Fuel quality impact analysis for practical implementation of corn COB gasification gas in conventional gas turbine power plants

Practical implementation of alternative fuels in gas turbine facilities is a challenging step towards cleaner and more responsible energy production. Despite numerous technical, economical and legal obstacles, possibilities for partial or complete substitution of fossil fuels are still subject of profound research. From all possible solutions, one with high acceptance is the symbiosis of existing gas turbine technologies and new ways of waste biomass energy utilization through firing or co – firing of biomass gasification gas. Therefore, the practical implementation of corn cob gasification gas with CO2 recirculation in gas turbines is analyzed in this paper. The followed methodology approaches this solution through two different scenarios each with 5 different cases. In the first scenario fuel mass flows are kept constant regardless of the fuel quality change consequence of the corn cob gas share, while in the second scenario fuel volume flows are assumed constant. Fuel quality refers to fuel composition which affects heat capacity, as well as physical and chemical characteristics of fuel. Impact of fuel composition changes on combustion product characteristics was analyzed using CHEMKIN PRO with GRI–Mech 3.0. Finally, fuel quality impacts on a gas turbine power plant performance are analyzed using a numerical model of a physical cycle that enables the simulation of a 3.9 MW experimentally correlated gas turbine. The results show that utilization of corn cob gasification gas is possible through co-firing with natural gas with acceptable values without modification of the fuel system or gas turbine

A Mesh Adaptation Strategy to Predict Pressure Losses in LES of Swirled Flows

The research leading to these results has received funding from the European Research Council under the European Union’s Seventh Framework Program (FP/2007-2013) / ERC Grant Agreement ERC-AdG 319067-INTECOCIS

Mps1Mph1 kinase phosphorylates Mad3 to inhibit Cdc20Slp1-APC/C and maintain spindle checkpoint arrests

<div><p>The spindle checkpoint is a mitotic surveillance system which ensures equal segregation of sister chromatids. It delays anaphase onset by inhibiting the action of the E3 ubiquitin ligase known as the anaphase promoting complex or cyclosome (APC/C). Mad3/BubR1 is a key component of the mitotic checkpoint complex (MCC) which binds and inhibits the APC/C early in mitosis. Mps1^Mph1 kinase is critical for checkpoint signalling and MCC-APC/C inhibition, yet few substrates have been identified. Here we identify Mad3 as a substrate of fission yeast Mps1^Mph1 kinase. We map and mutate phosphorylation sites in Mad3, producing mutants that are targeted to kinetochores and assembled into MCC, yet display reduced APC/C binding and are unable to maintain checkpoint arrests. We show biochemically that Mad3 phospho-mimics are potent APC/C inhibitors <i>in vitro</i>, demonstrating that Mad3p modification can directly influence Cdc20^Slp1-APC/C activity. This genetic dissection of APC/C inhibition demonstrates that Mps1^Mph1 kinase-dependent modifications of Mad3 and Mad2 act in a concerted manner to maintain spindle checkpoint arrests.</p></div

Kdm3a lysine demethylase is an Hsp90 client required for cytoskeletal rearrangements during spermatogenesis

The lysine demethylase Kdm3a (Jhdm2a, Jmjd1a) is required for male fertility, sex determination, and metabolic homeostasis through its nuclear role in chromatin remodeling. Many histone-modifying enzymes have additional nonhistone substrates, as well as nonenzymatic functions, contributing to the full spectrum of events underlying their biological roles. We present two Kdm3a mouse models that exhibit cytoplasmic defects that may account in part for the globozoospermia phenotype reported previously. Electron microscopy revealed abnormal acrosome and manchette and the absence of implantation fossa at the caudal end of the nucleus in mice without Kdm3a demethylase activity, which affected cytoplasmic structures required to elongate the sperm head. We describe an enzymatically active new Kdm3a isoform and show that subcellular distribution, protein levels, and lysine demethylation activity of Kdm3a depended on Hsp90. We show that Kdm3a localizes to cytoplasmic structures of maturing spermatids affected in Kdm3a mutant mice, which in turn display altered fractionation of beta-actin and gamma-tubulin. Kdm3a is therefore a multifunctional Hsp90 client protein that participates directly in the regulation of cytoskeletal components.Publisher PDFPeer reviewe