@article{PitaKraemerZouhetal.2008,
  author    = {Pita, Marcos and Kr{\"a}mer, Melina and Zouh, Jian and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Fernandez, Victor M. and Katz, Evgeny},
  title     = {Optoelectronic Properties of Nanostructured Ensembles Controlled by Biomolecular Logic Systems},
  series = {ACS Nano. 10 (2008), H. 2},
  journal   = {ACS Nano. 10 (2008), H. 2},
  isbn      = {1936-086X},
  pages     = {2160 -- 2166},
  year      = {2008},
  language  = {en}
}
@article{ArreolaMaetzkowDuranetal.2016,
  author    = {Arreola, Julio and M{\"a}tzkow, Malte and Dur{\´a}n, Marlena Palomar and Greeff, Anton and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of the immobilization of bacterial spores on glass substrates with organosilanes},
  series = {Physica status solidi (A) : Applications and materials science},
  volume    = {213},
  journal   = {Physica status solidi (A) : Applications and materials science},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201532914},
  pages     = {1463 -- 1470},
  year      = {2016},
  abstract  = {Spores can be immobilized on biosensors to function as sensitive recognition elements. However, the immobilization can affect the sensitivity and reproducibility of the sensor signal. In this work, three different immobilization strategies with organosilanes were optimized and characterized to immobilize Bacillus atrophaeus spores on glass substrates. Five different silanization parameters were investigated: nature of the solvent, concentration of the silane, silanization time, curing process, and silanization temperature. The resulting silane layers were resistant to a buffer solution (e.g., Ringer solution) with a polysorbate (e.g., Tween®80) and sonication.},
  language  = {en}
}
@article{DegeringEggertPulsetal.2010,
  author    = {Degering, Christian and Eggert, Thorsten and Puls, Michael and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Jaeger, Karl-Erich},
  title     = {Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides},
  series = {Applied and environmental microbiology},
  volume    = {76},
  journal   = {Applied and environmental microbiology},
  number    = {19},
  publisher = {American Society for Microbiology},
  address   = {Washington, DC},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  doi       = {10.1128/AEM.01146-10},
  pages     = {6370 -- 6378},
  year      = {2010},
  abstract  = {Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.},
  language  = {en}
}
@article{FassbenderSchmittSchoeningetal.2000,
  author    = {Faßbender, F. and Schmitt, G. and Sch{\"o}ning, Michael Josef and L{\"u}th, H. and Buß, G. and Schultze, J. W.},
  title     = {Optimization of passivation layers for corrosion protection of silicon-based microelectrode arrays},
  series = {Sensors and Actuators B. 68 (2000), H. 1-3},
  journal   = {Sensors and Actuators B. 68 (2000), H. 1-3},
  isbn      = {0925-4005},
  pages     = {128 -- 133},
  year      = {2000},
  language  = {en}
}
@article{DantismRoehlenWagneretal.2018,
  author    = {Dantism, Shahriar and R{\"o}hlen, Desiree and Wagner, Torsten and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of Cell-Based Multi-Chamber LAPS Measurements Utilizing FPGA-Controlled Laser-Diode Modules},
  series = {physica status solidi a : applications and materials sciences},
  volume    = {215},
  journal   = {physica status solidi a : applications and materials sciences},
  number    = {15},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201800058},
  pages     = {Article number 1800058},
  year      = {2018},
