@article{PoghossianWagnerSchoening2010, author = {Poghossian, Arshak and Wagner, H. and Sch{\"o}ning, Michael Josef}, title = {Automatisiertes „wafer level"-Testsystem zur Charakterisierung von siliziumbasierten Chemo- und Biosensoren}, series = {Sensoren und Messsysteme 2010 [Elektronische Ressource] : Vortr{\"a}ge der 15. ITG/GMA-Fachtagung vom 18. bis 19. Mai 2010 in N{\"u}rnberg / Informationstechnische Gesellschaft im VDE (ITG); VDI/VDE-Gesellschaft Mess- und Automatisierungstechnik (GMA)}, journal = {Sensoren und Messsysteme 2010 [Elektronische Ressource] : Vortr{\"a}ge der 15. ITG/GMA-Fachtagung vom 18. bis 19. Mai 2010 in N{\"u}rnberg / Informationstechnische Gesellschaft im VDE (ITG); VDI/VDE-Gesellschaft Mess- und Automatisierungstechnik (GMA)}, publisher = {VDE Verlag}, address = {Berlin}, isbn = {978-3-8007-3260-9}, pages = {89 -- 92}, year = {2010}, language = {de} } @article{BuniatyanHuckPoghossianetal.2013, author = {Buniatyan, V. and Huck, Christina and Poghossian, Arshak and Aroutiounian, V. M. and Sch{\"o}ning, Michael Josef}, title = {BaxSr1-x TiO3/pc-Si heterojunction}, series = {Armenian journal of physics}, volume = {6}, journal = {Armenian journal of physics}, number = {4}, publisher = {National Academy of Sciences of Armenia}, address = {Yerevan}, issn = {1829-1171}, pages = {177 -- 187}, year = {2013}, language = {en} } @article{BuniatyanHuckPoghossianetal.2013, author = {Buniatyan, V. and Huck, Christina and Poghossian, Arshak and Aroutiounian, V. M. and Sch{\"o}ning, Michael Josef}, title = {BaxSr1-x TiO3/pc-Si heterojunction capacitance}, series = {Armenian journal of physics}, volume = {6}, journal = {Armenian journal of physics}, number = {4}, publisher = {National Academy of Sciences of Armenia}, address = {Yerevan}, issn = {1829-1171}, pages = {188 -- 197}, year = {2013}, language = {en} } @article{DarmoSchaefferFoersteretal.2000, author = {Darmo, J. and Sch{\"a}ffer, F. and F{\"o}rster, Arnold and Kordos, P.}, title = {Beryllium doped low-temperature-grown MBE GaAs: material for photomixing in the THz frequency range}, series = {ASDAM 2000 : conference proceedings / edited by Jozef Osvald ... [et al.]}, journal = {ASDAM 2000 : conference proceedings / edited by Jozef Osvald ... [et al.]}, publisher = {IEEE}, address = {Piscataway, NJ}, isbn = {0780359399}, pages = {147 -- 150}, year = {2000}, language = {en} } @article{WernerGroebelSchuhmacheretal.2009, author = {Werner, Frederik and Groebel, Simone and Schuhmacher, K. and Spelthahn, Heiko and Wagner, Torsten and Selmer, Thorsten and Baumann, Marcus and Sch{\"o}ning, Michael Josef}, title = {Bestimmung der metabolischen Aktivit{\"a}t von Mikroorganismen w{\"a}hrend des Biogasbildungsprozesses}, 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 = {201 -- 204}, year = {2009}, language = {de} } @article{KramerHalamkovaPoghossianetal.2013, author = {Kramer, Friederike and Halamkova, Lenka and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Katz, Evgeny and Halamek, Jan}, title = {Biocatalytic analysis of biomarkers for forensic identification of ethnicity between Caucasian and African American}, series = {The analyst. August 2013}, volume = {Vol. 138}, journal = {The analyst. August 2013}, publisher = {Royal Society of Chemistry}, address = {Cambridge}, issn = {1364-5528 (E-Journal); 0003-2654 (Print)}, pages = {6251 -- 6257}, year = {2013}, language = {en} } @article{FalkenbergKohnBottetal.2023, author = {Falkenberg, Fabian and Kohn, Sophie and Bott, Michael and Bongaerts, Johannes and Siegert, Petra}, title = {Biochemical characterisation of a novel broad pH spectrum subtilisin from