We carbonized simulated food waste (stage I) and then liquefied the biochar produced (stage II) with the goals of producing bio-oil and recovering nitrogen. Both stages used hydrothermal and pyrolytic approaches, so the influence of water during the treatments could be discerned. Pyrolysis produced biochars in the greatest yield (57 wt %) from the biomass feedstock, and it produced biocrudes with the greatest HHV (39.4 MJ/kg) via the liquefaction of biochar from hydrothermal carbonization. Pyrolysis of biochar for stage II gave negligible aqueous-phase product yields, however, which limited the nitrogen recovery with this approach solely to that recovered in the initial carbonization step. The highest N recovery (75%) in the aqueous-phase products occurred with hydrothermal treatment for both carbonization and liquefaction. This N recovery greatly exceeded those (<10%) for single-step hydrothermal liquefaction of this same feedstock. Energy recovery in the biocrude oil produced from this two-step process exceeded 50% in several runs. This two-step approach for food-waste valorization provides an opportunity for comparable energy recovery and much greater N recovery than are available from single-step hydrothermal liquefaction.
Although rarely used in nature, fluorine has emerged as an important elemental ingredient in the design of proteins with altered folding, stability, oligomerization propensities, and bioactivity. Adding to the molecular modification toolbox, here we report the ability of privileged perfluorinated amphiphiles to noncovalently decorate proteins to alter their conformational plasticity and potentiate their dispersion into fluorous phases. Employing a complementary suite of biophysical, in‐silico and in‐vitro approaches, we establish structure‐activity relationships defining these phenomena and investigate their impact on protein structural dynamics and intracellular trafficking. Notably, we show that the lead compound, perfluorononanoic acid, is 106 times more potent in inducing non‐native protein secondary structure in select proteins than is the well‐known helix inducer trifluoroethanol, and also significantly enhances the cellular uptake of complexed proteins. These findings could advance the rational design of fluorinated proteins, inform on potential modes of toxicity for perfluoroalkyl substances, and guide the development of fluorine‐modified biologics with desirable functional properties for drug discovery and delivery applications.
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