  abstract  = {A light-addressable potentiometric sensor (LAPS) is a field-effect-based potentiometric device, which detects concentration changes of an analyte solution on the sensor surface in a spatially resolved way. It uses a light source to generate electron-hole pairs inside the semiconductor, which are separated in the depletion region due to an applied bias voltage across the sensor structure and hence, a surface-potential-dependent photocurrent can be read out. However, depending on the beam angle of the light source, scattering effects can occur, which influence the recorded signal in LAPS-based differential measurements. To solve this problem, a novel illumination unit based on a field programmable gate array (FPGA) consisting of 16 small-sized tunable infrared laser-diode modules (LDMs) is developed. Due to the improved focus of the LDMs with a beam angle of only 2 mrad, undesirable scattering effects are minimized. Escherichia coli (E. coli) K12 bacteria are used as a test microorganism to study the extracellular acidification on the sensor surface. Furthermore, a salt bridge chamber is built up and integrated with the LAPS system enabling multi-chamber differential measurements with a single Ag/AgCl reference electrode.},
  language  = {en}
}
@article{PilasMarianoKeusgenetal.2015,
  author    = {Pilas, Johanna and Mariano, K. and Keusgen, M. and Selmer, Thorsten and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of an Enzyme-based Multi-parameter Biosensor for Monitoring Biogas Processes},
  series = {Procedia Engineering},
  volume    = {120},
  journal   = {Procedia Engineering},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1877-7058},
  doi       = {10.1016/j.proeng.2015.08.702},
  pages     = {532 -- 535},
  year      = {2015},
  language  = {en}
}
@article{PilasYaziciSelmeretal.2017,
  author    = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate},
  series = {Electrochimica Acta},
  volume    = {251},
  journal   = {Electrochimica Acta},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2017.07.119},
  pages     = {256 -- 262},
  year      = {2017},
  abstract  = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.},
  language  = {en}
}
@article{KirchnerOberlaenderFriedrichetal.2011,
  author    = {Kirchner, Patrick and Oberl{\"a}nder, Jan and Friedrich, Peter and Berger, J{\"o}rg and Suso, Henri-Pierre and Kupyna, Andriy and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Optimisation and fabrication of a calorimetric gas sensor built up on a polyimide substrate for H2O2 monitoring},
  series = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  journal   = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1862-6319},
  pages     = {1235 -- 1240},
  year      = {2011},
  language  = {en}
}
@article{WagnerBegingRotteretal.2007,
  author    = {Wagner, Torsten and Beging, Stefan and Rotter, L. and Poghossian, Arshak and Biselli, Manfred and Zang, Werner and Sch{\"o}ning, Michael Josef},
  title     = {Online-Messsysteme f{\"u}r die automatisierte Charakterisierung von feldeffektbasierten Biosensoren},
  series = {8. Dresdner Sensor-Symposium : Sensoren f{\"u}r Umwelt, Klima und Sicherheit, Biosensoren und Biosysteme, Sensoren und Sensorsysteme f{\"u}r die Prozesstechnik, Trends in der Sensortechnik, Materialentwicklung f{\"u}r die Sensorik; 8. Dresdner Sensor-Symposium, 10. - 12. Dezember 2007, Dresden / Gerald Gerlach ... (Hg.)},
  journal   = {8. Dresdner Sensor-Symposium : Sensoren f{\"u}r Umwelt, Klima und Sicherheit, Biosensoren und Biosysteme, Sensoren und Sensorsysteme f{\"u}r die Prozesstechnik, Trends in der Sensortechnik, Materialentwicklung f{\"u}r die Sensorik; 8. Dresdner Sensor-Symposium, 10. - 12. Dezember 2007, Dresden / Gerald Gerlach ... (Hg.)},
  publisher = {TUDpress, Verl. der Wissenschaften},
  address   = {Dresden},
  isbn      = {978-3-940046-45-1},
  pages     = {257 -- 260},
  year      = {2007},
  language  = {de}
}
@article{ZatkoDubeckyBohaceketal.2004,
  author    = {Zatko, B. and Dubeck{\´y}, F. and Bohacek, P. and Gombia, E. and Frigeri, P. and Mosca, R. and Franchi, S. and Huarn, J. and Nescas, V. and Sekacova, M. and F{\"o}rster, Arnold and Kordos, P.},
  title     = {On the spectrometric performance limit of radiation detectors based on semi-insulating GaAs},