Fictibacillus arsenicus DSM 15822ᵀ}, series = {FEBS Open Bio}, volume = {13}, journal = {FEBS Open Bio}, number = {11}, publisher = {Wiley}, address = {Hoboken, NJ}, issn = {2211-5463}, doi = {10.1002/2211-5463.13701}, pages = {2035 -- 2046}, year = {2023}, abstract = {Subtilisins from microbial sources, especially from the Bacillaceae family, are of particular interest for biotechnological applications and serve the currently growing enzyme market as efficient and novel biocatalysts. Biotechnological applications include use in detergents, cosmetics, leather processing, wastewater treatment and pharmaceuticals. To identify a possible candidate for the enzyme market, here we cloned the gene of the subtilisin SPFA from Fictibacillus arsenicus DSM 15822ᵀ (obtained through a data mining-based search) and expressed it in Bacillus subtilis DB104. After production and purification, the protease showed a molecular mass of 27.57 kDa and a pI of 5.8. SPFA displayed hydrolytic activity at a temperature optimum of 80 °C and a very broad pH optimum between 8.5 and 11.5, with high activity up to pH 12.5. SPFA displayed no NaCl dependence but a high NaCl tolerance, with decreasing activity up to concentrations of 5 m NaCl. The stability enhanced with increasing NaCl concentration. Based on its substrate preference for 10 synthetic peptide 4-nitroanilide substrates with three or four amino acids and its phylogenetic classification, SPFA can be assigned to the subgroup of true subtilisins. Moreover, SPFA exhibited high tolerance to 5\% (w/v) SDS and 5\% H₂O₂ (v/v). The biochemical properties of SPFA, especially its tolerance of remarkably high pH, SDS and H₂O₂, suggest it has potential for biotechnological applications.}, language = {en} } @article{FalkenbergRahbaFischeretal.2022, author = {Falkenberg, Fabian and Rahba, Jade and Fischer, David and Bott, Michael and Bongaerts, Johannes and Siegert, Petra}, title = {Biochemical characterization of a novel oxidatively stable, halotolerant, and high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T}, series = {FEBS Open Bio}, volume = {12}, journal = {FEBS Open Bio}, number = {10}, publisher = {Wiley}, address = {Hoboken, NJ}, issn = {2211-5463}, doi = {10.1002/2211-5463.13457}, pages = {1729 -- 1746}, year = {2022}, abstract = {Halophilic and halotolerant microorganisms represent a promising source of salt-tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T. The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high-alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0-12.0 and temperature 20-80 °C, optimally at pH 9.0-9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58\% of residual activity when incubated at 10 °C with 5\% (v/v) H2O2 for 1 h while stimulated at 1\% (v/v) H2O2. Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m. This study demonstrates the potential of SPAO for biotechnological applications in the future.}, language = {en} } @article{LuethThustSteffenetal.2000, author = {L{\"u}th, H. and Thust, M. and Steffen, A. and Kordos, P. and Sch{\"o}ning, Michael Josef}, title = {Biochemical sensors with structured and porous silicon capacitors}, series = {Materials Science and Engineering B. 69-70 (2000)}, journal = {Materials Science and Engineering B. 69-70 (2000)}, isbn = {0921-5107}, pages = {104 -- 108}, year = {2000}, language = {en} } @article{SchrothWeissbeckerSchuetzetal.2002, author = {Schroth, P. and Weißbecker, B. and Sch{\"u}tz, S. and Ecken, H. and Yoshinobu, T. