TY - JOUR A1 - Siqueira, José R. Jr. A1 - Abouzar, Maryam H. A1 - Poghossian, Arshak A1 - Zucolotto, Valtencir A1 - Oliveira, Osvaldo N. Jr. A1 - Schöning, Michael Josef T1 - Penicillin biosensor based on a capacitive field-effect structure functionalized with a dendrimer/carbon nanotube multilayer JF - Biosensors and Bioelectronics. 25 (2009), H. 2 Y1 - 2009 SN - 0956-5663 SP - 497 EP - 501 ER - TY - JOUR A1 - Schmitt, G. A1 - Faßbender, F. A1 - Lüth, H. A1 - Schöning, Michael Josef A1 - Schultze, J. W. A1 - Buß, G. T1 - Passivation and corrosion of microelectrode arrays JF - Materials and Corrosion. 51 (2000), H. 1 Y1 - 2000 SN - 0947-5117 SP - 20 EP - 25 ER - TY - JOUR A1 - Gun, Jenny A1 - Rizkov, Dan A1 - Lev, Ovadia A1 - Abouzar, Maryam H. A1 - Poghossian, Arshak A1 - Schöning, Michael Josef T1 - Oxygen plasma-treated gold nanoparticle-based field-effect devices as transducer structures for bio-chemical sensing JF - Microchimica Acta. 164 (2008), H. 3-4 Y1 - 2008 SN - 1436-5073 SP - 395 EP - 404 ER - TY - JOUR A1 - Pita, Marcos A1 - Krämer, Melina A1 - Zouh, Jian A1 - Poghossian, Arshak A1 - Schöning, Michael Josef A1 - Fernandez, Victor M. A1 - Katz, Evgeny T1 - Optoelectronic Properties of Nanostructured Ensembles Controlled by Biomolecular Logic Systems JF - ACS Nano. 10 (2008), H. 2 Y1 - 2008 SN - 1936-086X SP - 2160 EP - 2166 ER - TY - JOUR A1 - Arreola, Julio A1 - Mätzkow, Malte A1 - Durán, Marlena Palomar A1 - Greeff, Anton A1 - Keusgen, Michael A1 - Schöning, Michael Josef T1 - Optimization of the immobilization of bacterial spores on glass substrates with organosilanes JF - Physica status solidi (A) : Applications and materials science N2 - 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. KW - silanization KW - organosilanes KW - immobilization KW - endospores KW - biosensors KW - Bacillus atrophaeus Y1 - 2016 U6 - http://dx.doi.org/10.1002/pssa.201532914 SN - 1862-6319 VL - 213 IS - 6 SP - 1463 EP - 1470 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Degering, Christian A1 - Eggert, Thorsten A1 - Puls, Michael A1 - Bongaerts, Johannes A1 - Evers, Stefan A1 - Maurer, Karl-Heinz A1 - Jaeger, Karl-Erich T1 - Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides JF - Applied and environmental microbiology N2 - 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. Y1 - 2010 U6 - http://dx.doi.org/10.1128/AEM.01146-10 SN - 1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print) VL - 76 IS - 19 SP - 6370 EP - 6378 PB - American Society for Microbiology CY - Washington, DC ER - TY - JOUR A1 - Faßbender, F. A1 - Schmitt, G. A1 - Schöning, Michael Josef A1 - Lüth, H. A1 - Buß, G. A1 - Schultze, J. W. T1 - Optimization of passivation layers for corrosion protection of silicon-based microelectrode arrays JF - Sensors and Actuators B. 68 (2000), H. 1-3 Y1 - 2000 SN - 0925-4005 SP - 128 EP - 133 ER - TY - JOUR A1 - Dantism, Shahriar A1 - Röhlen, Desiree A1 - Wagner, Torsten A1 - Wagner, Patrick A1 - Schöning, Michael Josef T1 - Optimization of Cell-Based Multi-Chamber LAPS Measurements Utilizing FPGA-Controlled Laser-Diode Modules JF - physica status solidi a : applications and materials sciences N2 - 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. Y1 - 2018 U6 - http://dx.doi.org/10.1002/pssa.201800058 SN - 1862-6319 VL - 215 IS - 15 SP - Article number 1800058 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Pilas, Johanna A1 - Mariano, K. A1 - Keusgen, M. A1 - Selmer, Thorsten A1 - Schöning, Michael Josef T1 - Optimization of an Enzyme-based Multi-parameter Biosensor for Monitoring Biogas Processes JF - Procedia Engineering Y1 - 2015 U6 - http://dx.doi.org/10.1016/j.proeng.2015.08.702 SN - 1877-7058 N1 - Part of special issue "Eurosensors 2015" VL - 120 SP - 532 EP - 535 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Pilas, Johanna A1 - Yazici, Yasemen A1 - Selmer, Thorsten A1 - Keusgen, Michael A1 - Schöning, Michael Josef T1 - Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate JF - Electrochimica Acta N2 - 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. KW - Simultaneous determination KW - Enzymatic biosensor KW - Diaphorase KW - Dehydrogenase Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.electacta.2017.07.119 SN - 0013-4686 VL - 251 SP - 256 EP - 262 PB - Elsevier CY - Amsterdam ER -