  series = {Nuclear instruments and methods in physics research, Section A. 531 (2004), H. 1-2},
  journal   = {Nuclear instruments and methods in physics research, Section A. 531 (2004), H. 1-2},
  isbn      = {0168-9002},
  pages     = {111 -- 120},
  year      = {2004},
  language  = {en}
}
@article{WernerGroebelKrumbeetal.2012,
  author    = {Werner, Frederik and Groebel, Simone and Krumbe, Christoph and Wagner, Torsten and Selmer, Thorsten and Yoshinobu, Tatsuo and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Nutrient concentration-sensitive microorganism-based biosensor},
  series = {Physica Status Solidi (a)},
  volume    = {209},
  journal   = {Physica Status Solidi (a)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201100801},
  pages     = {900 -- 904},
  year      = {2012},
  language  = {en}
}
@article{IkenKirsanovLeginetal.2012,
  author    = {Iken, Heiko and Kirsanov, D. and Legin, A. and Sch{\"o}ning, Michael Josef},
  title     = {Novel Thin-Film Polymeric Materials for the Detection of Heavy Metals},
  series = {Procedia Engineering},
  journal   = {Procedia Engineering},
  number    = {47},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1877-7058},
  doi       = {10.1016/j.proeng.2012.09.148},
  pages     = {322 -- 325},
  year      = {2012},
  abstract  = {A variety of transition metals, e.g., copper, zinc, cadmium, lead, etc. are widely used in industry as components for wires, coatings, alloys, batteries, paints and so on. The inevitable presence of transition metals in industrial processes implies the ambition of developing a proper analytical technique for their adequate monitoring. Most of these elements, especially lead and cadmium, are acutely toxic for biological organisms. Quantitative determination of these metals at low activity levels in different environmental and industrial samples is therefore a vital task. A promising approach to achieve an at-side or on-line monitoring on a miniaturized and cost efficient way is the combination of a common potentiometric sensor array with heavy metal-sensitive thin-film materials, like chalcogenide glasses and polymeric materials, respectively.},
  language  = {en}
}
@article{HaegerJolmesOyenetal.2024,
  author    = {Haeger, Gerrit and Jolmes, Tristan and Oyen, Sven and Jaeger, Karl-Erich and Bongaerts, Johannes and Sch{\"o}rken, Ulrich and Siegert, Petra},
  title     = {Novel recombinant aminoacylase from Paraburkholderia monticola capable of N-acyl-amino acid synthesis},
  series = {Applied Microbiology and Biotechnology},
  journal   = {Applied Microbiology and Biotechnology},
  number    = {108},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614},
  doi       = {10.1007/s00253-023-12868-8},
  pages     = {14 Seiten},
  year      = {2024},
  abstract  = {N-Acyl-amino acids can act as mild biobased surfactants, which are used, e.g., in baby shampoos. However, their chemical synthesis needs acyl chlorides and does not meet sustainability criteria. Thus, the identification of biocatalysts to develop greener synthesis routes is desirable. We describe a novel aminoacylase from Paraburkholderia monticola DSM 100849 (PmAcy) which was identified, cloned, and evaluated for its N-acyl-amino acid synthesis potential. Soluble protein was obtained by expression in lactose autoinduction medium and co-expression of molecular chaperones GroEL/S. Strep-tag affinity purification enriched the enzyme 16-fold and yielded 15 mg pure enzyme from 100 mL of culture. Biochemical characterization revealed that PmAcy possesses beneficial traits for industrial application like high temperature and pH-stability. A heat activation of PmAcy was observed upon incubation at temperatures up to 80 °C. Hydrolytic activity of PmAcy was detected with several N-acyl-amino acids as substrates and exhibited the highest conversion rate of 773 U/mg with N-lauroyl-L-alanine at 75 °C. The enzyme preferred long-chain acyl-amino-acids and displayed hardly any activity with acetyl-amino acids. PmAcy was also capable of N-acyl-amino acid synthesis with good conversion rates. The best synthesis results were obtained with the cationic L-amino acids L-arginine and L-lysine as well as with L-leucine and L-phenylalanine. Exemplarily, L-phenylalanine was acylated with fatty acids of chain lengths from C8 to C18 with conversion rates of up to 75\%. N-lauroyl-L-phenylalanine was purified by precipitation, and the structure of the reaction product was verified by LC-MS and NMR.},
