@article{SiqueiraAbouzarPoghossianetal.2009, author = {Siqueira, Jos{\´e} R. Jr. and Abouzar, Maryam H. and Poghossian, Arshak and Zucolotto, Valtencir and Oliveira, Osvaldo N. Jr. and Sch{\"o}ning, Michael Josef}, title = {Penicillin biosensor based on a capacitive field-effect structure functionalized with a dendrimer/carbon nanotube multilayer}, series = {Biosensors and Bioelectronics. 25 (2009), H. 2}, journal = {Biosensors and Bioelectronics. 25 (2009), H. 2}, isbn = {0956-5663}, pages = {497 -- 501}, year = {2009}, language = {en} } @article{SchmittFassbenderLuethetal.2000, author = {Schmitt, G. and Faßbender, F. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef and Schultze, J. W. and Buß, G.}, title = {Passivation and corrosion of microelectrode arrays}, series = {Materials and Corrosion. 51 (2000), H. 1}, journal = {Materials and Corrosion. 51 (2000), H. 1}, isbn = {0947-5117}, pages = {20 -- 25}, year = {2000}, language = {en} } @article{GunRizkovLevetal.2008, author = {Gun, Jenny and Rizkov, Dan and Lev, Ovadia and Abouzar, Maryam H. and Poghossian, Arshak and Sch{\"o}ning, Michael Josef}, title = {Oxygen plasma-treated gold nanoparticle-based field-effect devices as transducer structures for bio-chemical sensing}, series = {Microchimica Acta. 164 (2008), H. 3-4}, journal = {Microchimica Acta. 164 (2008), H. 3-4}, isbn = {1436-5073}, pages = {395 -- 404}, year = {2008}, language = {en} } @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} }