@article{KramerHalamkovaPoghossianetal.2013,
  author    = {Kramer, Friederike and Halamkova, Lenka and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Katz, Evgeny and Halamek, Jan},
  title     = {Biocatalytic analysis of biomarkers for forensic identification of ethnicity between Caucasian and African American},
  series = {The analyst. August 2013},
  volume    = {Vol. 138},
  journal   = {The analyst. August 2013},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-5528 (E-Journal); 0003-2654 (Print)},
  pages     = {6251 -- 6257},
  year      = {2013},
  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}
}
@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}
}
@article{LuethThustSteffenetal.2000,
  author    = {L{\"u}th, H. and Thust, M. and Steffen, A. and Kordos, P. and Sch{\"o}ning, Michael Josef},
  title     = {Biochemical sensors with structured and porous silicon capacitors},
  series = {Materials Science and Engineering B. 69-70 (2000)},
  journal   = {Materials Science and Engineering B. 69-70 (2000)},
  isbn      = {0921-5107},
  pages     = {104 -- 108},
  year      = {2000},
  language  = {en}
}
@article{AkimbekovDigelTastambeketal.2013,
  author    = {Akimbekov, N. S. and Digel, Ilya and Tastambek, K. T. and Zhubanova, A. A.},
  title     = {Biocompatibility of carbonized rice husk with a rat heart cells line H9c2},
  series = {Experimental Biology},
  volume    = {59},
  journal   = {Experimental Biology},
  number    = {3/1},
  issn      = {1563-0218},
  pages     = {23 -- 25},
  year      = {2013},
  language  = {en}
}
@incollection{MansurovJandosovChenchiketal.2020,
  author    = {Mansurov, Zulkhair A. and Jandosov, Jakpar and Chenchik, D. and Azat, Seitkhan and Savitskaya, Irina S. and Kistaubaeva, Aida and Akimbekov, Nuraly and Digel, Ilya and Zhubanova, Azhar Achmet},
  title     = {Biocomposite Materials Based on Carbonized Rice Husk in Biomedicine and Environmental Applications},
  series = {Carbon Nanomaterials in Biomedicine and the Environment},
  booktitle = {Carbon Nanomaterials in Biomedicine and the Environment},
  publisher = {Jenny Stanford Publishing Pte. Ltd.},
  address   = {Singapore},
  isbn      = {978-981-4800-27-3},
  doi       = {10.1201/9780429428647-2},
  pages     = {3 -- 32},
  year      = {2020},
  abstract  = {This chapter describes the prospects for biomedical and environmental engineering applications of heterogeneous materials based on nanostructured carbonized rice husk. Efforts in engineering enzymology are focused on the following directions: development and optimization of immobilization methods leading to novel biotechnological and biomedical applications; construction of biocomposite materials based on individual enzymes, multi-enzyme complexes and whole cells, targeted on realization of specific industrial processes. Molecular biological and biochemical studies on cell adhesion focus predominantly on identification, isolation and structural analysis of attachment-responsible biological molecules and their genetic determinants. The chapter provides a short overview of applications of the biocomposite materials based of nanostructured carbonized adsorbents. It emphasizes that further studies and better understanding of the interactions between CNS and microbial cells are necessary. The future use of living cells as biocatalysts, especially in the environmental field, needs more systematic investigations of the microbial adsorption phenomenon.},
  language  = {en}
}
@article{SchrothWeissbeckerSchuetzetal.2002,
  author    = {Schroth, P. and Weißbecker, B. and Sch{\"u}tz, S. and Ecken, H. and Yoshinobu, T. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef},
  title     = {Bioelectronic signal processing - intact chemoreceptors coupled to field-effect devices},
  series = {Lecture Notes of the ICB Seminars},
  journal   = {Lecture Notes of the ICB Seminars},
  publisher = {MCB},
  address   = {Warsaw},
  pages     = {28 -- 42},
  year      = {2002},
  language  = {en}
}
@article{SchrothWeissbeckerSchuetzetal.2001,
  author    = {Schroth, P. and Weißbecker, B. and Sch{\"u}tz, S. and Ecken, H. and Yoshinobu, T. and L{\"u}th, H. and Sch{\"o}ning, Michael Josef},
  title     = {Bioelectronic signal processing - intact chemoreceptors coupled to field-effect devices},
  series = {Biocybernetics and Biomedical Engineering. 21 (2001), H. 3},
  journal   = {Biocybernetics and Biomedical Engineering. 21 (2001), H. 3},
  isbn      = {0208-5216},
  pages     = {27 -- 42},
  year      = {2001},
  language  = {en}
}
@book{Artmann2008,
  author    = {Artmann, Gerhard},
  title     = {Bioengineering in Cell and Tissue Research / Artmann, Gerhard M. ; Chien, Shu (Eds.)},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {978-3-540-75408-4},
  year      = {2008},
  language  = {en}
}