  language  = {en}
}
@article{GuoSekiMiyamotoetal.2014,
  author    = {Guo, Yuanyuan and Seki, Kosuke and Miyamoto, Ko-ichiro and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo},
  title     = {Novel photoexcitation method for light-addressable potentiometric sensor with higher spatial resolution},
  series = {Applied physics express : APEX},
  volume    = {7},
  journal   = {Applied physics express : APEX},
  number    = {6},
  publisher = {IOP},
  address   = {Bristol},
  issn      = {1882-0786 (E-Journa); 1882-0778 (Print)},
  doi       = {10.7567/APEX.7.067301},
  pages     = {067301-4},
  year      = {2014},
  abstract  = {A novel photoexcitation method for the light-addressable potentiometric sensor (LAPS) is proposed to achieve a higher spatial resolution of chemical images. The proposed method employs a combined light source that consists of a modulated light probe, which generates the alternating photocurrent signal, and a ring of constant illumination surrounding it. The constant illumination generates a sheath of carriers with increased concentration which suppresses the spread of photocarriers by enhanced recombination. A device simulation was carried out to verify the effect of constant illumination on the spatial resolution, which demonstrated that a higher spatial resolution can be obtained.},
  language  = {en}
}
@article{SchoeningMalkocThustetal.2000,
  author    = {Sch{\"o}ning, Michael Josef and Malkoc, {\"U}. and Thust, M. and Steffen, A. and Kordos, P. and L{\"u}th, H.},
  title     = {Novel electrochemical sensors with structured and porous semiconductor/insulator capacitors},
  series = {Sensors and Actuators B. 65 (2000), H. 1-3},
  journal   = {Sensors and Actuators B. 65 (2000), H. 1-3},
  isbn      = {0925-4005},
  pages     = {288 -- 290},
  year      = {2000},
  language  = {en}
}
@article{SchoeningLueth2001,
  author    = {Sch{\"o}ning, Michael Josef and L{\"u}th, H.},
  title     = {Novel concepts for silicon-based biosensors},
  series = {Physica Status Solidi (A) (2001)},
  journal   = {Physica Status Solidi (A) (2001)},
  isbn      = {0031-8965},
  pages     = {65 -- 77},
  year      = {2001},
  language  = {en}
}
@article{PoghossianBerndsenLuethetal.2001,
  author    = {Poghossian, Arshak and Berndsen, Lars and L{\"u}th, Hans and Sch{\"o}ning, Michael Josef},
  title     = {Novel concepts for flow-rate and flow-direction determination by means of pH-sensitive ISFETs},
  series = {Proceedings of SPIE. 4560 (2001)},
  journal   = {Proceedings of SPIE. 4560 (2001)},
  pages     = {19 -- 27},
  year      = {2001},
  language  = {en}
}
@article{WagnerMiyamotoSchoeningetal.2010,
  author    = {Wagner, Torsten and Miyamoto, Ko-ichiro and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo},
  title     = {Novel combination of digital light processing (DLP) and light-addressable potentiometric sensors (LAPS) for flexible chemical imaging},
  series = {Procedia Engineering. 5 (2010)},
  journal   = {Procedia Engineering. 5 (2010)},
  isbn      = {1877-7058},
  pages     = {520 -- 523},
  year      = {2010},
  language  = {en}
}
@article{HaegerProbstJaegeretal.2023,
  author    = {Haeger, Gerrit and Probst, Johanna and Jaeger, Karl-Erich and Bongaerts, Johannes and Siegert, Petra},
  title     = {Novel aminoacylases from Streptomyces griseus DSM 40236 and their recombinant production in Streptomyces lividans},
  series = {FEBS Open Bio},
  volume    = {13},
  journal   = {FEBS Open Bio},
