@article{FigueroaMirandaFengShiuetal.2018, author = {Figueroa-Miranda, Gabriela and Feng, Lingyan and Shiu, Simon Chi-Chin and Dirkzwager, Roderick Marshall and Cheung, Yee-Wai and Tanner, Julian Alexander and Sch{\"o}ning, Michael Josef and Offenh{\"a}usser, Andreas and Mayer, Dirk}, title = {Aptamer-based electrochemical biosensor for highly sensitive and selective malaria detection with adjustable dynamic response range and reusability}, series = {Sensor and Actuators B: Chemical}, volume = {255}, journal = {Sensor and Actuators B: Chemical}, number = {P1}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0925-4005}, doi = {10.1016/j.snb.2017.07.117}, pages = {235 -- 243}, year = {2018}, abstract = {Malaria infection remains a significant risk for much of the population of tropical and subtropical areas, particularly in developing countries. Therefore, it is of high importance to develop sensitive, accurate and inexpensive malaria diagnosis tests. Here, we present a novel aptamer-based electrochemical biosensor (aptasensor) for malaria detection by impedance spectroscopy, through the specific recognition between a highly discriminatory DNA aptamer and its target Plasmodium falciparum lactate dehydrogenase (PfLDH). Interestingly, due to the isoelectric point (pI) of PfLDH, the aptasensor response showed an adjustable detection range based on the different protein net-charge at variable pH environments. The specific aptamer recognition allows sensitive protein detection with an expanded detection range and a low detection limit, as well as a high specificity for PfLDH compared to analogous proteins. The specific feasibility of the aptasensor is further demonstrated by detection of the target PfLDH in human serum. Furthermore, the aptasensor can be easily regenerated and thus applied for multiple usages. The robustness, sensitivity, and reusability of the presented aptasensor make it a promising candidate for point-of-care diagnostic systems.}, language = {en} } @article{SchoeningTurekHeidenetal.2009, author = {Sch{\"o}ning, Michael Josef and Turek, M. and Heiden, W. and Riesen, A. and Chhabda, T. A. and Schubert, J. and Kr{\"u}ger, P. and Keusgen, M.}, title = {Artificial intelligence/fuzzy logic method for analysis of combined signals from heavy metal chemical sensors}, series = {Electrochimica Acta. 54 (2009), H. 25 Sp. Iss. SI}, journal = {Electrochimica Acta. 54 (2009), H. 25 Sp. Iss. SI}, publisher = {Elsevier}, address = {New York}, isbn = {0013-4686}, pages = {6082 -- 6088}, year = {2009}, language = {en} } @article{VahidpourGuthmanArreolaetal.2022, author = {Vahidpour, Farnoosh and Guthman, Eric and Arreola, Julia and Alghazali, Yousef H. M. and Wagner, Torsten and Sch{\"o}ning, Michael Josef}, title = {Assessment of Various Process Parameters for Optimized Sterilization Conditions Using a Multi-Sensing Platform}, series = {Foods}, volume = {11}, journal = {Foods}, number = {5}, publisher = {MDPI}, address = {Basel}, issn = {2304-8158}, doi = {10.3390/foods11050660}, pages = {Artikel 660}, year = {2022}, abstract = {In this study, an online multi-sensing platform was engineered to simultaneously evaluate various process parameters of food package sterilization using gaseous hydrogen peroxide (H₂O₂). The platform enabled the validation of critical aseptic parameters. In parallel, one series of microbiological count reduction tests was performed using highly resistant spores of B. atrophaeus DSM 675 to act as the reference method for sterility validation. By means of the multi-sensing platform together with microbiological tests, we examined sterilization process parameters to define the most effective conditions with regards to the highest spore kill rate necessary for aseptic packaging. As these parameters are mutually associated, a correlation between different factors was elaborated. The resulting correlation indicated the need for specific conditions regarding the applied H₂O₂ gas temperature, the gas flow and concentration, the relative humidity and the exposure time. Finally, the novel multi-sensing platform together with the mobile electronic readout setup allowed for the online and on-site monitoring of the sterilization process, selecting the best conditions for sterility and, at the same time, reducing the use of the time-consuming and costly microbiological tests that are currently used in the food package industry.}, language = {en} } @article{SiqueiraBaeckerPoghossianetal.2010, author = {Siqueira, Jos{\´e} R. Jr. and B{\"a}cker, Matthias and Poghossian, Arshak and Zucolotto, Valtencir and Oliveira, Osvaldo N. Jr. and Sch{\"o}ning, Michael Josef}, title = {Associating biosensing properties with the morphological structure of multilayers containing carbon nanotubes on field-effect devices}, series = {Physica status solidi (a). 207 (2010), H. 4}, journal = {Physica status solidi (a). 207 (2010), H. 4}, isbn = {1862-6300}, pages = {781 -- 786}, year = {2010}, 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}, 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{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} } @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} } @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} }