microbes colonize the skin where they promote immune development and prevent infection without inducing damaging inflammatory responses. In this issue of Cell Host & Microbe, Scharschmidt et al. (2017) show that during hair follicle development, commensals induce regulatory T cell migration to the skin to ensure cutaneous homeostasis

The 3D abstract Tile Assembly Model is Intrinsically Universal

In this paper, we prove that the three-dimensional abstract Tile Assembly Model (3DaTAM) is intrinsically universal. This means that there is a universal tile set in the 3DaTAM which can be used to simulate any 3DaTAM system. This result adds to a body of work on the intrinsic universality of models of self-assembly, and is specifically motivated by a result in FOCS 2016 showing that any intrinsically universal tile set for the 2DaTAM requires nondeterminism (i.e. undirectedness) even when simulating directed systems. To prove our result we have not only designed, but also fully implemented what we believe to be the first intrinsically universal tile set which has been implemented and simulated in any tile assembly model, and have made it and a simulator which can display it freely available

Towards Functional Flows for Hierarchical Models

The recursion relations of hierarchical models are studied and contrasted with functional renormalisation group equations in corresponding approximations. The formalisms are compared quantitatively for the Ising universality class, where the spectrum of universal eigenvalues at criticality is studied. A significant correlation amongst scaling exponents is pointed out and analysed in view of an underlying optimisation. Functional flows are provided which match with high accuracy all known scaling exponents from Dyson's hierarchical model for discrete block-spin transformations. Implications of the results are discussed.Comment: 17 pages, 4 figures; wording sharpened, typos removed, reference added; to appear with PR

Estrogen-Like Activity of Perfluoroalkyl Acids In Vivo and Interaction with Human and Rainbow Trout Estrogen Receptors In Vitro

The objectives of this study were to determine the structural characteristics of perfluoroalkyl acids (PFAAs) that confer estrogen-like activity in vivo using juvenile rainbow trout (Oncorhynchus mykiss) as an animal model and to determine whether these chemicals interact directly with the estrogen receptor (ER) using in vitro and in silico species comparison approaches. Perfluorooctanoic (PFOA), perfluorononanoic (PFNA), perfluorodecanoic (PFDA), and perfluoroundecanoic (PFUnDA) acids were all potent inducers of the estrogen-responsive biomarker protein vitellogenin (Vtg) in vivo, although at fairly high dietary exposures. A structure-activity relationship for PFAAs was observed, where eight to ten fluorinated carbons and a carboxylic acid end group were optimal for maximal Vtg induction. These in vivo findings were corroborated by in vitro mechanistic assays for trout and human ER. All PFAAs tested weakly bound to trout liver ER with half maximal inhibitory concentration (IC50) values of 15.2-289μM. Additionally, PFOA, PFNA, PFDA, PFUnDA, and perlfuorooctane sulfonate (PFOS) significantly enhanced human ERα-dependent transcriptional activation at concentrations ranging from 10-1000nM. Finally, we employed an in silico computational model based upon the crystal structure for the human ERα ligand-binding domain complexed with E2 to structurally investigate binding of these putative ligands to human, mouse, and trout ERα. PFOA, PFNA, PFDA, and PFOS all efficiently docked with ERα from different species and formed a hydrogen bond at residue Arg394/398/407 (human/mouse/trout) in a manner similar to the environmental estrogens bisphenol A and nonylphenol. Overall, these data support the contention that several PFAAs are weak environmental xenoestrogens of potential concer