Composite fibres that contain cellulose and lignin were produced from ionic liquid solutions by dry-jet wet spinning. Eucalyptus dissolving pulp and organosolv/kraft lignin blends in different ratios were dissolved in the ionic liquid 1,5-diazabicyclo[4.3.0]non-5-enium acetate to prepare a spinning dope from which composite fibres were spun successfully. The composite fibres had a high strength with slightly decreasing values for fibres with an increasing share of lignin, which is because of the reduction in crystallinity. The total orientation of composite fibres and SEM images show morphological changes caused by the presence of lignin. The hydrophobic contribution of lignin reduced the vapour adsorption in the fibre. Thermogravimetric analysis curves of the composite fibres reveal the positive effect of the lignin on the carbonisation yield. Finally, the composite fibre was found to be a potential raw material for textile manufacturing and as a precursor for carbon fibre production.

The self-assembled structure of toll-like receptor agonist lipopeptides containing the CSK4 peptide sequence is examined in aqueous solution. A remarkable dependence of morphology on the number of attached hexadecyl lipid chains is demonstrated, with spherical micelle structures for mono- and di-lipidated structures observed, but flexible wormlike micelles for the homologue containing three lipid chains. The distinct modes of assembly may have an important influence on the bioactivity of this class of lipopeptide.

In the European Union (EU), the major N and P sources in agriculture are synthetic fertilizers although inputs from animal manure remain important, especially in regions of high livestock density. The use of synthetic fertilizers has dramatically increased food production worldwide, but the unintended costs to the environment and human health due to surplus and inefficient application have also been substantial. Thus, alternatives are needed. One of those represents the valorization of organic waste, the amount of which increased exponentially during the last decades. Its estimated annual increase is around 25 million tons [1].A major source of organic waste is sewage sludge (SS). Containing high amounts of N, with a median of 3.3% [2], P and OM, this material offers an excellent feedstock for the production of soil amendments that can reduce the need of synthetic P and N fertilizer [3,4]. At the same time it may increase the C-sequestration potential of cropped soils. In addition, sludge recycling as fertilizer or organic amendment helps to reduce the amount of organic waste by returning it into the bio-cycle while at the same time soil physical and chemical properties are restored [5,6]. Indeed, the Sewage Sludge Directive [7] and the working document on sludge [8] describe the use of SS on soils as beneficial but also seek to encourage a safe use of this material in agriculture and to regulate its application to prevent harmful effects on soil, vegetation, animals and humans [9]. Thus, in order to enable the use of SS as soil application, it first has to be decontaminated by removing organic pollutants and pathogen bacteria. Different treatments can be used for the latter: thermal drying, anaerobic digestion, conditioning with lime, etc. In general, the process of removing pathogen bacteria of SS is called hygienization. Heavy metals content also need to be taken into account. In cases their concentrations are above the allowed thresholds, strategies have to be developed to avoid secondary contamination due to SS application.Hydrothermal carbonization and pyrolysis of sewage sludges: wWhat happen to carbon and nitrogen? M. Paneque a, ⁎

No abstract

Lipidation is a powerful strategy to improve the stability in vivo of peptide drugs. Attachment of a lipid chain to a hydrophilic peptide leads to amphiphilicity and the potential for surfactant-like self-assembly. Here, the self-assembly and conformation of three lipidated derivatives of the gastrointestinal peptide hormone PYY is examined using a comprehensive range of spectroscopic, scattering, and electron microscopy methods and compared to those of the parent PYY peptide. The peptides are lipidated at Ser(11), Arg(17), or Arg(23) in the peptide; the former is within the β-turn domain (based on the published solution NMR structure), and the latter two are both within the α-helical domain. We show that it is possible to access a remarkable diversity of nanostructures ranging from micelles to nanotapes and fibrillar hydrogels by control of assembly conditions (concentration, pH, and temperature). All of the lipopeptides self-assemble above a critical aggregation concentration (cac), determined through pyrene fluorescence probe measurements, and they all have predominantly α-helical secondary structure at their native pH. The pH and temperature dependence of the α-helical conformation were probed via circular dichroism spectroscopy experiments. Lipidation was found to provide enhanced stability against changes in temperature and pH. The self-assembled structures were investigated using small-angle X-ray scattering (SAXS) and cryogenic transmission electron microscopy (cryo-TEM). Distinct differences in nanostructure were observed for lipidated and unlipidated peptides, also depending on the position of lipidation. Remarkably, micelles containing lipopeptides with α-helical peptide conformation were observed. Gelation was observed at higher concentrations in certain pH intervals for the lipidated peptides, but not for unlipidated PYY. Thus, lipidation, in addition to enhancing stability against pH and temperature variation, also provides a route to prepare PYY peptide hydrogels. These findings provide important insights into the control of PYY conformation and aggregation by lipidation, relevant to the development of future therapeutics based on this peptide hormone, for example, in treatments for obesity.