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 - https://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 - Vahidpour, Farnoosh A1 - Oberländer, Jan A1 - Schöning, Michael Josef T1 - Flexible Calorimetric Gas Sensors for Detection of a Broad Concentration Range of Gaseous Hydrogen Peroxide: A Step Forward to Online Monitoring of Food-Package Sterilization Processes JF - Phys. Status Solidi A N2 - In this study, flexible calorimetric gas sensors are developed for specificdetection of gaseous hydrogen peroxide (H₂O₂) over a wide concentrationrange, which is used in sterilization processes for aseptic packaging industry.The flexibility of these sensors is an advantage for identifying the chemical components of the sterilant on the corners of the food boxes, so-called “coldspots”, as critical locations in aseptic packaging, which are of great importance. These sensors are fabricated on flexible polyimide films by means of thin-film technique. Thin layers of titanium and platinum have been deposited on polyimide to define the conductive structures of the sensors. To detect the high-temperature evaporated H₂O₂, a differential temperature set-up is proposed. The sensors are evaluated in a laboratory-scaled sterilizationsystem to simulate the sterilization process. The concentration range of the evaporated H₂O₂ from 0 to 7.7% v/v was defined and the sensors have successfully detected high as well as low H₂O₂ concentrations with a sensitivity of 5.04 °C/% v/v. The characterizations of the sensors confirm their precise fabrication, high sensitivity and the novelty of low H₂O₂ concentration detections for future inline monitoring of food-package sterilization. Y1 - 2018 U6 - https://doi.org/10.1002/pssa.201800044 VL - 215 IS - 15 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Figueroa-Miranda, Gabriela A1 - Feng, Lingyan A1 - Shiu, Simon Chi-Chin A1 - Dirkzwager, Roderick Marshall A1 - Cheung, Yee-Wai A1 - Tanner, Julian Alexander A1 - Schöning, Michael Josef A1 - Offenhäusser, Andreas A1 - Mayer, Dirk T1 - Aptamer-based electrochemical biosensor for highly sensitive and selective malaria detection with adjustable dynamic response range and reusability JF - Sensor and Actuators B: Chemical N2 - 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. Y1 - 2018 U6 - https://doi.org/10.1016/j.snb.2017.07.117 SN - 0925-4005 VL - 255 IS - P1 SP - 235 EP - 243 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Miyamoto, Koichiro A1 - Seki, Kosuke A1 - Suto, Takeyuki A1 - Werner, Frederik A1 - Wagner, Torsten A1 - Schöning, Michael Josef A1 - Yoshinobu, Tatsuo T1 - Improved spatial resolution of the chemical imaging sensor with a hybrid illumination that suppresses lateral diffusion of photocarriers JF - Sensor and Actuators B: Chemical N2 - The chemical imaging sensor is a semiconductor-based chemical sensor capable of visualizing pH and ion distributions. The spatial resolution depends on the lateral diffusion of photocarriers generated by illumination of the semiconductor substrate. In this study, two types of optical setups, one based on a bundle of optical fibers and the other based on a binocular tube head, were developed to project a hybrid illumination of a modulated light beam and a ring-shaped constant illumination onto the sensor plate. An improved spatial resolution was realized by the ring-shaped constant illumination, which suppressed lateral diffusion of photocarriers by enhanced recombination due to the increased carrier concentration. Y1 - 2018 U6 - https://doi.org/10.1016/j.snb.2018.07.016 SN - 0925-4005 VL - 273 SP - 1328 EP - 1333 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Rodrigues, Raul T. A1 - Morais, Paulo V. A1 - Nordi, Cristina S. F. A1 - Schöning, Michael Josef A1 - Siqueira Jr., José R. A1 - Caseli, Luciano T1 - Carbon Nanotubes and Algal Polysaccharides To Enhance the Enzymatic Properties of Urease in Lipid Langmuir-Blodgett Films JF - Langmuir N2 - Algal polysaccharides (extracellular polysaccharides) and carbon nanotubes (CNTs) were adsorbed on dioctadecyldimethylammonium bromide Langmuir monolayers to serve as a matrix for the incorporation of urease. The physicochemical properties of the supramolecular system as a monolayer at the air–water interface were investigated by surface pressure–area isotherms, surface potential–area isotherms, interfacial shear rheology, vibrational spectroscopy, and Brewster angle microscopy. The floating monolayers were transferred to hydrophilic solid supports, quartz, mica, or capacitive electrolyte–insulator–semiconductor (EIS) devices, through the Langmuir–Blodgett (LB) technique, forming mixed films, which were investigated by quartz crystal microbalance, fluorescence spectroscopy, and field emission gun scanning electron microscopy. The enzyme activity was studied with UV–vis spectroscopy, and the feasibility of the thin film as a urea sensor was essayed in an EIS sensor device. The presence of CNT in the enzyme–lipid LB film not only tuned the catalytic activity of urease but also helped to conserve its enzyme activity. Viability as a urease sensor was demonstrated with capacitance–voltage and constant capacitance measurements, exhibiting regular and distinctive output signals over all concentrations used in this work. These results are related to the synergism between the compounds on the active layer, leading to a surface morphology that allowed fast analyte diffusion owing to an adequate molecular accommodation, which also preserved the urease activity. This work demonstrates the feasibility of employing LB films composed of lipids, CNT, algal polysaccharides, and enzymes as EIS devices for biosensing applications. Y1 - 2018 U6 - https://doi.org/10.1021/acs.langmuir.7b04317 SN - 1520-5827 VL - 34 IS - 9 SP - 3082 EP - 3093 PB - ACS Publications CY - Washington, DC ER - TY - CHAP A1 - Schöning, Michael Josef A1 - Wagner, Torsten A1 - Poghossian, Arshak A1 - Miyamoto, K.I. A1 - Werner, C.F. A1 - Krause, S. A1 - Yoshinobu, T. T1 - Light-addressable potentiometric sensors for (bio-)chemical sensing and imaging T2 - Encyclopedia of Interfacial Chemistry: Surface Science and Electrochemistry. Vol. 7 Y1 - 2018 SN - 9780128097397 SP - 295 EP - 308 PB - Elsevier CY - Amsterdam ER - TY - CHAP A1 - Schöning, Michael Josef A1 - Poghossian, Arshak T1 - Enzyme und Biosensorik T2 - Einführung in die Enzymtechnologie N2 - Enzymbasierte Biosensoren finden seit mehr als fünf Jahrzehnten einen prosperierenden Wachstumsmarkt und werden zunehmend auch in biotechnologischen Prozessen eingesetzt. In diesem Kapitel werden, ausgehend vom Sensorbegriff und typischen Kenngrößen für Biosensoren (Abschn. 18.1), elektrochemische Enzym-Biosensoren vorgestellt und deren typischen Einsatzgebiete diskutiert (Abschn. 18.2). Ein Blick über den „Tellerrand“ hinaus zeigt alternative Transduktorprinzipien (Abschn. 18.3) und führt abschließend in aktuelle Forschungstrends ein (Abschn. 18.4). Y1 - 2018 SN - 978-3-662-57619-9 U6 - https://doi.org/10.1007/978-3-662-57619-9_18 SP - 323 EP - 347 PB - Springer Spektrum CY - Berlin ER - TY - CHAP A1 - Yoshinobu, Tatsuo A1 - Krause, Steffi A1 - Miyamoto, Ko-ichiro A1 - Werner, Frederik A1 - Poghossian, Arshak A1 - Wagner, Torsten A1 - Schöning, Michael Josef T1 - (Bio-)chemical Sensing and Imaging by LAPS and SPIM T2 - Label-free biosensing: advanced materials, devices and applications N2 - The light-addressable potentiometric sensor (LAPS) and scanning photo-induced impedance microscopy (SPIM) are two closely related methods to visualise the distributions of chemical species and impedance, respectively, at the interface between the sensing surface and the sample solution. They both have the same field-effect structure based on a semiconductor, which allows spatially resolved and label-free measurement of chemical species and impedance in the form of a photocurrent signal generated by a scanning light beam. In this article, the principles and various operation modes of LAPS and SPIM, functionalisation of the sensing surface for measuring various species, LAPS-based chemical imaging and high-resolution sensors based on silicon-on-sapphire substrates are described and discussed, focusing on their technical details and prospective applications. KW - Chemical imaging KW - Field-effect device KW - Light-addressable potentiometric sensor KW - Potentiometry Y1 - 2018 SN - 978-3-319-75219-8 SP - 103 EP - 132 PB - Springer CY - Cham ER - TY - JOUR A1 - Koch, Claudia A1 - Poghossian, Arshak A1 - Schöning, Michael Josef A1 - Wege, Christian T1 - Penicillin Detection by Tobacco Mosaic Virus-Assisted Colorimetric Biosensors JF - Nanotheranostics N2 - The presentation of enzymes on viral scaffolds has beneficial effects such as an increased enzyme loading and a prolonged reusability in comparison to conventional immobilization platforms. Here, we used modified tobacco mosaic virus (TMV) nanorods as enzyme carriers in penicillin G detection for the first time. Penicillinase enzymes were conjugated with streptavidin and coupled to TMV rods by use of a bifunctional biotin-linker. Penicillinase-decorated TMV particles