@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{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{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{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{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{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{PoghossianYoshinobuSimonisetal.2001, author = {Poghossian, Arshak and Yoshinobu, Tatsuo and Simonis, A. and Ecken, H. and L{\"u}th, Hans and Sch{\"o}ning, Michael Josef}, title = {Penicillin detection by means of field-effect based sensors: EnFET, capacitive EIS sensor or LAPS?}, series = {Sensors and Actuators B. 78 (2001), H. 1-3}, journal = {Sensors and Actuators B. 78 (2001), H. 1-3}, isbn = {0925-4005}, pages = {237 -- 242}, year = {2001}, language = {en} } @article{PoghossianYoshinobuSimonisetal.2000, author = {Poghossian, Arshak and Yoshinobu, T. and Simonis, A. and Ecken, H. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef}, title = {Penicillin detection by means of field-effect based sensors: EnFET, capacitive EIS sensor or LAPS?}, series = {Proceedings : Copenhagen, Denmark, 27 - 30 August 2000 / [ed.: R. de Reus ...]}, journal = {Proceedings : Copenhagen, Denmark, 27 - 30 August 2000 / [ed.: R. de Reus ...]}, publisher = {MIC, Mikroelektronik Centret}, address = {Lyngby, Denmark}, isbn = {87-89935-50-0}, pages = {27 -- 30}, year = {2000}, language = {en} } @article{PoghossianThustSchrothetal.2001, author = {Poghossian, Arshak and Thust, M. and Schroth, P. and Steffen, A. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef}, title = {Penicillin detection by means of silicon-based field-effect structures}, series = {Sensors and Materials. 13 (2001), H. 4}, journal = {Sensors and Materials. 13 (2001), H. 4}, isbn = {0392-2510}, pages = {207 -- 223}, year = {2001}, language = {en} } @article{KochPoghossianSchoeningetal.2018, author = {Koch, Claudia and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Wege, Christian}, title = {Penicillin Detection by Tobacco Mosaic Virus-Assisted Colorimetric Biosensors}, series = {Nanotheranostics}, volume = {2}, journal = {Nanotheranostics}, number = {2}, publisher = {Ivyspring}, address = {Sydney}, issn = {2206-7418}, doi = {10.7150/ntno.22114}, pages = {184 -- 196}, year = {2018}, abstract = {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.}, language = {en} }