@article{ReisertHenkelSchneideretal.2009, author = {Reisert, Steffen and Henkel, H. and Schneider, A. and Sch{\"a}fer, D. and Friedrich, P. and Berger, J. and Sch{\"o}ning, Michael Josef}, title = {Entwicklung eines Handheld-Sensorsystems f{\"u}r die „On-line"-Messung der H2O2-Konzentration in aseptischen Entkeimungsprozessen}, series = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]}, journal = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]}, publisher = {TUDpress}, address = {Dresden}, isbn = {978-3-941298-44-6}, pages = {285 -- 288}, year = {2009}, language = {de} } @article{ReisertHenkelSchneideretal.2010, author = {Reisert, Steffen and Henkel, Hartmut and Schneider, Andreas and Sch{\"a}fer, Daniel and Friedrich, Peter and Berger, J{\"o}rg and Sch{\"o}ning, Michael Josef}, title = {Development of a handheld sensor system for the online measurement of hydrogen peroxide in aseptic filling systems}, series = {Physica Status Solidi (A). 207 (2010), H. 4}, journal = {Physica Status Solidi (A). 207 (2010), H. 4}, isbn = {1862-6300}, pages = {913 -- 918}, year = {2010}, language = {en} } @article{ReisertSchneiderGeissleretal.2013, author = {Reisert, Steffen and Schneider, Benno and Geissler, Hanno and Gompel, Matthias van and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Multi-sensor chip for the investigation of different types of metal oxides for the detection of H2O2 in the ppm range}, series = {physica status solidi (a)}, volume = {210}, journal = {physica status solidi (a)}, number = {5}, publisher = {Wiley}, address = {Weinheim}, issn = {1862-6319}, pages = {898 -- 904}, year = {2013}, abstract = {In this work, a multi-sensor chip for the investigation of the sensing properties of different types of metal oxides towards hydrogen peroxide in the ppm range is presented. The fabrication process and physical characterization of the multi-sensor chip are described. Pure SnO2 and WO3 as well as Pd- and Pt-doped SnO2 films are characterized in terms of their sensitivity to H2O2. The sensing films have been prepared by drop-coating of water-dispensed nano-powders. A physical characterization, including scanning electron microscopy and X-ray diffraction analysis of the deposited metal-oxide films, was done. From the measurements in hydrogen peroxide atmosphere, it could be shown, that all of the tested metal oxide films are suitable for the detection of H2O2 in the ppm range. The highest sensitivity and reproducibility was achieved using Pt-doped SnO2. Calibration plot of a SnO2, WO3, Pt-, and Pd-doped SnO2 gas sensor for H2O2 concentrations in the ppm range.}, 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{RibitschKarlBirnerGruenbergeretal.2010, author = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.}, title = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli}, series = {Journal of biotechnology}, volume = {150}, journal = {Journal of biotechnology}, number = {3}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2010.09.947}, pages = {408 -- 416}, year = {2010}, abstract = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.}, language = {en} } @article{RiemerSchrothSchuetzetal.2000, author = {Riemer, A. and Schroth, P. and Sch{\"u}tz, S. and Hummel, Hans E. and L{\"u}th, H. and Kohl, C.-D. and Sch{\"o}ning, Michael Josef}, title = {The future of fire detection: Biological sensors? - Die Zukunft der Brandgassensorik: Biologische Sensoren?