@incollection{UlrichSchlegelMertensetal., author = {Ulrich, Rainer G. and Schlegel, Matthias and Mertens, Marc and Groschup, Martin H. and Schmidt-Chanasit, Jonas and Plenge-B{\"o}nig, Anita and Jacob, Jens and Pelz, Hans-Joachim and Freise, Jona and Wenk, Matthias and Thiel, J{\"o}rg and Triebenbacher, Cornelia and Schmolz, Eric and Kurth, Andreas and Kr{\"u}ger, Frank and R{\"u}he, Ferdinand and Kiffner, Christian and Ansorge, Hermann and Gerwin, Werner and Wegener, Wolfgang and M{\"u}ller, J{\"o}rg and Bemmann, Margit and Wolf, Ronny and Otto, Lutz-Florian and Oehme, Rainer and Pfeffer, Martin and Heckel, Gerald and Schex, Susanne and Essbauer, Sandra S.}, title = {Netzwerk Nagetier-{\"u}bertragene Pathogene: Monitoring von Hantavirus-Infektionen in Deutschland}, series = {Wildhygiene, Wildtierkrankheiten, Parasiten, Epidemiologie}, booktitle = {Wildhygiene, Wildtierkrankheiten, Parasiten, Epidemiologie}, publisher = {Ges. f{\"u}r Wildtier- und Jagdforschung}, address = {Halle/Saale}, isbn = {978-378-88131-2-3}, issn = {1436-3895}, pages = {229 -- 250}, language = {de} } @misc{FoersterSchenkZollneretal., author = {F{\"o}rster, Stefan and Schenk, Sebastian and Zollner, Eva Maria and Krahn, Oliver and Chiang, Cheng-Tien and Schumann, Florian O. and Bayat, Alireza and Schindler, Karl-Michael and Trautmann, Martin and Hammer, Ren{\´e} and Meinel, Klaus and Adeagbo, Waheed A. and Hergert, Wolfram and Flege, Jan Ingo and Falta, Jens and Ellguth, Martin and Tusche, Christian and DeBoissieu, Marc and Muntwiler, Matthias and Gerber, Thomas and Widdra, Wolf}, title = {Quasicrystals and their Approximants in 2D Ternary Oxides}, series = {Physia Status Solidi B}, volume = {257}, journal = {Physia Status Solidi B}, number = {7}, issn = {0370-1972}, doi = {10.1002/pssb.201900624}, pages = {11}, abstract = {2D oxide quasicrystals (OQCs) are recently discovered aperiodic, but well-ordered oxide interfaces. In this topical review, an introduction to these new thin-film systems is given. The concept of quasicrystals and their approximants is explained for BaTiO3 and SrTiO3 derived OQCs and related periodic structures in these 2D oxides. In situ microscopy unravels the high-temperature formation process of OQCs on Pt(111). The dodecagonal structure is discussed regarding tiling statistics and tiling decoration based on the results of atomically resolved scanning tunneling microscopy and various diffraction techniques. In addition, angle-resolved ultraviolet photoemission spectroscopy and X-ray photoelectron spectroscopy results prove a metallic character of the 2D oxide.}, language = {en} } @misc{BoehlerRosencrantzWolfetal., author = {B{\"o}hler, Stefan and Rosencrantz, Sophia and Wolf, Karina and Heinemann, Robert and Schmidt, Peer and Ganster, Johannes and B{\"u}sse, Thomas and Balko, Jens and Rosencrantz, Ruben R.}, title = {Active protease formulation in commodity polymers withstands melt processing into compounds and blown films}, series = {Materials Today Communications}, volume = {34}, journal = {Materials Today Communications}, issn = {2352-4928}, doi = {10.1016/j.mtcomm.2022.105018}, pages = {1 -- 9}, abstract = {Integrating enzymes into thermoplastic polymers is challenging due to their lack of robustness with respect to temperature and shear fields during conventional melt processing. In the present study, blown films from low-density polyethylene (LDPE) were prepared containing a technical protease from Bacillus sp. First, LDPE/protease compounds were produced followed by blown film extrusion, both processes at melt mass temperatures of 130 °C or higher. Enzyme activity was proven, both for the LDPE/protease compound and the blown film. The highest enzyme activity in the compound was determined for processing at 132 °C and a screw speed of 75 rpm. The influence of melt temperature and shear fields was studied in detail. Enzyme activities were determined for melt temperatures up to 160 °C and for screw speeds ranging from 75 to 300 rpm during compounding by twin-screw extrusion. The process was also applied for biobased and biodegradable polyesters, where similar protease activity after compounding was verified. Electron microscopy, X-ray diffraction, nuclear magnetic resonance spectroscopy and differential scanning calorimetry served to analyze components and morphology of the enzyme formulation used here. It is proposed that the porous morphology of the protease particles is beneficial for the enzyme to remain active after processing. Additionally, the polymer matrix surrounding the particles protects the protease at elevated temperatures, which can be attributed to thermal insulation. Thus, the right combination of a suited technical enzyme formulation with appropriate mild melt compounding conditions allows enzymes to be incorporated into thermoplastics and retain their activity. This opens the way to use the abundant biological functions of enzymes in thermoplastic applications.}, language = {en} } @inproceedings{IfwerWolfAnhedenetal., author = {Ifwer, Karin and Wolf, Jens and Anheden, Marie and Sarunac, Nenad and Bullinger, Charlie and Ness, Marc and H{\"o}hne, Olaf}, title = {Air/Nitrogen lignite dryer as an alternative to a stream dryer in a power plant using oxyfuel technique for CO2 capture}, language = {de} }