@article{ThustSchoeningMuchandanietal.2003, author = {Thust, M. and Sch{\"o}ning, Michael Josef and Muchandani, A. and Wang, J. and Arzdorf, Michael and Mulchandani, P. and Chen, W.}, title = {Feldeffekt-Enzymsensor zur Detektion von Pestiziden}, series = {Sensoren f{\"u}r zuk{\"u}nftige Hochtechnologien und Neuentwicklungen f{\"u}r die Verfahrenstechnik / 6. Dresdner Sensor-Symposium, 8. - 10. Dezember 2003, Dresden. J{\"o}rg Peter Baselt; Gerald Gerlach (Hg.)}, journal = {Sensoren f{\"u}r zuk{\"u}nftige Hochtechnologien und Neuentwicklungen f{\"u}r die Verfahrenstechnik / 6. Dresdner Sensor-Symposium, 8. - 10. Dezember 2003, Dresden. J{\"o}rg Peter Baselt; Gerald Gerlach (Hg.)}, publisher = {w.e.b.-Univ.-Verl.}, address = {Dresden}, isbn = {3-935712-92-8}, pages = {125 -- 128}, year = {2003}, language = {de} } @article{WendlandtKochBritzetal.2023, author = {Wendlandt, Tim and Koch, Claudia and Britz, Beate and Liedek, Anke and Schmidt, Nora and Werner, Stefan and Gleba, Yuri and Vahidpour, Farnoosh and Welden, Melanie and Poghossian, Arshak and Sch{\"o}ning, Michael Josef}, title = {Facile Purification and Use of Tobamoviral Nanocarriers for Antibody-Mediated Display of a Two-Enzyme System}, series = {Viruses}, volume = {9}, journal = {Viruses}, number = {15}, publisher = {MDPI}, address = {Basel}, issn = {1999-4915}, doi = {doi.org/10.3390/v15091951}, pages = {Artikel 1951}, year = {2023}, abstract = {Immunosorbent turnip vein clearing virus (TVCV) particles displaying the IgG-binding domains D and E of Staphylococcus aureus protein A (PA) on every coat protein (CP) subunit (TVCVPA) were purified from plants via optimized and new protocols. The latter used polyethylene glycol (PEG) raw precipitates, from which virions were selectively re-solubilized in reverse PEG concentration gradients. This procedure improved the integrity of both TVCVPA and the wild-type subgroup 3 tobamovirus. TVCVPA could be loaded with more than 500 IgGs per virion, which mediated the immunocapture of fluorescent dyes, GFP, and active enzymes. Bi-enzyme ensembles of cooperating glucose oxidase and horseradish peroxidase were tethered together on the TVCVPA carriers via a single antibody type, with one enzyme conjugated chemically to its Fc region, and the other one bound as a target, yielding synthetic multi-enzyme complexes. In microtiter plates, the TVCVPA-displayed sugar-sensing system possessed a considerably increased reusability upon repeated testing, compared to the IgG-bound enzyme pair in the absence of the virus. A high coverage of the viral adapters was also achieved on Ta2O5 sensor chip surfaces coated with a polyelectrolyte interlayer, as a prerequisite for durable TVCVPA-assisted electrochemical biosensing via modularly IgG-assembled sensor enzymes.}, language = {en} } @article{YoshinobuSchoeningFingeretal.2004, author = {Yoshinobu, T. and Sch{\"o}ning, Michael Josef and Finger, F. and Moritz, W. and Iwasaki, H.}, title = {Fabrication of thin-film LAPS with amorphous silicon}, series = {Sensors. 4 (2004), H. 10}, journal = {Sensors. 4 (2004), H. 10}, isbn = {1424-8220}, pages = {163 -- 169}, year = {2004}, language = {en} } @article{MuckWangJacobsetal.2004, author = {Muck, A. and Wang, J. and Jacobs, M. and Chen, G. and Chatrathi, M. P. and Jurka, V. and Vyborny, Z. and Spillmann, S. D. and Sridharan, G. and Sch{\"o}ning, Michael Josef}, title = {Fabrication of poly(methyl methacrylate) microfluidic chips by atmospheric molding}, series = {Analytical Chemistry. 76 (2004), H. 8}, journal = {Analytical Chemistry. 76 (2004), H. 8}, isbn = {0003-2700}, pages = {2290 -- 2297}, year = {2004}, language = {en} } @article{TakenagaSchneiderErbayetal.2015, author = {Takenaga, Shoko and Schneider, Benno and Erbay, E. and Biselli, Manfred and Schnitzler, Thomas and Sch{\"o}ning, Michael Josef and Wagner, Torsten}, title = {Fabrication of biocompatible lab-on-chip devices for biomedical applications by means of a 3D-printing process}, series = {Physica status solidi (a)}, volume = {212}, journal = {Physica status solidi (a)}, number = {6}, publisher = {Wiley}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201532053}, pages = {1347 -- 1352}, year = {2015}, abstract = {A new microfluidic assembly method for semiconductor-based biosensors using 3D-printing technologies was proposed for a rapid and cost-efficient design of new sensor systems. The microfluidic unit is designed and printed by a 3D-printer in just a few hours and assembled on a light-addressable potentiometric sensor (LAPS) chip using a photo resin. The cell growth curves obtained from culturing cells within microfluidics-based LAPS systems were compared with cell growth curves in cell culture flasks to examine biocompatibility of the 3D-printed chips. Furthermore, an optimal cell culturing within microfluidics-based LAPS chips was achieved by adjusting the fetal calf serum concentrations of the cell culture medium, an important factor for the cell proliferation.