@article{MorenoiCodinachsKloockSchoeningetal.2008, author = {Moreno i Codinachs, Lia and Kloock, Joachim P. and Sch{\"o}ning, Michael Josef and Baldi, Antoni and Ipatov, Andrey and Bratov, Andrey and Jimenez-Jorquera, Cecilia}, title = {Electronic integrated multisensor tongue applied to grape juice and wine analysis}, series = {Analyst. 133 (2008)}, journal = {Analyst. 133 (2008)}, isbn = {1364-5528}, pages = {1440 -- 1448}, year = {2008}, language = {en} } @article{KrafftFoersterHartetal.2001, author = {Krafft, B. and F{\"o}rster, Arnold and Hart, A. van der and Sch{\"a}pers, T.}, title = {Control of Aharonov-Bohm oscillations in a AlGaAs/GaAs ring by asymmetric and symmetric gate biasing}, series = {Physica E: Low-dimensional Systems and Nanostructures. 9 (2001), H. 4}, journal = {Physica E: Low-dimensional Systems and Nanostructures. 9 (2001), H. 4}, isbn = {1386-9477}, pages = {635 -- 641}, year = {2001}, 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} } @article{ItabashiKosakaMiyamotoetal.2013, author = {Itabashi, Akinori and Kosaka, Naoki and Miyamoto, Ko-ichiro and Wagner, Torsten and Sch{\"o}ning, Michael Josef}, title = {High-speed chemical imaging system based on front-side-illuminated LAPS}, series = {Sensors and actuators B: Chemical}, volume = {182}, journal = {Sensors and actuators B: Chemical}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-3077}, doi = {10.1016/j.snb.2013.03.016}, pages = {315 -- 321}, year = {2013}, abstract = {The chemical imaging sensor is a semiconductor-based chemical sensor that can visualize the spatial distribution of specific ions on the sensing surface. The conventional chemical imaging system based on the light-addressable potentiometric sensor (LAPS), however, required a long time to obtain a chemical image, due to the slow mechanical scan of a single light beam. For high-speed imaging, a plurality of light beams modulated at different frequencies can be employed to measure the ion concentrations simultaneously at different locations on the sensor plate by frequency division multiplex (FDM). However, the conventional measurement geometry of back-side illumination limited the bandwidth of the modulation frequency required for FDM measurement, because of the low-pass filtering characteristics of carrier diffusion in the Si substrate. In this study, a high-speed chemical imaging system based on front-side-illuminated LAPS was developed, which achieved high-speed spatiotemporal recording of pH change at a rate of 70 frames per second.}, language = {en} } @article{IkenAhlbornGerlachetal.2013, author = {Iken, Heiko and Ahlborn, K. and Gerlach, F. and Vonau, W. and Zander, W. and Schubert, J. and Sch{\"o}ning, Michael Josef}, title = {Development of redox glasses and subsequent processing by means of pulsed laser deposition for realizing silicon-based thin-film sensors}, series = {Electrochimica acta}, journal = {Electrochimica acta}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-3859 (E-Journal); 0013-4686 (Print)}, pages = {Available online 30.8.2013}, year = {2013}, language = {en} } @article{BandodkarMolinnusMirzaetal.2014, author = {Bandodkar, Amay J. and Molinnus, Denise and Mirza, Omar and Guinovart, Tomas and Windmiller, Joshua R. and Valdes-Ramirez, Gabriela and Andrade, Francisco J. and Sch{\"o}ning, Michael Josef and Wang, Joseph}, title = {Epidermal tattoo potentiometric sodium sensors with wireless signal transduction for continuous non-invasive sweat monitoring}, series = {Biosensors and bioelectronics}, volume = {54}, journal = {Biosensors and bioelectronics}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4235 (E-Journal); 0956-5663 (Print)}, doi = {10.1016/j.bios.2013.11.039}, pages = {603 -- 609}, year = {2014}, abstract = {This article describes the fabrication, characterization and application of an epidermal temporary-transfer tattoo-based potentiometric sensor, coupled with a miniaturized wearable wireless transceiver, for real-time monitoring of sodium in the human perspiration. Sodium excreted during perspiration is an excellent marker for electrolyte imbalance and provides valuable information regarding an individual's physical and mental wellbeing. The realization of the new skin-worn non-invasive tattoo-like sensing device has been realized by amalgamating several state-of-the-art thick film, laser printing, solid-state potentiometry, fluidics and wireless technologies. The resulting tattoo-based potentiometric sodium sensor displays a rapid near-Nernstian response with