@article{WiegandVoigtAlbrechtetal.2013, author = {Wiegand, Sandra and Voigt, Birgit and Albrecht, Dirk and Bongaerts, Johannes and Evers, Stefan and Hecker, Michael and Daniel, Rolf and Liesegang, Heiko}, title = {Fermentation stage-dependent adaptations of Bacillus licheniformis during enzyme production}, series = {Microbial Cell Factories}, volume = {12}, journal = {Microbial Cell Factories}, publisher = {Biomed Central}, address = {London}, issn = {1475-2859}, doi = {10.1186/1475-2859-12-120}, pages = {120}, year = {2013}, language = {en} } @article{WiegandDietrichHerteletal.2013, author = {Wiegand, Sandra and Dietrich, Sascha and Hertel, Robert and Bongaerts, Johannes and Evers, Stefan and Volland, Sonja and Daniel, Rolf and Liesegang, Heiko}, title = {RNA-Seq of Bacillus licheniformis: active regulatory RNA features expressed within a productive fermentation}, series = {BMC genomics}, volume = {Vol. 14}, journal = {BMC genomics}, publisher = {BioMed Central}, address = {London}, issn = {1471-2164}, pages = {667}, year = {2013}, language = {en} } @article{WhiteheadOehlschlaegerAlmajhdietal.2014, author = {Whitehead, Mark and {\"O}hlschl{\"a}ger, Peter and Almajhdi, Fahad N. and Alloza, Leonor and Marz{\´a}bal, Pablo and Meyers, Ann E. and Hitzeroth, Inga I. and Rybicki, Edward P.}, title = {Human papillomavirus (HPV) type 16 E7 protein bodies cause tumour regression in mice}, series = {BMC cancer}, journal = {BMC cancer}, number = {14:367}, publisher = {BioMed Central}, address = {London}, issn = {1471-2407}, doi = {10.1186/1471-2407-14-367}, pages = {1 -- 15}, year = {2014}, language = {en} } @article{WernerKrumbeSchumacheretal.2011, author = {Werner, Frederik and Krumbe, Christoph and Schumacher, Katharina and Groebel, Simone and Spelthahn, Heiko and Stellberg, Michael and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Keusgen, Michael and Baumann, Marcus and Sch{\"o}ning, Michael Josef}, title = {Determination of the extracellular acidification of Escherichia coli by a light-addressable potentiometric sensor}, 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 = {1340 -- 1344}, year = {2011}, 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{WerkhausenAlbrachtCroninetal.2017, author = {Werkhausen, Amelie and Albracht, Kirsten and Cronin, Neil J. and Meier, Rahel and Mojsen-Moeller, Jens and Seynnes, Olivier R.}, title = {Modulation of muscle-tendon interaction in the human triceps surae during an energy dissipation task}, series = {Journal of Experimental Biology}, volume = {220}, journal = {Journal of Experimental Biology}, number = {22}, issn = {0022-0949}, doi = {10.1242/jeb.164111}, pages = {4141 -- 4149}, year = {2017}, language = {en} } @incollection{WendorffEggertPohletal.2007, author = {Wendorff, Marion and Eggert, Thorsten and Pohl, Martina and Dresen, Carola and M{\"u}ller, Michael and Jaeger, Karl-Erich and Sprenger, Georg A. and Sch{\"u}rmann, Melanie and Sch{\"u}rmann, Martin and Johnen, Sandra and Sprenger, Gerda and Sahm, Hermann and Inoue, Tomoyuki and Sch{\"o}rken, Ulrich and Breittaupt, Holger and Fr{\"o}lich, Bettina and Heim, Petra and Iding, Hans and Juchem, Bettina and Siegert, Petra and Kula, Maria-Regina and Weckbecker, Andrea and Hummel, Werner and Fessner, Wolf-Dieter and Elling, Lothar and Wolberg, Michael and Bode, Silke and Feldmann, Ralf and Geilenkirchen, Petra and Schubert, Thomas and Walter, Lydia and D{\"u}nnwald, Thomas and Demir, Ayhan S. and Kolter-Jung, Doris and Nitsche, Adam and D{\"u}nkelmann, Pascal and Cosp, Annabel and Lingen, Bettina}, title = {Catalytic asymmetric synthesis : section 2.2}, series = {Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...}, booktitle = {Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...}, publisher = {Wiley-VCH}, address = {Weinheim}, isbn = {978-3-527-31473-7}, pages = {298 -- 413}, year = {2007}, language = {en} } @article{WeldenJablonskiWegeetal.2021, author = {Welden, Rene and Jablonski, Melanie and Wege, Christina and Keusgen, Michael and Wagner, Patrick Hermann and Wagner, Torsten and Sch{\"o}ning, Michael Josef}, title = {Light-Addressable Actuator-Sensor Platform for Monitoring and Manipulation of pH Gradients in Microfluidics: A Case Study with the Enzyme Penicillinase}, series = {Biosensors}, volume = {11}, journal = {Biosensors}, number = {6}, publisher = {MDPI}, address = {Basel}, issn = {2079-6374}, doi = {10.3390/bios11060171}, pages = {Artikel 171}, year = {2021}, abstract = {The feasibility of light-addressed detection and manipulation of pH gradients inside an