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef}, title = {Bioelectronic signal processing - intact chemoreceptors coupled to field-effect devices}, series = {Lecture Notes of the ICB Seminars}, journal = {Lecture Notes of the ICB Seminars}, publisher = {MCB}, address = {Warsaw}, pages = {28 -- 42}, year = {2002}, language = {en} } @article{SchrothWeissbeckerSchuetzetal.2001, author = {Schroth, P. and Weißbecker, B. and Sch{\"u}tz, S. and Ecken, H. and Yoshinobu, T. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef}, title = {Bioelectronic signal processing - intact chemoreceptors coupled to field-effect devices}, series = {Biocybernetics and Biomedical Engineering. 21 (2001), H. 3}, journal = {Biocybernetics and Biomedical Engineering. 21 (2001), H. 3}, isbn = {0208-5216}, pages = {27 -- 42}, year = {2001}, language = {en} } @article{SchoeningPoghossian2006, author = {Sch{\"o}ning, Michael Josef and Poghossian, Arshak}, title = {BioFEDs (field-effect devices) : State-of-the-art and new directions}, series = {Electroanalysis}, volume = {18}, journal = {Electroanalysis}, number = {19-20}, issn = {1521-4109}, doi = {10.1002/elan.200603609}, pages = {1893 -- 1900}, year = {2006}, language = {en} } @inproceedings{KasperSchiffelsKrafftetal.2016, author = {Kasper, Katharina and Schiffels, Johannes and Krafft, Simone and Kuperjans, Isabel and Elbers, Gereon and Selmer, Thorsten}, title = {Biogas Production on Demand Regulated by Butyric Acid Addition}, series = {IOP Conference Series: Earth and Environmental Science. Bd. 32}, volume = {32}, booktitle = {IOP Conference Series: Earth and Environmental Science. Bd. 32}, issn = {1755-1315}, doi = {10.1088/1755-1315/32/1/012009}, pages = {012009/1 -- 012009/4}, year = {2016}, language = {en} } @article{OliveiraMolinnusBegingetal.2021, author = {Oliveira, Danilo A. and Molinnus, Denise and Beging, Stefan and Siqueira Jr, Jos{\´e} R. and Sch{\"o}ning, Michael Josef}, title = {Biosensor Based on Self-Assembled Films of Graphene Oxide and Polyaniline Using a Field-Effect Device Platform}, series = {physica status solidi (a) applications and materials science}, volume = {218}, journal = {physica status solidi (a) applications and materials science}, number = {13}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.202000747}, pages = {1 -- 9}, year = {2021}, abstract = {A new functionalization method to modify capacitive electrolyte-insulator-semiconductor (EIS) structures with nanofilms is presented. Layers of polyallylamine hydrochloride (PAH) and graphene oxide (GO) with the compound polyaniline:poly(2-acrylamido-2-methyl-1-propanesulfonic acid) (PANI:PAAMPSA) are deposited onto a p-Si/SiO2 chip using the layer-by-layer technique (LbL). Two different enzymes (urease and penicillinase) are separately immobilized on top of a five-bilayer stack of the PAH:GO/PANI:PAAMPSA-modified EIS chip, forming a biosensor for detection of urea and penicillin, respectively. Electrochemical characterization is performed by constant capacitance (ConCap) measurements, and the film morphology is characterized by atomic force microscopy (AFM) and scanning electron microscopy (SEM). An increase in the average sensitivity of the modified biosensors (EIS-nanofilm-enzyme) of around 15\% is found in relation to sensors, only carrying the enzyme but without the nanofilm (EIS-enzyme). In this sense, the nanofilm acts as a stable bioreceptor onto the EIS chip improving the output signal in terms of sensitivity and stability.