302 research outputs found

    At Berkeley, we recycle everything but CO 2

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    Designing Materials and Processes for CO2 Capture with Solid Sorbents

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    Cyclic adsorption and regeneration of solid sorbents to remove CO2 from gas streams can be accomplished with a variety of different adsorbents and processes. Determining which adsorbents and which processes will be best suited for a given application requires simulations or experimental measurements of many different materials in many different processes. However, general principles can guide the development of carbon capture systems, based primarily on the performance and limitations of different adsorbents, types of gas-solid contactors used, heat exchange method, and managing pressure changes. The main types of adsorption processes are temperature swing, pressure swing, or a combined temperature and pressure swing. Temperature swing adsorption processes involve regenerating a sorbent saturated with CO2 through heating. In these processes heat transfer is generally the rate-limiting step and heating and cooling the sorbent is also the most energy intensive component of the process. To minimize the energy consumption of the process, the sorbent should have a moderate heat of adsorption to allow a large change in CO2 capacity through changing the temperature, the heat capacity of the heated and cooled material should be minimized, and heat transfer should be maximized. For pressure swing adsorption processes, on the other hand, the driving force for regenerating CO2 is provided by changing the partial pressure of CO2 between the adsorption and regeneration steps. Changing the pressure is the main component of the energy consumption and cycle time, and these are minimized by allowing complex process configurations with multiple pressure differentials and using an adsorbent with high capacity but low heat of adsorption. Combined temperature and pressure swing adsorption can be optimized through a combination of the factors above. Each of these cases yields a different optimal material, contacting strategy, and process configuration, but all can be approached using a common design methodology. This paper will present a design methodology for solid sorbent CCS systems. This will include design considerations for how to maximize the performance of a range of traditionally deployed and newly-discovered solid sorbents. Similarly, standard and novel process configurations will be discussed with descriptions of the possible benefits or drawbacks and the types of sorbent material that are best suited for each configuration. By comparing the performance of mature adsorbents and processes and the expected performance of adsorbents and processes currently under development, the state of the art and potential advances for CCS with solid adsorbents will be presented

    Clostridium perfringensepsilon toxin H149A mutant as a platform for receptor binding studies

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    Clostridium perfringens epsilon toxin (Etx) is a pore-forming toxin responsible for a severe and rapidly fatal enterotoxemia of ruminants. The toxin is classified as a category B bioterrorism agent by the U.S. Government Centres for Disease Control and Prevention (CDC), making work with recombinant toxin difficult. To reduce the hazard posed by work with recombinant Etx, we have used a variant of Etx that contains a H149A mutation (Etx-H149A), previously reported to have reduced, but not abolished, toxicity. The three-dimensional structure of H149A prototoxin shows that the H149A mutation in domain III does not affect organisation of the putative receptor binding loops in domain I of the toxin. Surface exposed tyrosine residues in domain I of Etx-H149A (Y16, Y20, Y29, Y30, Y36 and Y196) were mutated to alanine and mutants Y30A and Y196A showed significantly reduced binding to MDCK.2 cells relative to Etx-H149A that correlated with their reduced cytotoxic activity. Thus, our study confirms the role of surface exposed tyrosine residues in domain I of Etx in binding to MDCK cells and the suitability of Etx-H149A for further receptor binding studies. In contrast, binding of all of the tyrosine mutants to ACHN cells was similar to that of Etx-H149A, suggesting that Etx can recognise different cell surface receptors. In support of this, the crystal structure of Etx-H149A identified a glycan (β-octyl-glucoside) binding site in domain III of Etx-H149A, which may be a second receptor binding site. These findings have important implications for developing strategies designed to neutralise toxin activity

    Techno-Economic Analysis of a Secondary Air Stripper Process

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    We present results of an initial techno-economic assessment on a post-combustion CO2 capture process developed by the Center for Applied Energy Research (CAER) at the University of Kentucky using Mitsubishi Hitachi Power Systems’ H3-1 aqueous amine solvent. The analysis is based on data collected at a 0.7 MWe pilot unit combined with laboratory data and process simulations. The process adds a secondary air stripper to a conventional solvent process, which increases the cyclic loading of the solvent in two ways. First, air strips additional CO2 from the solvent downstream of the conventional steam-heated thermal stripper. This extra stripping of CO2 reduces the lean loading entering the absorber. Second, the CO2-enriched air is then sent to the boiler for use as secondary air. This recycling of CO2 results in a higher concentration of CO2 in the flue gas sent to the absorber, and hence a higher rich loading of the solvent exiting the absorber. A process model was incorporated into a full-scale supercritical pulverized coal power plant model to determine the plant performance and heat and mass balances. The performance and heat and mass balance data were used to size equipment and develop cost estimates for capital and operating costs. Lifecycle costs were considered through a levelized cost of electricity (LCOE) assessment based on the capital cost estimate and modeled performance. The results of the simulations show that the CAER process yields a regeneration energy of 3.12 GJ/t CO2, a 53.05/tCO2capturecost,andLCOEof53.05/t CO2 capture cost, and LCOE of 174.59/MWh. This compares to the U.S. Department of Energy\u27s projected costs (Case 10) of regeneration energy of 3.58 GJ/t CO2, a 61.31/tCO2capturecost,andLCOEof61.31/t CO2 capture cost, and LCOE of 189.59/MWh. For H3-1, the CAER process results in a regeneration energy of 2.62 GJ/tCO2 with a stripper pressure of 5.2 bar, a capture cost of 46.93/tCO2,andanLCOEof46.93/t CO2, and an LCOE of 164.33/MWh

    Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemia

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    Epsilon toxin (Etx) is a β-pore-forming toxin produced by Clostridium perfringens toxinotypes B and D and plays a key role in the pathogenesis of enterotoxemia, a severe, often fatal disease of ruminants that causes significant economic losses to the farming industry worldwide. This study aimed to determine the potential of a site-directed mutant of Etx (Y30A-Y196A) to be exploited as a recombinant vaccine against enterotoxemia. Replacement of Y30 and Y196 with alanine generated a stable variant of Etx with significantly reduced cell binding and cytotoxic activities in MDCK.2 cells relative to wild type toxin (>430-fold increase in CT50) and Y30A-Y196A was inactive in mice after intraperitoneal administration of trypsin activated toxin at 1000× the expected LD50 dose of trypsin activated wild type toxin. Moreover, polyclonal antibody raised in rabbits against Y30A-Y196A provided protection against wild type toxin in an in vitro neutralisation assay. These data suggest that Y30A-Y196A mutant could form the basis of an improved recombinant vaccine against enterotoxemia

    N-terminal amino acid sequences of chloroform/methanol-soluble proteins and albumins from endosperms of wheat, barley and related species: Homology with inhibitors of α-amylase and trypsin and with 2 S storage globulins

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    The N-terminal amino acid sequences of two chloroform/methanol soluble globulins from barley and one form wheat are reported. They are homologous with N-terminal sequences previously reported for α-amylase and trypsin inhibitors from cereals and 2 S storage proteins from castor bean and rape. Three albumins were also purified from Aegilops squarrosa and Triticum monococcum. These had N-terminal amino acid sequences most closely related to the α-amylase and trypsin inhibitors. The relationships of this superfamily of seed proteins are discussed
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