@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} }