}, language = {en} } @article{KeusgenJuengerKrestetal.2003, author = {Keusgen, Michael and J{\"u}nger, Martina and Krest, Ingo and Sch{\"o}ning, Michael Josef}, title = {Biosensoric detection of the cysteine sulphoxide alliin}, series = {Sensors and Actuators B. 95 (2003), H. 1-3}, journal = {Sensors and Actuators B. 95 (2003), H. 1-3}, isbn = {0925-4005}, pages = {297 -- 302}, year = {2003}, language = {en} } @article{KeusgenJuengerSchoening2002, author = {Keusgen, M. and J{\"u}nger, M. and Sch{\"o}ning, Michael Josef}, title = {Biosensoric detection of the cysteine sulphoxide alliin}, series = {Book of abstracts / ed. by J. Saneistr.}, journal = {Book of abstracts / ed. by J. Saneistr.}, publisher = {Czech Technical University, Faculty of Electrical Engineering, Department of Measurement}, address = {Prague}, isbn = {80-01-02576-4}, pages = {1175 -- 1178}, year = {2002}, language = {en} } @article{PaczkowskiWeissbeckerSchoeningetal.2011, author = {Paczkowski, Sebastian and Weißbecker, Bernhard and Sch{\"o}ning, Michael Josef and Sch{\"u}tz, Stefan}, title = {Biosensors on the Basis of Insect Olfaction}, series = {Insect biotechnology / Andreas Vilcinskas, ed.}, journal = {Insect biotechnology / Andreas Vilcinskas, ed.}, publisher = {Springer}, address = {Dordrecht [u.a.]}, isbn = {978-90-481-9640-1}, pages = {225 -- 240}, year = {2011}, 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} } @incollection{KirchnerReisertSchoening2014, author = {Kirchner, Patrick and Reisert, Steffen and Sch{\"o}ning, Michael Josef}, title = {Calorimetric gas sensors for hydrogen peroxide monitoring in aseptic food processes}, series = {Gas sensing fundamentals. (Springer Series on Chemical Sensors and Biosensors ; 15)}, booktitle = {Gas sensing fundamentals. (Springer Series on Chemical Sensors and Biosensors ; 15)}, publisher = {Springer}, address = {Heidelberg}, isbn = {978-3-642-54518-4 (Print) ; 978-3-642-54519-1 (Online)}, doi = {10.1007/5346_2013_51}, pages = {279 -- 309}, year = {2014}, abstract = {For the sterilisation of aseptic food packages it is taken advantage of the microbicidal properties of hydrogen peroxide (H2O2). Especially, when applied in vapour phase, it has shown high potential of microbial inactivation. In addition, it offers a high environmental compatibility compared to other chemical sterilisation agents, as it decomposes into oxygen and water, respectively. Due to a lack in sensory detection possibilities, a continuous monitoring of the H2O2 concentration was recently not available. Instead, the sterilisation efficacy is validated using microbiological tests. However, progresses in the development of calorimetric gas sensors during the last 7 years have made it possible to monitor the H2O2 concentration during operation. This chapter deals with the fundamentals of calorimetric gas sensing with special focus on the detection of gaseous hydrogen peroxide. A sensor principle based on a calorimetric differential set-up is described. Special emphasis is given to the sensor design with respect to the operational requirements under field conditions. The state-of-the-art regarding a sensor set-up for the on-line monitoring and secondly, a miniaturised sensor for in-line monitoring are summarised. Furthermore, alternative detection methods and a novel multi-sensor system for the characterisation of aseptic sterilisation processes are described.}, language = {en} } @article{SchoeningMourzinaSchubertetal.2001, author = {Sch{\"o}ning, Michael Josef and Mourzina, Y. G. and Schubert, J. and Zander, W. and Legin, A. and Vlasov, Y. G. and L{\"u}th, H.}, title = {Can pulsed laser deposition serve as an advanced technique in fabricating chemical sensors?}, series = {Sensors and Actuators B. 78 (2001), H. 1-3}, journal = {Sensors and Actuators B. 78 (2001), H. 1-3}, isbn = {0925-4005}, pages = {273 -- 278}, year = {2001}, language = {en} }