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Aircraft configurations with propellers have been drawing more attention in recent times, partly due to new propulsion concepts based on hydrogen fuel cells and electric motors. These configurations are prone to whirl flutter, which is an aeroelastic instability affecting airframes with elastically supported propellers. It commonly needs to be mitigated already during the design phase of such configurations, requiring, among other things, unsteady aerodynamic transfer functions for the propeller. However, no comprehensive assessment of unsteady propeller aerodynamics for aeroelastic analysis is available in the literature. This paper provides a detailed comparison of nine different low- to mid-fidelity aerodynamic methods, demonstrating their impact on linear, unsteady aerodynamics, as well as whirl flutter stability prediction. Quasi-steady and unsteady methods for blade lift with or without coupling to blade element momentum theory are evaluated and compared to mid-fidelity potential flow solvers (UPM and DUST) and classical, derivative-based methods. Time-domain identification of frequency-domain transfer functions for the unsteady propeller hub loads is used to compare the different methods. Predictions of the minimum required pylon stiffness for stability show good agreement among the mid-fidelity methods. The differences in the stability predictions for the low-fidelity methods are higher. Most methods studied yield a more unstable system than classical, derivative-based whirl flutter analysis, indicating that the use of more sophisticated aerodynamic modeling techniques might be required for accurate whirl flutter prediction.
N-Acyl-amino acids can act as mild biobased surfactants, which are used, e.g., in baby shampoos. However, their chemical synthesis needs acyl chlorides and does not meet sustainability criteria. Thus, the identification of biocatalysts to develop greener synthesis routes is desirable. We describe a novel aminoacylase from Paraburkholderia monticola DSM 100849 (PmAcy) which was identified, cloned, and evaluated for its N-acyl-amino acid synthesis potential. Soluble protein was obtained by expression in lactose autoinduction medium and co-expression of molecular chaperones GroEL/S. Strep-tag affinity purification enriched the enzyme 16-fold and yielded 15 mg pure enzyme from 100 mL of culture. Biochemical characterization revealed that PmAcy possesses beneficial traits for industrial application like high temperature and pH-stability. A heat activation of PmAcy was observed upon incubation at temperatures up to 80 °C. Hydrolytic activity of PmAcy was detected with several N-acyl-amino acids as substrates and exhibited the highest conversion rate of 773 U/mg with N-lauroyl-L-alanine at 75 °C. The enzyme preferred long-chain acyl-amino-acids and displayed hardly any activity with acetyl-amino acids. PmAcy was also capable of N-acyl-amino acid synthesis with good conversion rates. The best synthesis results were obtained with the cationic L-amino acids L-arginine and L-lysine as well as with L-leucine and L-phenylalanine. Exemplarily, L-phenylalanine was acylated with fatty acids of chain lengths from C8 to C18 with conversion rates of up to 75%. N-lauroyl-L-phenylalanine was purified by precipitation, and the structure of the reaction product was verified by LC–MS and NMR.