@misc{O'ConnellHovenSiegertetal.2007,
  author    = {O'Connell, Timothy and Hoven, Nina and Siegert, Petra and Maurer, Karl-Heinz},
  title     = {Amadoriasen in Wasch- und Reinigungsmitteln [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 45},
  year      = {2007},
  language  = {de}
}
@misc{SchulzezurWiescheOttoKleenetal.2005,
  author    = {Schulze zur Wiesche, Erik and Otto, Ralf and Kleen, Astrid and Hollenberg, Detlef and S{\"a}ttler, Andrea and Siegert, Petra and Boßmann, Britta},
  title     = {Verfahren zur dauerhaften Ausr{\"u}stung keratinischer Fasern mit Pflegewirkstoffen durch Carboxylesterhydrolasen [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt},
  address   = {M{\"u}nchen / Den Hague},
  pages     = {1 -- 13},
  year      = {2005},
  language  = {de}
}
@misc{KluinMaurerBanowskietal.2005,
  author    = {Kluin, Cornelia and Maurer, Karl-Heinz and Banowski, Bernhard and Bessler, Cornelius and Siegert, Petra},
  title     = {Verwendung von Siderophoren gegen Geruchskeime [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt},
  address   = {M{\"u}nchen},
  pages     = {1 -- 32},
  year      = {2005},
  language  = {de}
}
@misc{BankowskiHoffmannWadleetal.2003,
  author    = {Bankowski, Bernhard and Hoffmann, Daniele and Wadle, Armin and Siegert, Petra and S{\"a}ttler, Andrea and Gerke, Thomas},
  title     = {Beta-Glucuronidase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt / WIPO},
  address   = {M{\"u}nchen / Den Hague / Genf},
  pages     = {1 -- 24},
  year      = {2003},
  language  = {de}
}
@misc{SiegertBankowski2003,
  author    = {Siegert, Petra and Bankowski, Bernhard},
  title     = {Verwendung von Steroidsulfatase-Inhibitoren zur Verminderung von Haarausfall ; Kosmetische und pharmazeutische Zusammensetzungen enthaltend Steroidsulfatase-Inhibitoren und deren Verwendung zur Verminderung von Haarausfall [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt},
  address   = {M{\"u}nchen / Den Hague},
  pages     = {1 -- 38},
  year      = {2003},
  language  = {de}
}
@misc{BanowskiWadleSiegert2004,
  author    = {Banowski, Bernhard and Wadle, Armin and Siegert, Petra},
  title     = {Arylsulfatase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]},
  publisher = {Deutsches Patent- und Markenamt / Europ{\"a}isches Patentamt},
  address   = {M{\"u}nchen / Den Hague},
  pages     = {1 -- 15},
  year      = {2004},
  language  = {de}
}
@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}
}
@techreport{SiegertBongaertsWagneretal.2022,
  author    = {Siegert, Petra and Bongaerts, Johannes and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Selmer, Thorsten},
  title     = {Abschlussbericht zum Projekt zur {\"U}berwachung biotechnologischer Prozesse mittels Diacetyl-/Acetoin-Biosensor und Evaluierung von Acetoin-Reduktasen zur Verwendung in Biotransformationen},
  address   = {Aachen},
  organization    = {FH Aachen},
  pages     = {16 Seiten},
  year      = {2022},
  language  = {de}
}
@article{FalkenbergKohnBottetal.2023,
  author    = {Falkenberg, Fabian and Kohn, Sophie and Bott, Michael and Bongaerts, Johannes and Siegert, Petra},
  title     = {Biochemical characterisation of a novel broad pH spectrum subtilisin from Fictibacillus arsenicus DSM 15822ᵀ},
  series = {FEBS Open Bio},
  volume    = {13},
  journal   = {FEBS Open Bio},
  number    = {11},
  publisher = {Wiley},
  address   = {Hoboken, NJ},
  issn      = {2211-5463},
  doi       = {10.1002/2211-5463.13701},
  pages     = {2035 -- 2046},
  year      = {2023},
  abstract  = {Subtilisins from microbial sources, especially from the Bacillaceae family, are of particular interest for biotechnological applications and serve the currently growing enzyme market as efficient and novel biocatalysts. Biotechnological applications include use in detergents, cosmetics, leather processing, wastewater treatment and pharmaceuticals. To identify a possible candidate for the enzyme market, here we cloned the gene of the subtilisin SPFA from Fictibacillus arsenicus DSM 15822ᵀ (obtained through a data mining-based search) and expressed it in Bacillus subtilis DB104. After production and purification, the protease showed a molecular mass of 27.57 kDa and a pI of 5.8. SPFA displayed hydrolytic activity at a temperature optimum of 80 °C and a very broad pH optimum between 8.5 and 11.5, with high activity up to pH 12.5. SPFA displayed no NaCl dependence but a high NaCl tolerance, with decreasing activity up to concentrations of 5 m NaCl. The stability enhanced with increasing NaCl concentration. Based on its substrate preference for 10 synthetic peptide 4-nitroanilide substrates with three or four amino acids and its phylogenetic classification, SPFA can be assigned to the subgroup of true subtilisins. Moreover, SPFA exhibited high tolerance to 5\% (w/v) SDS and 5\% H₂O₂ (v/v). The biochemical properties of SPFA, especially its tolerance of remarkably high pH, SDS and H₂O₂, suggest it has potential for biotechnological applications.},
