| 1. |
- Marchese, Marco, et al.
(author)
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Techno-economic feasibility of a biomass-to-X plant : Fischer-Tropsch wax synthesis from digestate gasification
- 2021
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In: Energy. - : Elsevier BV. - 0360-5442 .- 1873-6785. ; 228
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Journal article (peer-reviewed)abstract
- A techno-economic analysis is performed, assessing the production costs of Fischer-Tropsch syncrude and waxes of carbon number C20+. The products are obtained from the gasification of digestate from anaerobic digestion inside a dual fluidized bed gasifier (3.11 MWth). The results are compared against the same system fed with lignocellulosic biomass. The syngas is cleaned from impurities and conditioned to reach the desired H-2/CO molar ratio of 1.8 at the inlet of the Fischer-Tropsch reactor. The Fischer-Tropsch products distribution is based on experimental data of a cobalt-based catalyst. Two process configurations are studied: (1) the Fischer-Tropsch off-gas are employed to produce electricity; (2) the off-gas are recirculated to the gasifier for enhanced wax production. Co-production of steam is also investigated. The results show an advantageous production of Fischer-Tropsch compounds utilizing digestate over wood biomass. The highest plant efficiency (i.e., biomass-to-liquid fuel) of 56.3% is reached with digestate feedstock and off-gas recirculation, outputting 61.5 kg(wax)/t(dig). The minimum wax production cost is of 3.04 (sic)/kg(wax), assuming 7.5% discount rate and 25-years plant operation.
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| 2. |
- Rullo, Mariagrazia, et al.
(author)
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Bioisosteric replacement based on 1,2,4-oxadiazoles in the discovery of 1H-indazole-bearing neuroprotective MAO B inhibitors
- 2023
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In: European Journal of Medicinal Chemistry. - : Elsevier. - 0223-5234 .- 1768-3254. ; 255
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Journal article (peer-reviewed)abstract
- Following a hybridization strategy, a series of 5-substituted-1H-indazoles were designed and evaluated in vitro as inhibitors of human monoamine oxidase (hMAO) A and B. Among structural modifications, the bioisostere-based introduction of 1,2,4-oxadiazole ring returned the most potent and selective human MAO B inhibitor (compound 20, IC50 = 52 nM, SI > 192). The most promising inhibitors were studied in cell-based neuroprotection models of SH-SY5Y and astrocytes line against H2O2. Moreover, preliminary drug-like features (aqueous solubility at pH 7.4; hydrolytic stability at acidic and neutral pH) were assessed for selected 1,2,4-oxadiazoles and compared to amide analogues through RP-HPLC methods. Molecular docking simulations highlighted the crucial role of molecular flexibility in providing a better shape complementarity for compound 20 within MAO B enzymatic cleft than rigid analogue 18. Enzymatic kinetics analysis along with thermal stability curves (Tm shift = +2.9 °C) provided clues of a tight-binding mechanism for hMAO B inhibition by 20.
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