}, language = {en} } @article{RibitschHeumannKarletal.2012, author = {Ribitsch, D. and Heumann, S. and Karl, W. and Gerlach, J. and Leber, R. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Siegert, Petra and Lange, J. and Maurer, Karl-Heinz and Berg, G. and Guebitz, G. M. and Schwab, H.}, title = {Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli}, series = {Journal of biotechnology}, volume = {157}, journal = {Journal of biotechnology}, number = {1}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2011.09.025}, pages = {140 -- 147}, year = {2012}, abstract = {A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3. From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.}, language = {en} } @article{SchrothSchoeningLuethetal.2001, author = {Schroth, P. and Sch{\"o}ning, Michael Josef and L{\"u}th, H. and Weißbecker, B. and Hummel, Hans E. and Sch{\"u}tz, S.}, title = {Extending the capabilities of an antenna/chip biosensor by employing various insect species}, series = {Sensors and Actuators B. 78 (2001), H. 1-3}, journal = {Sensors and Actuators B. 78 (2001), H. 1-3}, isbn = {0925-4005}, pages = {1 -- 5}, year = {2001}, language = {en} } @article{SchrothSchoeningLuethetal.2000, author = {Schroth, P. and Sch{\"o}ning, Michael Josef and L{\"u}th, H. and Weißbecker, B. and Hummel, Hans E. and Sch{\"u}tz, S.}, title = {Extending the capabilities of an antenna/chip biosensor by employing various insect species}, series = {Proceedings : Copenhagen, Denmark, 27 - 30 August 2000 / [ed.: R. de Reus ...]}, journal = {Proceedings : Copenhagen, Denmark, 27 - 30 August 2000 / [ed.: R. de Reus ...]}, publisher = {MIC, Mikroelektronik Centret}, address = {Lyngby, Denmark}, isbn = {87-89935-50-0}, pages = {27 -- 30}, year = {2000}, language = {en} } @article{JildehOberlaenderKirchneretal.2018, author = {Jildeh, Zaid B. and Oberl{\"a}nder, Jan and Kirchner, Patrick and Keusgen, Michael and Wagner, Patrick H. and Sch{\"o}ning, Michael Josef}, title = {Experimental and Numerical Analyzes of a Sensor Based on Interdigitated Electrodes for Studying Microbiological Alterations}, series = {physica status solidi (a): applications and materials science}, volume = {215}, journal = {physica status solidi (a): applications and materials science}, number = {15}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201700920}, pages = {Artikel 1700920}, year = {2018}, abstract = {In this work, a cell-based biosensor to evaluate the sterilization efficacy of hydrogen peroxide vapor sterilization processes is characterized. The transducer of the biosensor is based on interdigitated gold electrodes fabricated on an inert glass substrate. Impedance spectroscopy is applied to evaluate the sensor behavior and the alteration of test microorganisms due to the sterilization process. These alterations are related to changes in relative permittivity and electrical conductivity of the bacterial spores. Sensor measurements are conducted with and without bacterial spores (Bacillus atrophaeus), as well as after an industrial sterilization protocol. Equivalent two-dimensional numerical models based on finite element method of the periodic finger structures of the interdigitated gold electrodes are designed and validated using COMSOL® Multiphysics software by the application of known dielectric properties. The validated models are used to compute the electrical properties at different sensor states (blank, loaded with spores, and after sterilization). As a final result, we will derive and tabulate the frequency-dependent electrical parameters of the spore layer using a novel model that combines experimental data with numerical optimization techniques.}, language = {en} } @article{SiegertMcLeishBaumannetal.2005, author = {Siegert, Petra and McLeish, Michael J. and Baumann, Martin and Iding, Hans and Kneen, Malea M. and Kenyon, George L. and Pohl, Martina}, title = {Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida}, series = {Protein engineering, design, and selection : peds}, volume = {Vol. 18}, journal = {Protein engineering, design, and selection : peds}, number = {Iss. 7}, issn = {1460-213X (E-Journal); 1741-0134 (E-Journal); 0269-2139 (Print); 1741-0126 (Print)}, pages = {345 -- 357}, year = {2005}, language = {en} }