Results
The project aims at synthesizing protein/enzyme-based active membranes to be employed in membrane modules for the efficient process control of aldolase-catalyzed reactions. This modular approach is based on the synthesis of protein-polymer conjugates, which form a thin nanoporous membrane via self-assembly at fluid interfaces. The membrane function is controlled via the protein/enzyme building block employed. Membrane stability will be introduced via the proper choice of the polymer matrix.
Participating Core Groups (CG)
Coordinator
Prof. Dr. A. Böker, Makromolekulare Materialien und Oberflächen (MMO), RWTH Aachen University
Forckenbeckstr. 50
52056 Aachen
Germany
phone: +49 241 80 23304
e-mail: boker@dwi.rwth-aachen.de
Partners
Prof. Dr. J. Pietruszka, Bioorganische Chemie (BOC), Heinrich-Heine-University Düsseldorf
Prof. Dr. A. Spieß, AVT – Enzymprozesstechnik (AVT – EPT), RWTH Aachen University
Funding period
01.07.2014 – 30.09.2015
Funding
FlowCom is part of the NRW-Strategieprojekt BioSC and thus funded by the Ministry of Innovation, Science and Research of the German State of North Rhine-Westphalia.
Publications
Bisterfeld, C, Küberl, I, Dick, M and Pietruszka, J (2016). A fluorogenic screening for enantio- and diastereoselectivity of 2-deoxy-d-ribose-5-phosphate aldolases. Synlett 27(01): 11-16.
Dick, M, Hartmann, R, Weiergraber, OH, Bisterfeld, C, Classen, T, Schwarten, M, Neudecker, P, Willbold, D and Pietruszka, J (2016). Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: Structural insights and protective strategies. Chemical Science 7(7): 4492-4502.
Dick, M, Weiergräber, OH, Classen, T, Bisterfeld, C, Bramski, J, Gohlke, H and Pietruszka, J (2016). Trading off stability against activity in extremophilic aldolases. Scientific Reports 6: 17908.
Reinicke, S, Rees, HC, Espeel, P, Vanparijs, N, Bisterfeld, C, Dick, M, Rosencrantz, RR, Brezesinski, G, de Geest, BG, Du Prez, FE, Pietruszka, J and Boker, A (2017). Immobilization of 2-deoxy-d-ribose-5-phosphate aldolase in polymeric thin films via the langmuir-schaefer technique. ACS Appl Mater Interfaces 9(9): 8317-8326