@article{SelmerNetzPohletal.2002,
  author    = {Selmer, Thorsten and Netz, Daili Jacqueline Aguilar and Pohl, Regula and Beck-Sickinger, Annette G.},
  title     = {Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus / Netz, Daili Jacqueline Aguilar ; Pohl, Regula ; Beck-Sickinger, Annette G. ; Selmer, Thorsten ; Pierik, Antonio J. ; Carmo de Frei},
  series = {Journal of Molecular Biology. 319 (2002), H. 3},
  journal   = {Journal of Molecular Biology. 319 (2002), H. 3},
  isbn      = {0022-2836},
  pages     = {745 -- 756},
  year      = {2002},
  language  = {en}
}
@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{FalkenbergRahbaFischeretal.2022,
  author    = {Falkenberg, Fabian and Rahba, Jade and Fischer, David and Bott, Michael and Bongaerts, Johannes and Siegert, Petra},
  title     = {Biochemical characterization of a novel oxidatively stable, halotolerant, and high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T},
  series = {FEBS Open Bio},
  volume    = {12},
  journal   = {FEBS Open Bio},
  number    = {10},
  publisher = {Wiley},
  address   = {Hoboken, NJ},
  issn      = {2211-5463},
  doi       = {10.1002/2211-5463.13457},
  pages     = {1729 -- 1746},
  year      = {2022},
  abstract  = {Halophilic and halotolerant microorganisms represent a promising source of salt-tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T. The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high-alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0-12.0 and temperature 20-80 °C, optimally at pH 9.0-9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58\% of residual activity when incubated at 10 °C with 5\% (v/v) H2O2 for 1 h while stimulated at 1\% (v/v) H2O2. Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m. This study demonstrates the potential of SPAO for biotechnological applications in the future.},
  language  = {en}
}
@inproceedings{KasperSchiffelsKrafftetal.2016,
  author    = {Kasper, Katharina and Schiffels, Johannes and Krafft, Simone and Kuperjans, Isabel and Elbers, Gereon and Selmer, Thorsten},
  title     = {Biogas Production on Demand Regulated by Butyric Acid Addition},
  series = {IOP Conference Series: Earth and Environmental Science. Bd. 32},
  volume    = {32},
  booktitle = {IOP Conference Series: Earth and Environmental Science. Bd. 32},
  issn      = {1755-1315},
  doi       = {10.1088/1755-1315/32/1/012009},
  pages     = {012009/1 -- 012009/4},
  year      = {2016},
  language  = {en}
}
@article{MaggakisKelemenBorkKayseretal.2003,
  author    = {Maggakis-Kelemen, C. and Bork, M. and Kayser, Peter and Biselli, Manfred and Artmann, Gerhard},
  title     = {Biological and mechanical quality of red blood cells cultured from human umbilical cord blood stem cells},
  series = {Medical and biological engineering and computing. 41 (2003), H. 3},
  journal   = {Medical and biological engineering and computing. 41 (2003), H. 3},
  isbn      = {0140-0118},
  pages     = {350 -- 356},
  year      = {2003},
  language  = {en}
}
@book{ArtmannTemizArtmannZhubanovaetal.2018,
  author    = {Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l and Zhubanova, Azhar A. and Digel, Ilya},
  title     = {Biological, physical and technical basics of cell engineering},
  editor    = {Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l and Zhubanova, Azhar A. and Digel, Ilya},
  publisher = {Springer},
  address   = {Singapore},
  isbn      = {978-981-10-7903-0},
  pages     = {xxiv, 481 Seiten ; Illustrationen, Diagramme},
  year      = {2018},
  language  = {en}
}
@techreport{TippkoetterWagner2019,
  author    = {Tippk{\"o}tter, Nils and Wagner, Sebastian},
  title     = {Biomimetischer Klebstoff aus ligninhaltigen Pflanzenresten (Teilvorhaben 1 und 2) : Schlussbericht zum Vorhaben : Laufzeit: 01.01.2016 bis 31.03.2019},
  publisher = {FH Aachen},
  address   = {J{\"u}lich},
  doi       = {10.2314/KXP:169732777X},
  pages     = {109 S.},
  year      = {2019},
  language  = {de}
}
@book{JerominBertau2005,
  author    = {Jeromin, G{\"u}nter Erich and Bertau, Martin},
  title     = {Bioorganikum : ein Praktikum der Biotransformationen. - 1. Aufl.},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  isbn      = {3-527-31245-5},
  pages     = {300 S.},
  year      = {2005},
  language  = {de}
}
@article{BiselliHilbertJelineketal.2001,
  author    = {Biselli, Manfred and Hilbert, U. and Jelinek, N. and Schmidt, S.},
  title     = {Bioprocess development for the cultivation of human T-lymphocytes / Hilbert, U. ; Jelinek, N. Schmidt, S. ; Biselli, M.},
  series = {Engineering in Life Sciences. 1 (2001)},
  journal   = {Engineering in Life Sciences. 1 (2001)},
  isbn      = {1618-0240},
  pages     = {20 -- 23},
  year      = {2001},
  language  = {en}
}
@article{BiselliJelinekSchmidtetal.2001,
  author    = {Biselli, Manfred and Jelinek, N. and Schmidt, S. and Noll, T.},
  title     = {Bioreaktoren zur Kultivierung blutbildender Zellen / Jelinek, N. ; Schmidt, S. ; Noll, T. ; Biselli, M.},
  series = {Bioforum. 24 (2001), H. 6},
  journal   = {Bioforum. 24 (2001), H. 6},
  isbn      = {0940-0079},
  pages     = {418 -- 419},
  year      = {2001},
  language  = {de}
}