  number    = {12},
  publisher = {Wiley},
  address   = {Hoboken, NJ},
  issn      = {2211-5463},
  doi       = {10.1002/2211-5463.13723},
  pages     = {2224 -- 2238},
  year      = {2023},
  abstract  = {Amino acid-based surfactants are valuable compounds for cosmetic formulations. The chemical synthesis of acyl-amino acids is conventionally performed by the Schotten-Baumann reaction using fatty acyl chlorides, but aminoacylases have also been investigated for use in biocatalytic synthesis with free fatty acids. Aminoacylases and their properties are diverse; they belong to different peptidase families and show differences in substrate specificity and biocatalytic potential. Bacterial aminoacylases capable of synthesis have been isolated from Burkholderia, Mycolicibacterium, and Streptomyces. Although several proteases and peptidases from S. griseus have been described, no aminoacylases from this species have been identified yet. In this study, we investigated two novel enzymes produced by S. griseus DSM 40236ᵀ . We identified and cloned the respective genes and recombinantly expressed an α-aminoacylase (EC 3.5.1.14), designated SgAA, and an ε-lysine acylase (EC 3.5.1.17), designated SgELA, in S. lividans TK23. The purified aminoacylase SgAA was biochemically characterized, focusing on its hydrolytic activity to determine temperature- and pH optima and stabilities. The aminoacylase could hydrolyze various acetyl-amino acids at the Nα -position with a broad specificity regarding the sidechain. Substrates with longer acyl chains, like lauroyl-amino acids, were hydrolyzed to a lesser extent. Purified aminoacylase SgELA specific for the hydrolysis of Nε -acetyl-L-lysine was unstable and lost its enzymatic activity upon storage for a longer period but could initially be characterized. The pH optimum of SgELA was pH 8.0. While synthesis of acyl-amino acids was not observed with SgELA, SgAA catalyzed the synthesis of lauroyl-methionine.},
  language  = {en}
}
@article{KarschuckFilipovBollellaetal.2019,
  author    = {Karschuck, T. L. and Filipov, Y. and Bollella, P. and Sch{\"o}ning, Michael Josef and Katz, E.},
  title     = {Not-XOR (NXOR) logic gate based on an enzyme-catalyzed reaction},
  series = {International Journal of Unconventional Computing},
  volume    = {14},
  journal   = {International Journal of Unconventional Computing},
  number    = {3-4},
  publisher = {Old City Publishing},
  address   = {Philadelphia},
  issn      = {1548-7199},
  pages     = {235 -- 242},
  year      = {2019},
  abstract  = {Enzyme-catalyzed reactions have been designed to mimic various Boolean logic gates in the general framework of unconventional biomolecular computing. While some of the logic gates, particularly OR, AND, are easy to realize with biocatalytic reactions and have been reported in numerous publications, some other, like NXOR, are very challenging and have not been realized yet with enzyme reactions. The paper reports on a novel approach to mimicking the NXOR logic gate using the bell-shaped enzyme activity dependent on pH values. Shifting pH from the optimum value to the acidic or basic values by using acid or base inputs (meaning 1,0 and 0,1 inputs) inhibits the enzyme reaction, while keeping the optimum pH (assuming 0,0 and 1,1 input combinations) preserves a high enzyme activity. The challenging part of the present approach is the selection of an enzyme with a well-demonstrated bell-shape activity dependence on the pH value. While many enzymes can satisfy this condition, we selected pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenase as this enzyme has the optimum pH center-located on the pH scale allowing the enzyme activity change by the acidic and basic pH shift from the optimum value corresponding to the highest activity. The present NXOR gate is added to the biomolecular "toolbox" as a new example of Boolean logic gates based on enzyme reactions.},
  language  = {en}
}