electrochemical microfluidic cell was studied. Local pH changes, induced by a light-addressable electrode (LAE), were detected using a light-addressable potentiometric sensor (LAPS) with different measurement modes representing an actuator-sensor system. Biosensor functionality was examined depending on locally induced pH gradients with the help of the model enzyme penicillinase, which had been immobilized in the microfluidic channel. The surface morphology of the LAE and enzyme-functionalized LAPS was studied by scanning electron microscopy. Furthermore, the penicillin sensitivity of the LAPS inside the microfluidic channel was determined with regard to the analyte's pH influence on the enzymatic reaction rate. In a final experiment, the LAE-controlled pH inhibition of the enzyme activity was monitored by the LAPS.}, language = {en} } @article{WeldenSeverinsPoghossianetal.2022, author = {Welden, Melanie and Severins, Robin and Poghossian, Arshak and Wege, Christina and Bongaerts, Johannes and Siegert, Petra and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Detection of acetoin and diacetyl by a tobacco mosaic virus-assisted field-effect biosensor}, series = {Chemosensors}, volume = {10}, journal = {Chemosensors}, number = {6}, publisher = {MDPI}, address = {Basel}, issn = {2227-9040}, doi = {10.3390/chemosensors10060218}, pages = {Artikel 218}, year = {2022}, abstract = {Acetoin and diacetyl have a major impact on the flavor of alcoholic beverages such as wine or beer. Therefore, their measurement is important during the fermentation process. Until now, gas chromatographic techniques have typically been applied; however, these require expensive laboratory equipment and trained staff, and do not allow for online monitoring. In this work, a capacitive electrolyte-insulator-semiconductor sensor modified with tobacco mosaic virus (TMV) particles as enzyme nanocarriers for the detection of acetoin and diacetyl is presented. The enzyme acetoin reductase from Alkalihalobacillus clausii DSM 8716ᵀ is immobilized via biotin-streptavidin affinity, binding to the surface of the TMV particles. The TMV-assisted biosensor is electrochemically characterized by means of leakage-current, capacitance-voltage, and constant capacitance measurements. In this paper, the novel biosensor is studied regarding its sensitivity and long-term stability in buffer solution. Moreover, the TMV-assisted capacitive field-effect sensor is applied for the detection of diacetyl for the first time. The measurement of acetoin and diacetyl with the same sensor setup is demonstrated. Finally, the successive detection of acetoin and diacetyl in buffer and in diluted beer is studied by tuning the sensitivity of the biosensor using the pH value of the measurement solution.}, language = {en} } @article{WeldenPoghossianVahidpouretal.2022, author = {Welden, Melanie and Poghossian, Arshak and Vahidpour, Farnoosh and Wendlandt, Tim and Keusgen, Michael and Wege, Christina and Sch{\"o}ning, Michael Josef}, title = {Towards multi-analyte detection with field-effect capacitors modified with tobacco mosaic virus bioparticles as enzyme nanocarriers}, series = {Biosensors}, volume = {12}, journal = {Biosensors}, number = {1}, publisher = {MDPI}, address = {Basel}, issn = {2079-6374}, doi = {10.3390/bios12010043}, pages = {Artikel 43}, year = {2022}, abstract = {Utilizing an appropriate enzyme immobilization strategy is crucial for designing enzyme-based biosensors. Plant virus-like particles represent ideal nanoscaffolds for an extremely dense and precise immobilization of enzymes, due to their regular shape, high surface-to-volume ratio and high density of surface binding sites. In the present work, tobacco mosaic virus (TMV) particles were applied for the co-immobilization of penicillinase and urease onto the gate surface of a field-effect electrolyte-insulator-semiconductor capacitor (EISCAP) with a p-Si-SiO₂-Ta₂O₅ layer structure for the sequential detection of penicillin and urea. The TMV-assisted bi-enzyme EISCAP biosensor exhibited a high urea and penicillin sensitivity of 54 and 85 mV/dec, respectively, in the concentration range of 0.1-3 mM. For comparison, the characteristics of single-enzyme EISCAP biosensors modified with TMV particles immobilized with either penicillinase or urease were also investigated. The surface morphology of the TMV-modified Ta₂O₅-gate was analyzed by scanning electron microscopy. Additionally, the bi-enzyme EISCAP was applied to mimic an XOR (Exclusive OR) enzyme logic gate.}, language = {en} }