@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{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}
}
@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{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}
}
@incollection{MufflerPothSiekeretal.2011,
  author    = {Muffler, Kai and Poth, Sabastian and Sieker, Tim and Tippk{\"o}tter, Nils and Ulber, Roland and Sell, Dieter},
  title     = {Bio-feedstocks},
  series = {Comprehensive biotechnology : principles and practices in industry, agcriculture, medicine and the environment. Volume 2: Engineering fundamentals of biotechnology},
  booktitle = {Comprehensive biotechnology : principles and practices in industry, agcriculture, medicine and the environment. Volume 2: Engineering fundamentals of biotechnology},
  editor    = {Moo-Young, Murray},
  edition   = {2. edition},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {978-0-444-53352-4},
  doi       = {10.1016/B978-0-08-088504-9.00088-X},
  pages     = {93 -- 101},
  year      = {2011},
  language  = {en}
}
@article{IdingDuennwaldGreineretal.2000,
  author    = {Iding, Hans and D{\"u}nnwald, Thomas and Greiner, Lasse and Liese, Andreas and M{\"u}ller, Michael and Siegert, Petra and Gr{\"o}tzinger, Joachim and Demir, Ayhan S. and Pohl, Martina},
  title     = {Benzoylformate Decarboxylase from Pseudomonas putida as Stable Catalyst for the Synthesis of Chiral 2-Hydroxy Ketones},
  series = {Chemistry - a European journal},
  volume    = {Vol. 6},
  journal   = {Chemistry - a European journal},
  number    = {Iss. 8},
  issn      = {1521-3765 (E-Journal); 0947-6539 (Print)},
  pages     = {1483 -- 1495},
  year      = {2000},
  language  = {en}
}
@article{BurgerLindnerRumpfetal.2022,
  author    = {Burger, Ren{\´e} and Lindner, Simon and Rumpf, Jessica and Do, Xuan Tung and Diehl, Bernd W.K. and Rehahn, Matthias and Monakhova, Yulia and Schulze, Margit},
  title     = {Benchtop versus high field NMR: Comparable performance found for the molecular weight determination of lignin},
  series = {Journal of Pharmaceutical and Biomedical Analysis},
  volume    = {212},
  journal   = {Journal of Pharmaceutical and Biomedical Analysis},
  number    = {Article number: 114649},
  publisher = {Elsevier},
  address   = {New York, NY},
  isbn      = {0731-7085},
  doi       = {10.1016/j.jpba.2022.114649},
  year      = {2022},
  abstract  = {Lignin is a promising renewable biopolymer being investigated worldwide as an environmentally benign substitute of fossil-based aromatic compounds, e.g. for the use as an excipient with antioxidant and antimicrobial properties in drug delivery or even as active compound. For its successful implementation into process streams, a quick, easy, and reliable method is needed for its molecular weight determination. Here we present a method using 1H spectra of benchtop as well as conventional NMR systems in combination with multivariate data analysis, to determine lignin's molecular weight (Mw and Mn) and polydispersity index (PDI). A set of 36 organosolv lignin samples (from Miscanthus x giganteus, Paulownia tomentosa and Silphium perfoliatum) was used for the calibration and cross validation, and 17 samples were used as external validation set. Validation errors between 5.6\% and 12.9\% were achieved for all parameters on all NMR devices (43, 60, 500 and 600 MHz). Surprisingly, no significant difference in the performance of the benchtop and high-field devices was found. This facilitates the application of this method for determining lignin's molecular weight in an industrial environment because of the low maintenance expenditure, small footprint, ruggedness, and low cost of permanent magnet benchtop NMR systems.},
  language  = {en}
}
@article{BiselliThoemmesKulaetal.1994,
  author    = {Biselli, Manfred and Th{\"o}mmes, J. and Kula, M.-R. and Wandrey, Christian},
  title     = {Batch kinetic data of hybridoma growth and productivity as a basis for the simulation of antibody production in various culture systems / Th{\"o}mmes, J. ; Biselli, M. ; Kula, M.-R. ; Wandrey, C.},
  series = {Animal cell technology : products of today, prospects for tomorrow ; ESACT, European Society for Animal Cell Technology, the 12th meeting / Ed. R. E. Spier},
  journal   = {Animal cell technology : products of today, prospects for tomorrow ; ESACT, European Society for Animal Cell Technology, the 12th meeting / Ed. R. E. Spier},
  publisher = {Butterworth-Heinemann},
  address   = {Oxford},
  isbn      = {0750618450},
  pages     = {513 -- 517},
  year      = {1994},
  language  = {en}
}
@article{SelmerJennemannBaueretal.1999,
  author    = {Selmer, Thorsten and Jennemann, Richard and Bauer, Bernhard L. and Bertalanffy, Helmut},
  title     = {Basidiolipids from Agaricus are novel immune adjuvants / Jennemann, R. ; Bauer, BL. ; Bertalanffy, H. ; Selmer, T. ; Wiegandt, H.},
  series = {Immunobiology. 200 (1999), H. 2},
  journal   = {Immunobiology. 200 (1999), H. 2},
  isbn      = {0171-2985},
  pages     = {277 -- 289},
  year      = {1999},
  language  = {en}
}
@article{HandtkeSchroeterJuergenetal.2014,
  author    = {Handtke, Stefan and Schroeter, Rebecca and J{\"u}rgen, Britta and Methling, Karen and Schl{\"u}ter, Rabea and Albrecht, Dirk and Hijum, Sacha A. F. T. van and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Schweder, Thomas and Hecker, Michael and Voigt, Birgit},
  title     = {Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress},
  series = {PLOS one},
  volume    = {9},
  journal   = {PLOS one},
  number    = {1},
  publisher = {PLOS},
  address   = {San Francisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0085625},
  pages     = {e85625},
  year      = {2014},
  abstract  = {Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.},
  language  = {en}
}