negligible carryover effects, and good resiliency against various mechanical deformations experienced by the human epidermis. On-body testing of the tattoo sensor coupled to a wireless transceiver during exercise activity demonstrated its ability to continuously monitor sweat sodium dynamics. The real-time sweat sodium concentration was transmitted wirelessly via a body-worn transceiver from the sodium tattoo sensor to a notebook while the subjects perspired on a stationary cycle. The favorable analytical performance along with the wearable nature of the wireless transceiver makes the new epidermal potentiometric sensing system attractive for continuous monitoring the sodium dynamics in human perspiration during diverse activities relevant to the healthcare, fitness, military, healthcare and skin-care domains.}, language = {en} } @article{ReisertGeisslerFloerkeetal.2013, author = {Reisert, Steffen and Geissler, Hanno and Fl{\"o}rke, Rudolf and Weiler, Christian and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Characterisation of aseptic sterilisation processes using an electronic nose}, series = {International journal of nanotechnology}, volume = {Vol. 10}, journal = {International journal of nanotechnology}, number = {No. 5-7}, publisher = {Inderscience Enterprises}, address = {Gen{\`e}ve}, issn = {1475-7435 (Print) 7141-8151 (Online)}, pages = {470 -- 484}, year = {2013}, language = {en} } @article{MiyamotoHirayamaWagneretal.2013, author = {Miyamoto, Ko-ichiro and Hirayama, Yuji and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo}, title = {Visualization of enzymatic reaction in a microfluidic channel using chemical imaging sensor}, series = {Electrochimica acta}, journal = {Electrochimica acta}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-3859 (E-Journal); 0013-4686 (Print)}, pages = {Publ. online}, year = {2013}, language = {en} } @misc{IngebrandtWagnerSchoening2013, author = {Ingebrandt, Sven and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Engineering of functional interfaces / guest eds. Sven Ingebrandt ; Patrick Wagner ; Michael J. Sch{\"o}ning}, series = {Physica Status Solidi (A)}, volume = {Vol. 210}, journal = {Physica Status Solidi (A)}, number = {Iss. 5}, issn = {1521-396X (E-Journal); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)}, pages = {845}, year = {2013}, language = {en} } @misc{AbdelghaniMenaaObareetal.2013, author = {Abdelghani, Adnane and Menaa, Bouzid and Obare, Sherine O. and Sch{\"o}ning, Michael Josef}, title = {Special issue on nanoscale science and technology / guest eds.: Adnane Abdelghani, Bouzid Menaa, Sherine O. Obare, Michael J. Sch{\"o}ning}, series = {International journal of nanotechnology}, volume = {Vol. 10}, journal = {International journal of nanotechnology}, number = {No. 5-7}, issn = {1741-8151 (E-Journal), 1475-7435 (Print)}, pages = {373 -- 619}, year = {2013}, language = {en} } @article{SabitovaEbertLenzetal.2013, author = {Sabitova, A. and Ebert, Ph. and Lenz, A. and Schaafhausen, S. and Ivanova, L. and D{\"a}hne, M. and Hoffmann, A. and Dunin-Borkowski, R. E. and F{\"o}rster, Arnold and Grandidier, B. and Eisele, H.}, title = {Intrinsic bandgap of cleaved ZnO(112¯0) surfaces}, series = {Applied physics letters}, volume = {Vol. 102}, journal = {Applied physics letters}, issn = {1077-3118 (E-Journal); 0003-6951 (Print)}, pages = {021608}, year = {2013}, language = {en} } @inproceedings{TakenagaHerreraWerneretal.2013, author = {Takenaga, Shoko and Herrera, Cony F. and Werner, Frederik and Biselli, Manfred and Schnitzler, Thomas and Sch{\"o}ning, Michael Josef and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten}, title = {Detection of the metabolic activity of cells by differential measurements based on a single light-addressable potentiometric sensor chip}, series = {11. Dresdner Sensor-Symposium : 9.-11.12.2013}, booktitle = {11. Dresdner Sensor-Symposium : 9.-11.12.2013}, organization = {Dresdner Sensor-Symposium <11, 2013>}, isbn = {978-3-9813484-5-3}, pages = {63 -- 67}, year = {2013}, language = {en} } @article{HeineHerrmannSelmeretal.2014, author = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.}, title = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily}, series = {Proteins}, volume = {82}, journal = {Proteins}, number = {9}, publisher = {Wiley-Liss}, address = {New York}, issn = {1097-0134 (E-Journal); 0887-3585 (Print)}, doi = {10.1002/prot.24557}, pages = {2041 -- 2053}, year = {2014}, abstract = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.