  language  = {en}
}
@article{MuschallikKippReckeretal.2020,
  author    = {Muschallik, Lukas and Kipp, Carina Ronja and Recker, Inga and Bongaerts, Johannes and Pohl, Martina and Gelissen, Melanie and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra},
  title     = {Synthesis of α-hydroxy ketones and vicinal diols with the Bacillus licheniformis DSM 13T butane-2, 3-diol dehydrogenase},
  series = {Journal of Biotechnology},
  volume    = {202},
  journal   = {Journal of Biotechnology},
  number    = {Vol. 324},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {2590-1559},
  doi       = {10.1016/j.jbiotec.2020.09.016},
  pages     = {61 -- 70},
  year      = {2020},
  abstract  = {The enantioselective synthesis of α-hydroxy ketones and vicinal diols is an intriguing field because of the broad applicability of these molecules. Although, butandiol dehydrogenases are known to play a key role in the production of 2,3-butandiol, their potential as biocatalysts is still not well studied. Here, we investigate the biocatalytic properties of the meso-butanediol dehydrogenase from Bacillus licheniformis DSM 13T (BlBDH). The encoding gene was cloned with an N-terminal StrepII-tag and recombinantly overexpressed in E. coli. BlBDH is highly active towards several non-physiological diketones and α-hydroxyketones with varying aliphatic chain lengths or even containing phenyl moieties. By adjusting the reaction parameters in biotransformations the formation of either the α-hydroxyketone intermediate or the diol can be controlled.},
  language  = {en}
}
@article{JablonskiMuenstermannNorketal.2021,
  author    = {Jablonski, Melanie and M{\"u}nstermann, Felix and Nork, Jasmina and Molinnus, Denise and Muschallik, Lukas and Bongaerts, Johannes and Wagner, Torsten and Keusgen, Michael and Siegert, Petra and Sch{\"o}ning, Michael Josef},
  title     = {Capacitive field-effect biosensor applied for the detection of acetoin in alcoholic beverages and fermentation broths},
  series = {physica status solidi (a) applications and materials science},
  volume    = {218},
  journal   = {physica status solidi (a) applications and materials science},
  number    = {13},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.202000765},
  pages     = {7 Seiten},
  year      = {2021},
  abstract  = {An acetoin biosensor based on a capacitive electrolyte-insulator-semiconductor (EIS) structure modified with the enzyme acetoin reductase, also known as butane-2,3-diol dehydrogenase (Bacillus clausii DSM 8716ᵀ), is applied for acetoin detection in beer, red wine, and fermentation broth samples for the first time. The EIS sensor consists of an Al/p-Si/SiO₂/Ta₂O₅ layer structure with immobilized acetoin reductase on top of the Ta₂O₅ transducer layer by means of crosslinking via glutaraldehyde. The unmodified and enzyme-modified sensors are electrochemically characterized by means of leakage current, capacitance-voltage, and constant capacitance methods, respectively.},
  language  = {en}
}
@article{MuschallikMolinnusJablonskietal.2020,
  author    = {Muschallik, Lukas and Molinnus, Denise and Jablonski, Melanie and Kipp, Carina Ronja and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra},
  title     = {Synthesis of α-hydroxy ketones and vicinal (R, R)-diols by Bacillus clausii DSM 8716ᵀ butanediol dehydrogenase},
  series = {RSC Advances},
  volume    = {10},
  journal   = {RSC Advances},
  publisher = {Royal Society of Chemistry (RSC)},
  address   = {Cambridge},
  issn      = {2046-2069},
  doi       = {10.1039/D0RA02066D},
  pages     = {12206 -- 12216},
  year      = {2020},
  abstract  = {α-hydroxy ketones (HK) and 1,2-diols are important building blocks for fine chemical synthesis. Here, we describe the R-selective 2,3-butanediol dehydrogenase from B. clausii DSM 8716ᵀ (BcBDH) that belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR) and catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. Supplementation of Mn²⁺ (1 mM) increases BcBDH's activity in biotransformations. Furthermore, the biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated.},
  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}
}
@misc{O'ConnellSiegertEversetal.2010,
  author    = {O'Connell, Timothy and Siegert, Petra and Evers, Stefan and Bongaerts, Johannes and Weber, Thomas and Maurer, Karl-Heinz and Bessler, Cornelius},
  title     = {Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft [Offenlegungsschrift]},
  publisher = {Deutsches Patentamt},
  address   = {M{\"u}nchen},
  pages     = {1 -- 34},
  year      = {2010},
  language  = {de}
}
@techreport{HaegerBongaertsSiegert2023,
  author    = {Haeger, Gerrit and Bongaerts, Johannes and Siegert, Petra},
  title     = {Abschlussbericht Teil II: Eingehende Darstellung Neue biobasierte Lipopeptide aus nachhaltiger Produktion (LipoPep)},
  pages     = {17Seiten},
  year      = {2023},
  language  = {de}
}