Facile Route for Effective Separation and Full-Scale Recycling of Fly Ash and Unburned Carbon.

The synchronous production of high-quality unburned carbon concentrate and cleaned ash from high LOI (loss on ignition) fly ash without yielding secondary solid waste is a dilemma issue. In this study, a viable flotation process with one rougher and two cleaners is developed for simultaneously obtaining carbon concentrate with a yield of 18.00% and an ash content of 17.49% and cleaned ash with a yield of 82.00% and a LOI of 4.63% from fly ash, reaching 84.72% of combustible substance recovery and 80.66% of flotation perfection index. The characteristic analyses of the stage by stage releasing products using laser particle size analysis, XRF, XRD, and SEM-EDS demonstrate that the inevitable factors that lead to a remaining higher ash content in the one-step flotation carbon concentrate are the random entrainment of mineral particles in the size range of 0-20 µm, especially the quasi-colloidal parts within 0-12.5 µm and the weak selective collection of fine-grained conjoined granules in the size range of 0-40 µm. Consequently, at least two cleaning steps are required for the effective separation of unburned carbon and ash. Furthermore, batch flotation test results show that diesel is superior to kerosene in the collection of unburned carbon, with an optimum dosage of 800 g/t; no. 2 oil acts more positively than MIBC for the separation of unburned carbon and ash, with an optimal dosing amount of 600 g/t; the optimum pulp concentration and flotation time are as follows: 100 g/L and 3.5 min for the rougher, 45 g/L and 2 min for the first cleaning, and 30 g/L and 3 min for the second cleaning. This study provides an economically feasible technological solution for the full-scale recovery of high-LOI fly ash in one step and avoids the problem of secondary solid waste that would have been generated in previous studies.

An investigation of alkaline phosphatase enzymatic activity after electrospinning and electrospraying.

The high target specificity and multifunctionality of proteins has led to great interest in their clinical use. To this end, the development of delivery systems capable of preserving their bioactivity and improving bioavailability is pivotal to achieve high effectiveness and satisfactory therapeutic outcomes. Electrohydrodynamic (EHD) techniques, namely electrospinning and electrospraying, have been widely explored for protein encapsulation and delivery. In this work, monoaxial and coaxial electrospinning and electrospraying were used to encapsulate alkaline phosphatase (ALP) into poly(ethylene oxide) fibres and particles, respectively, and the effects of the processing techniques on the integrity and bioactivity of the enzyme were assessed. A full morphological and physicochemical characterisation of the blend and core-shell products was performed. ALP was successfully encapsulated within monolithic and core-shell electrospun fibres and electrosprayed particles, with drug loadings and encapsulation efficiencies of up to 21% and 99%, respectively. Monoaxial and coaxial electrospinning were equally effective in preserving ALP function, leading to no activity loss compared to fresh aqueous solutions of the enzyme. While the same result was observed for monoaxial electrospraying, coaxial electrospraying of ALP caused a 40% reduction in its bioactivity, which was attributed to the high voltage (22.5 kV) used during processing. This demonstrates that choosing between blend and coaxial EHD processing for protein encapsulation is not always straightforward, being highly dependent on the chosen therapeutic agent and the effects of the processing conditions on its bioactivity.

Biogenesis, transport and remodeling of lysophospholipids in Gram-negative bacteria.

Lysophospholipids (LPLs) are metabolic intermediates in bacterial phospholipid turnover. Distinct from their diacyl counterparts, these inverted cone-shaped molecules share physical characteristics of detergents, enabling modification of local membrane properties such as curvature. The functions of LPLs as cellular growth factors or potent lipid mediators have been extensively demonstrated in eukaryotic cells but are still undefined in bacteria. In the envelope of Gram-negative bacteria, LPLs are derived from multiple endogenous and exogenous sources. Although several flippases that move non-glycerophospholipids across the bacterial inner membrane were characterized, lysophospholipid transporter LplT appears to be the first example of a bacterial protein capable of facilitating rapid retrograde translocation of lyso forms of glycerophospholipids across the cytoplasmic membrane in Gram-negative bacteria. LplT transports lyso forms of the three bacterial membrane phospholipids with comparable efficiency, but excludes other lysolipid species. Once a LPL is flipped by LplT to the cytoplasmic side of the inner membrane, its diacyl form is effectively regenerated by the action of a peripheral enzyme, acyl-ACP synthetase/LPL acyltransferase (Aas). LplT-Aas also mediates a novel cardiolipin remodeling by converting its two lyso derivatives, diacyl or deacylated cardiolipin, to a triacyl form. This coupled remodeling system provides a unique bacterial membrane phospholipid repair mechanism. Strict selectivity of LplT for lyso lipids allows this system to fulfill efficient lipid repair in an environment containing mostly diacyl phospholipids. A rocker-switch model engaged by a pair of symmetric ion-locks may facilitate alternating substrate access to drive LPL flipping into bacterial cells. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.