@misc{BanowskiWadleSiegert2003, author = {Banowski, Bernhard and Wadle, Armin and Siegert, Petra}, title = {Arylsulfatase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt}, address = {M{\"u}nchen}, pages = {1 -- 20}, year = {2003}, language = {de} } @misc{BanowskiHoffmannWadleetal.2002, author = {Banowski, Bernhard and Hoffmann, Daniele and Wadle, Armin and Siegert, Petra and S{\"a}ttler, Andrea and Gerke, Thomas}, title = {Arylsulfatase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Polish Patent Office / WIPO}, address = {M{\"u}nchen / Warsaw / Genf}, pages = {1 -- 22}, year = {2002}, language = {de} } @misc{BanowskiWadleSiegert2005, author = {Banowski, Bernhard and Wadle, Armin and Siegert, Petra}, title = {Use of hydroxydiphenyl ether derivatives as arylsulfatase-inhibitors in deodorants and antiperspirants [Europ{\"a}ische Patentanmeldung / US Patentanmeldung / Australische Patentanmeldung / Internationale Patentanmeldung]}, publisher = {Europ{\"a}isches Patentamt / USPTO / IP Australia / WIPO}, address = {Den Hague / Washington / Canberra/ Genf}, pages = {1 -- 40}, year = {2005}, language = {de} } @misc{SchmitzSpitzMerkeletal.2004, author = {Schmitz, Susanne and Spitz, Astrid and Merkel, Marion and Siegert, Petra}, title = {Verfahren zur Bestimmung des enzymatischen Status humaner Haut in vitro [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / IP Australia / WIPO}, address = {M{\"u}nchen / Den Hague / Canberra / Genf}, pages = {1 -- 7}, year = {2004}, language = {de} } @misc{BanowskiWadleSiegertetal.2004, author = {Banowski, Bernhard and Wadle, Armin and Siegert, Petra and S{\"a}ttler, Andrea}, title = {Lipase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt}, address = {M{\"u}nchen / Den Hague}, pages = {1 -- 22}, year = {2004}, language = {de} } @misc{BanowskiWaldmannLaueWadleetal.2004, author = {Banowski, Bernhard and Waldmann-Laue, Marianne and Wadle, Armin and Siegert, Petra and S{\"a}ttler, Andreas}, title = {5-Lipoxigenase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]}, publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt}, address = {M{\"u}nchen / Den Hague}, pages = {1 -- 12}, year = {2004}, language = {de} } @article{MolinnusBaeckerSiegertetal.2015, author = {Molinnus, Denise and B{\"a}cker, Matthias and Siegert, Petra and Willenberg, H. and Poghossian, Arshak and Keusgen, M. and Sch{\"o}ning, Michael Josef}, title = {Detection of Adrenaline Based on Substrate Recycling Amplification}, series = {Procedia Engineering}, volume = {120}, journal = {Procedia Engineering}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1877-7058}, doi = {10.1016/j.proeng.2015.08.708}, pages = {540 -- 543}, year = {2015}, abstract = {An amperometric enzyme biosensor has been applied for the detection of adrenaline. The adrenaline biosensor has been prepared by modification of an oxygen electrode with the enzyme laccase that operates at a broad pH range between pH 3.5 to pH 8. The enzyme molecules were immobilized via cross-linking with glutaraldehyde. The sensitivity of the developed adrenaline biosensor in different pH buffer solutions has been studied.}, language = {en} } @misc{O'ConnellSiegertMaureretal.2010, author = {O'Connell, Timothy and Siegert, Petra and Maurer, Karl-Heinz and Schiedel, Marc-Steffen and Vockenroth, Inga Kerstin}, title = {Method for improving the cleaning action of a detergent or cleaning agent [Internationale Patentanmeldung]}, publisher = {WIPO}, address = {Genf}, pages = {1 -- 15}, year = {2010}, language = {en} } @article{MolinnusSorichBartzetal.2016, author = {Molinnus, Denise and Sorich, Maren and Bartz, Alexander and Siegert, Petra and Willenberg, Holger S. and Lisdat, Fred and Poghossian, Arshak and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Towards an adrenaline biosensor based on substrate recycling amplification in combination with an enzyme logic gate}, series = {Sensors and Actuators B: Chemical}, volume = {237}, journal = {Sensors and Actuators B: Chemical}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0925-4005}, doi = {10.1016/j.snb.2016.06.064}, pages = {190 -- 195}, year = {2016}, abstract = {An amperometric biosensor using a substrate recycling principle was realized for the detection of low adrenaline concentrations (1 nM) by measurements in phosphate buffer and Ringer's solution at pH 6.5 and pH 7.4, respectively. In proof-of-concept experiments, a Boolean logic-gate principle has been applied to develop a digital adrenaline biosensor based on an enzyme AND logic gate. The obtained results demonstrate that the developed digital biosensor is capable for a rapid qualitative determination of the presence/absence of adrenaline in a YES/NO statement. Such digital biosensor could be used in clinical diagnostics for the control of a correct insertion of a catheter in the adrenal veins during adrenal venous-sampling procedure.}, language = {en} } @article{MuschallikMolinnusBongaertsetal.2017, author = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten}, title = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme}, series = {Journal of Biotechnology}, volume = {258}, journal = {Journal of Biotechnology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0168-1656}, doi = {10.1016/j.jbiotec.2017.07.020}, pages = {41 -- 50}, year = {2017}, abstract = {The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43\%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.}, language = {en} }