}, language = {en} } @article{TakenagaBiselliSchnitzleretal.2014, author = {Takenaga, Shoko and Biselli, Manfred and Schnitzler, Thomas and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten and Sch{\"o}ning, Michael Josef}, title = {Toward multi-analyte bioarray sensors: LAPS-based on-chip determination of a Michaelis-Menten-like kinetics for cell culturing}, series = {Physica status solidi A : Applications and materials science}, volume = {211}, journal = {Physica status solidi A : Applications and materials science}, number = {6}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1521-396X (E); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)}, doi = {10.1002/pssa.201330464}, pages = {1410 -- 1415}, year = {2014}, abstract = {The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17-200 mM) follows a Michaelis-Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.}, language = {en} } @article{OberlaenderKirchnerBoyenetal.2014, author = {Oberl{\"a}nder, Jan and Kirchner, Patrick and Boyen, Hans-Gerd and Sch{\"o}ning, Michael Josef}, title = {Detection of hydrogen peroxide vapor by use of manganese(IV) oxide as catalyst for calorimetric gas sensors}, series = {Physica status solidi A: Applications and materials science}, volume = {211}, journal = {Physica status solidi A: Applications and materials science}, number = {6}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1521-396X (E-Journal); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)}, doi = {10.1002/pssa.201330359}, pages = {1372 -- 1376}, year = {2014}, abstract = {In this work, the catalyst manganese(IV) oxide (MnO2), of calorimetric gas sensors (to monitor the sterilization agent vaporized hydrogen peroxide) has been investigated in more detail. Chemical analyses by means of X-ray-induced photoelectron spectroscopy have been performed to unravel the surface chemistry prior and after exposure to hydrogen peroxide vapor at elevated temperature, as applied in the sterilization processes of beverage cartons. The surface characterization reveals a change in oxidation states of the metal oxide catalyst after exposure to hydrogen peroxide. Additionally, a cleaning effect of the catalyst, which itself is attached to the sensor surface by means of a polymer interlayer, could be observed.}, language = {en} } @article{GuoMiyamotoWagneretal.2014, author = {Guo, Yuanyuan and Miyamoto, Ko-ichiro and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo}, title = {Theoretical study and simulation of light-addressable potentiometric sensors}, series = {Physica status solidi (A) : applications and materials}, volume = {211}, journal = {Physica status solidi (A) : applications and materials}, number = {6}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0031-8965}, doi = {10.1002/pssa.201330354}, pages = {1467 -- 1472}, year = {2014}, abstract = {The light-addressable potentiometric sensor (LAPS) is a semiconductor-based potentiometric sensor using a light probe with an ability of detecting the concentration of biochemical species in a spatially resolved manner. As an important biomedical sensor, research has been conducted to improve its performance, for instance, to realize high-speed measurement. In this work, the idea of facilitating the device-level simulation, instead of using an equivalent-circuit model, is presented for detailed analysis and optimization of the performance of the LAPS. Both carrier distribution and photocurrent response have been simulated to provide new insight into both amplitude-mode and phase-mode operations of the LAPS. Various device parameters can be examined to effectively design and optimize the LAPS structures and setups for enhanced performance.}, language = {en} } @phdthesis{Werner2014, author = {Werner, Frederik}, title = {Development of light-addressable potentiometric sensor systems and their applications in biotechnological environments}, pages = {XI, 149 S.}, year = {2014}, language = {en} } @article{MartinezJakobTuetal.2013, author = {Martinez, Ronny and Jakob, Felix and Tu, Ran and Siegert, Petra and Maurer, Karl-Heinz and Schwaneberg, Ulrich}, title = {Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution}, series = {Biotechnology and bioengineering}, volume = {Vol. 110}, journal = {Biotechnology and bioengineering}, number = {Iss. 3}, publisher = {Wiley}, address = {Weinheim}, issn = {1097-0290 (E-Journal); 0006-3592 (Print); 0368-1467 (Print)}, pages = {711 -- 720}, year = {2013}, 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} }