Poultry Feather Waste as Bio-Based Cross-Linking Additive for Ethylene Propylene Diene Rubber.

Most rubbers used today rely on sulphur as a cross-linking agent and carbon black from fossil resources to modify the mechanical properties. A very promising substitute can be found in natural keratins such as feathers. These are not only tough, but also contain a relevant amount of sulphur in the form of disulphide bridges. The present study shows that these can be activated under vulcanisation conditions and then bind covalently to EPDM rubber to form a cross-linked network. Feathers were cut into lengths of 0.08, 0.2, and 1 mm and incorporated at 38, 69, or 100 phr into EPDM mixtures containing either no carbon black or no carbon black nor sulphur. The presence of feather cuttings increases the tensile and compressive strength as well as the hardness, and reduces the rebound resilience. Due to their high (approximately 17%) nitrogen content, the feathers also improve the thermal stability of the composite, as the main degradation step is shifted from 400 °C to 470 °C and the decomposition is significantly slowed down. Since elastomers are a large market and feathers in particular are a high-volume waste, the combination of these two offers enormous ecological and economic prospects.

Autogenous Cross-Linking of Recycled Keratin from Poultry-Feather Waste to Hydrogels for Plant-Growth Media.

The global rise in atmospheric temperature is leading to an increasing spread of semi-arid and arid regions and is accompanied by a deterioration of arable land. Polymers can help in a number of ways, but they must not be a burden to the environment. In this context, we present herein a method by which goose feathers, representative of keratin waste in general, can be transformed into hydrogels for use as a plant growth medium. The treatment of shredded feathers in Na2S solution at ambient conditions dissolves approx. 80% of the keratin within 30 min. During evaporation, the thiol groups of cysteine reoxidise to disulphide bridges. Additionally, the protein chains form ß-sheets. Both act as cross-links that enables the formation of gels. The drying conditions were found to be crucial as slower evaporation affords gels with higher degrees of swelling at the cost of reduced gel yields. The cress germination test indicated the absence of toxic substances in the gel, which strongly adheres to the roots. Thereby, the plants are protected from drought stress as long as the gel still contains moisture.

Protein Hydrolysates from Biogenic Waste as an Ecological Flame Retarder and Binder for Fiberboards.

The increasing demand for sustainable building materials requires alternative flame retarders, which have superior sustainability to those previously used. In this respect, we present our initial results with protein hydrolysates made from poultry-feather waste for the preparation of flame-retardant fiberboards. Impregnated wood fibers show a significantly decreased decomposition rate in the region between 300 and 450 °C, as measured by thermogravimetric analysis. Final combustion of the impregnated fibers is shifted up by 50 °C to the interval 450-500 °C and occurs stepwise rather than instantaneously as for untreated wood. At a total protein content of approx. 10 wt %, plates produced in the "wet" process are self-extinguishing and show very little subsequent smouldering. In three-point bending tests, these fiberboard prototypes were able to withstand stresses of up to 15 N/mm2, the threshold required by DIN EN 622 for commercial, formaldehyde-bound MBH fiberboards. This indicates that the upcycled protein hydrolysates not only have an impressive flame-retarding effect but also can be used as a fully sustainable binder for a new generation of ecological fiberboards. As these boards are based solely on natural materials, they can be shredded and composted at the end of their life cycle.

Synthesis of oxime-based CO-releasing molecules, CORMs and their immobilization on maghemite nanoparticles for magnetic-field induced CO release.

Oxime-based CO-releasing molecules (oximeCORMs) were immobilized with a catechol-modified backbone on maghemite iron oxide nanoparticles (IONPs) to give oximeCORM@IONP. The CO release from the free and immobilized oximeCORMs was measured using the standard myoglobin assay. The oximeCORM-nanoparticles were coated with dextran for improved water solubility and confined into an alginate shell for protection and separation from the surrounding myoglobin assay to allow for CO release studies by UV/Vis absorption without interference from highly-absorptive oximeCORM@IONP. Half-lifes of the oxime-based polymer-confined alginate@dextran@oximeCORM@IONPs were estimated at 20 °C to 814 ± 23 min, at 37 °C to 346 ± 83 min and at 50 °C to 73 ± 1 min. The alginate@dextran@oximeCORM@IONP composite showed a further decrease of the half-life of CO release to 153 ± 27 min at 37 °C through local magnetic heating of the susceptible iron oxide nanoparticles with application of an external alternating magnetic field (31.7 kA m(-1), 247 kHz, 39.9 mTesla). The activation energy for the CO release from molecular dicarbonylchlorido(imidazole-2-carbaldehydeoxime)(alkoxycarbonyl)ruthenium(ii) complexes is determined to be ∼100 kJ mol(-1) for five different imidazole-oxime derivatives.

Up-regulation of striatal adenosine A(2A) receptors in schizophrenia.

Adenosine A (2A) receptors have been implicated in the pathophysiology of schizophrenia by clinical, anatomical, biochemical and genetic studies. We hypothesized that a genetically determined low number of adenosine A (2A) receptors could be a vulnerability factor for the development of the disease. The density of adenosine A (2A) receptors was investigated in human postmortem striatum of patients with schizophrenia (n = 9) and matched controls ( n= 9) using [ H)CGS 21680 as a radioligand probe. The maximum number of binding sites (B) (max) was 70% higher in patients with schizophrenia than in matched controls (609.4 +/- 259.1 354.0 +/- 156.4 fmol/mg protein, p=0.04). No significant difference could be discerned for the affinity of caffeine for adenosine A receptors between patients and controls. The increase in receptor density correlated with the dose of antipsychotic medication in chlorpromazine equivalents (r =0.61, = 0.014). We failed to provide evidence for a genetically determined reduction of adenosine A 2(A) receptors in schizophrenia. Instead, consistent with findings from animal experiments, our observation supports a role of adenosine A (2A) receptors in the molecular effects of antipsychotic drugs.