were characterized extensively in halochromic dye-based biosensing. Acidometric analyte detection was performed with bromcresol purple as pH indicator and spectrophotometry. The TMV-assisted sensors exhibited increased enzyme loading and strongly improved reusability, and higher analysis rates compared to layouts without viral adapters. They extended the half-life of the sensors from 4 - 6 days to 5 weeks and thus allowed an at least 8-fold longer use of the sensors. Using a commercial budget-priced penicillinase preparation, a detection limit of 100 µM penicillin was obtained. Initial experiments also indicate that the system may be transferred to label-free detection layouts. Y1 - 2018 U6 - https://doi.org/10.7150/ntno.22114 SN - 2206-7418 VL - 2 IS - 2 SP - 184 EP - 196 PB - Ivyspring CY - Sydney ER - TY - CHAP A1 - Koch, Claudia A1 - Poghossian, Arshak A1 - Wege, Christina A1 - Schöning, Michael Josef ED - Wege, Christina T1 - TMV-Based Adapter Templates for Enhanced Enzyme Loading in Biosensor Applications T2 - Virus-Derived Nanoparticles for Advanced Technologies N2 - Nanotubular tobacco mosaic virus (TMV) particles and RNA-free lower-order coat protein (CP) aggregates have been employed as enzyme carriers in different diagnostic layouts and compared for their influence on biosensor performance. In the following, we describe a label-free electrochemical biosensor for improved glucose detection by use of TMV adapters and the enzyme glucose oxidase (GOD). A specific and efficient immobilization of streptavidin-conjugated GOD ([SA]-GOD) complexes on biotinylated TMV nanotubes or CP aggregates was achieved via bioaffinity binding. Glucose sensors with adsorptively immobilized [SA]-GOD, and with [SA]-GOD cross-linked with glutardialdehyde, respectively, were tested in parallel on the same sensor chip. Comparison of these sensors revealed that TMV adapters enhanced the amperometric glucose detection remarkably, conveying highest sensitivity, an extended linear detection range and fastest response times. These results underline a great potential of an integration of virus/biomolecule hybrids with electronic transducers for applications in biosensorics and biochips. Here, we describe the fabrication and use of amperometric sensor chips combining an array of circular Pt electrodes, their loading with GOD-modified TMV nanotubes (and other GOD immobilization methods), and the subsequent investigations of the sensor performance. KW - Tobacco mosaic virus (TMV) KW - Coat protein KW - Enzyme nanocarrier KW - Glucose biosensor KW - Glucose oxidase Y1 - 2018 SN - 978-1-4939-7808-3 U6 - https://doi.org/10.1007/978-1-4939-7808-3 N1 - Methods in Molecular Biology, vol 1776 SP - 553 EP - 568 PB - Humana Press CY - New York, NY ER - TY - BOOK A1 - Schöning, Michael Josef A1 - Poghossian, Arshak T1 - Label-free biosensing: advanced materials, devices and applications Y1 - 2018 SN - 978-3-319-75219-8 PB - Springer CY - Cham ER - TY - JOUR A1 - Poghossian, Arshak A1 - Jablonski, Melanie A1 - Koch, Claudia A1 - Bronder, Thomas A1 - Rolka, David A1 - Wege, Christina A1 - Schöning, Michael Josef T1 - Field-effect biosensor using virus particles as scaffolds for enzyme immobilization JF - Biosensors and Bioelectronics N2 - A field-effect biosensor employing tobacco mosaic virus (TMV) particles as scaffolds for enzyme immobilization is presented. Nanotubular TMV scaffolds allow a dense immobilization of precisely positioned enzymes with retained activity. To demonstrate feasibility of this new strategy, a penicillin sensor has been developed by coupling a penicillinase with virus particles as a model system. The developed field-effect penicillin biosensor consists of an Al-p-Si-SiO₂-Ta₂O₅-TMV structure and has been electrochemically characterized in buffer solutions containing different concentrations of penicillin G. In addition, the morphology of the biosensor surface with virus particles was characterized by scanning electron microscopy and atomic force microscopy methods. The sensors possessed a high penicillin sensitivity of ~ 92 mV/dec in a nearly-linear range from 0.1 mM to 10 mM, and a low detection limit of about 50 µM. The long-term stability of the penicillin biosensor was periodically tested over a time period of about one year without any significant loss of sensitivity. The biosensor has also been successfully applied for penicillin detection in bovine milk samples. Y1 - 2018 U6 - https://doi.org/10.1016/j.bios.2018.03.036 SN - 0956-5663 VL - 110 SP - 168 EP - 174 PB - Elsevier CY - Amsterdam ER -