Procédé agroalimentaire | EPFL Graph Search

vignette|Production de fromage. 10 000 litres de lait sont contenus dans la cuve de gauche, le lait est mélangé avec de la présure et est maintenant cassé pour la production d'Emmental. Les procédés agroalimentaires sont les moyens utilisés par l'industrie agroalimentaire pour transformer les produits agricoles alimentaires issus d'animaux (vache, poule) et de végétaux (céréales, légume) en aliments transformés industriels dévolus à l'alimentation humaine Articles connexes

Abattoir
Conservation des aliments
Réutilisation des déchets agroalimentaires
Emballage

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Uncooperative Rendezvous in Space: Design of an Electronic Architecture for High Performance Avionic with Multi Sensor Input and Intensive Data Rate.

Michaël Yannick Juillard

Active Debris Removal missions consist of sending a satellite in space and removing one or more debris from their current orbit. A key challenge is to obtain information about the uncooperative target. By gathering the velocity, position, and rotation of the desired object, the satellite is able to plan its trajectory and define the sequence of approach. It requires the use of a variety of sensors with often a high data rate. For this task, a dedicated payload computer is envisioned with the responsibility of processing the information from the various rendezvous sensors. This component has the goal to provide meaningful information to the main satellite computer about the targeted debris. The focus of this work is on the data processing, the number of elements, and the electrical energy with constraints due to internal communication.First, an avionic testbench was built at the EPFL Space Center to assess early hardware and software architectures. The goal is to enable Hardware-In-the-Loop testing while developing the payload computer. A communication data bus has been implemented between the Platform and the Payload On-Board Computer. Emphasis was placed on the reliability of the high-level protocol and multiple concepts for improvement were analyzed.In a second phase, the testbench has been extended to support other data buses. The aim was to develop a reliable and efficient backup or fall-back data bus in case of failure in the main link. Four data buses have been tested with extensive analyses on their resilience to error and the efficiency of their data exchange.In parallel, extensive work has been performed to develop a simulation and optimization tool. Its goal is to support the design of payload avionic architectures for ADR missions by providing trade-offs and analyses. In the first iteration, a simulator has been created with instances of various high-level elements modeled.The second iteration introduced the additional dimension of optimization. It is trying to determine the best set of instruments and algorithms to use. With this capability, numerous analyses have been conducted on the influence of various parameters linked to the general optimizer behavior. It allows us to better understand the strength and limitations of the tool.The third step regarding the tool was to start its verification. The task has been to develop an Hardware-In-the-Loop architecture to compare its behavior with the results of the optimizer. The implementation of various mock-up algorithms enables the verification of their models in the tool. These analyses guarantee the feasibility of the outputted solution.The last part was dedicated to the creation and analysis of a realistic payload avionic architecture. The goal was to test the capability of the tool with hardware elements inspired by actual components. This work has shown the procedure to efficiently use the tool in the design phase of a mission.In conclusion, the work on the communication between the Payload and the Platform On-Board Computer has brought valuable lessons and experiences to the projects. They can now be used for the establishment of the high-level protocol into ClearSpace-1 flight software. In addition, the optimizer created allows tackling the design of complex payload avionic architecture where mass saving and processing resources are crucial. It is an essential point to develop a highly efficient payload computer for an Active Debris Removal satellite.

EPFL2022

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Paolo De Los Rios, Giovanni Dietler, Jérôme Flakowski, Raffaele Mezzenga

The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections[1–5]. However, the physical mechanisms responsible for amyloidosis—the irreversible fibril formation of various proteins that is linked to disorders such as Alzheimer’s, Creutzfeldt–Jakob and Huntington’s diseases—have not yet been fully elucidated[6–9]. Here, we show that different stages of amyloid aggregation can be examined by performing a stat- istical polymer physics analysis of single-molecule atomic force microscopy images of heat-denatured b-lactoglobulin fibrils. The atomic force microscopy analysis, supported by theoretical arguments, reveals that the fibrils have a multistranded helical shape with twisted ribbon-like structures. Our results also indicate a possible general model for amyloid fibril assembly and illustrate the potential of this approach for investigating fibrillar systems. 1. Caughey, B. & Lansbury, P. T. Protofibrils, pores, fibrils and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267–298 (2003). 2. Stradner, A. et al. Equilibrium cluster formation in concentrated protein solutions and colloids. Nature 432, 492–495 (2004). 3. Mezzenga, R., Schurtenberger, P., Burbidge, A. & Michel, M. Understanding foods as soft materials. Nature Mater. 4, 729–740 (2005). 4. Selkoe, D. J. Folding proteins in fatal ways. Nature 426, 900–904 (2003). 5. Chiti, F. & Dobson, C. M. Amyloid formation by globular proteins under native conditions. Nature Chem. Biol. 5, 15–22 (2009). 6. Knowles, T. P. et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318, 1900–1903 (2007). 7. Nelson, R. et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature 435, 773–778 (2005). 8. Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid and human disease. Annu. Rev. Biochem. 75, 333–366 (2006). 9. Dobson, C. M. Protein folding and misfolding. Nature 426, 884–890 (2003).

Nature Publishing Group2010