}, series = {Gassensorik in der Brandmeldetechnik : [VdS-Fachtagung, am 15. und 16. November 2000 in K{\"o}ln] = Gas sensors for fire detection / VdS Schadenverh{\"u}tung}, journal = {Gassensorik in der Brandmeldetechnik : [VdS-Fachtagung, am 15. und 16. November 2000 in K{\"o}ln] = Gas sensors for fire detection / VdS Schadenverh{\"u}tung}, publisher = {VdS Schadenverh{\"u}tung}, address = {K{\"o}ln}, pages = {1 -- 7}, year = {2000}, language = {en} } @inproceedings{RoderburgSchoening2008, author = {Roderburg, Katharina and Sch{\"o}ning, Michael Josef}, title = {1. Graduierten-Tagung : 9. September 2008 / [Hrsg.: K. Roderburg ; M. J. Sch{\"o}ning]}, organization = {FH Aachen, University of Applied Sciences / Graduiertentagung <1, 2008>}, url = {http://nbn-resolving.de/urn:nbn:de:hbz:a96-opus-3125}, year = {2008}, abstract = {Tagungsband der Graduiertentagung der FH Aachen, in dem Doktorandinnen und Doktoranden und ihre Forschungsbereiche vorgestellt werden}, subject = {Aachen / Fachhochschule Aachen}, language = {de} } @article{RodriguesMoraisNordietal.2018, author = {Rodrigues, Raul T. and Morais, Paulo V. and Nordi, Cristina S. F. and Sch{\"o}ning, Michael Josef and Siqueira Jr., Jos{\´e} R. and Caseli, Luciano}, title = {Carbon Nanotubes and Algal Polysaccharides To Enhance the Enzymatic Properties of Urease in Lipid Langmuir-Blodgett Films}, series = {Langmuir}, volume = {34}, journal = {Langmuir}, number = {9}, publisher = {ACS Publications}, address = {Washington, DC}, issn = {1520-5827}, doi = {10.1021/acs.langmuir.7b04317}, pages = {3082 -- 3093}, year = {2018}, abstract = {Algal polysaccharides (extracellular polysaccharides) and carbon nanotubes (CNTs) were adsorbed on dioctadecyldimethylammonium bromide Langmuir monolayers to serve as a matrix for the incorporation of urease. The physicochemical properties of the supramolecular system as a monolayer at the air-water interface were investigated by surface pressure-area isotherms, surface potential-area isotherms, interfacial shear rheology, vibrational spectroscopy, and Brewster angle microscopy. The floating monolayers were transferred to hydrophilic solid supports, quartz, mica, or capacitive electrolyte-insulator-semiconductor (EIS) devices, through the Langmuir-Blodgett (LB) technique, forming mixed films, which were investigated by quartz crystal microbalance, fluorescence spectroscopy, and field emission gun scanning electron microscopy. The enzyme activity was studied with UV-vis spectroscopy, and the feasibility of the thin film as a urea sensor was essayed in an EIS sensor device. The presence of CNT in the enzyme-lipid LB film not only tuned the catalytic activity of urease but also helped to conserve its enzyme activity. Viability as a urease sensor was demonstrated with capacitance-voltage and constant capacitance measurements, exhibiting regular and distinctive output signals over all concentrations used in this work. These results are related to the synergism between the compounds on the active layer, leading to a surface morphology that allowed fast analyte diffusion owing to an adequate molecular accommodation, which also preserved the urease activity. This work demonstrates the feasibility of employing LB films composed of lipids, CNT, algal polysaccharides, and enzymes as EIS devices for biosensing applications.}, language = {en} } @article{RolkaPoghossianSchoening2004, author = {Rolka, David and Poghossian, Arshak and Sch{\"o}ning, Michael Josef}, title = {Integration of a capacitive EIS sensor into a FIA system for pH and penicillin determination}, series = {Sensors. 4 (2004)}, journal = {Sensors. 4 (2004)}, isbn = {1424-8220}, pages = {84 -- 94}, year = {2004}, language = {en} } @article{RosenauerOberstLitvinovetal.2000, author = {Rosenauer, A. and Oberst, W. and Litvinov, D. and Gerthsen, D. and F{\"o}rster, Arnold and Schmidt, R.}, title = {Structural and Chemical Investigation of In-0.6Ga0.4As Stranski-Krastanow Layers Burried in GaAs by Transmission Electron Microscopy}, series = {Physical Review B. 61 (2000), H. 12}, journal = {Physical Review B. 61 (2000), H. 12}, isbn = {1095-3795}, pages = {8276 -- 8288}, year = {2000}, language = {en} }