TY - JOUR A1 - Fateri, Miranda A1 - Gebhardt, Andreas T1 - Selective Laser Melting of Soda-Lime Glass Powder JF - International Journal of Applied Ceramic Technology Y1 - 2015 U6 - https://doi.org/10.1111/ijac.12338 SN - 1744-7402 VL - 12 IS - 1 SP - 53 EP - 61 PB - Wiley-Blackwell CY - Oxford ER - TY - JOUR A1 - Fateri, Miranda A1 - Gebhardt, Andreas T1 - Process Parameters Development of Selective Laser Melting of Lunar Regolith for On-Site Manufacturing Applications JF - International Journal of Applied Ceramic Technology Y1 - 2015 SN - 1744-7402 U6 - https://doi.org/10.1111/ijac.12326 VL - 12 IS - 1 SP - 46 EP - 52 PB - Wiley-Blackwell CY - Oxford ER - TY - JOUR A1 - Falkenberg, Fabian A1 - Voß, Leonie A1 - Bott, Michael A1 - Bongaerts, Johannes A1 - Siegert, Petra T1 - New robust subtilisins from halotolerant and halophilic Bacillaceae JF - Applied Microbiology and Biotechnology N2 - The aim of the present study was the characterisation of three true subtilisins and one phylogenetically intermediate subtilisin from halotolerant and halophilic microorganisms. Considering the currently growing enzyme market for efficient and novel biocatalysts, data mining is a promising source for novel, as yet uncharacterised enzymes, especially from halophilic or halotolerant Bacillaceae, which offer great potential to meet industrial needs. Both halophilic bacteria Pontibacillus marinus DSM 16465ᵀ and Alkalibacillus haloalkaliphilus DSM 5271ᵀ and both halotolerant bacteria Metabacillus indicus DSM 16189 and Litchfieldia alkalitelluris DSM 16976ᵀ served as a source for the four new subtilisins SPPM, SPAH, SPMI and SPLA. The protease genes were cloned and expressed in Bacillus subtilis DB104. Purification to apparent homogeneity was achieved by ethanol precipitation, desalting and ion-exchange chromatography. Enzyme activity could be observed between pH 5.0–12.0 with an optimum for SPPM, SPMI and SPLA around pH 9.0 and for SPAH at pH 10.0. The optimal temperature for SPMI and SPLA was 70 °C and for SPPM and SPAH 55 °C and 50 °C, respectively. All proteases showed high stability towards 5% (w/v) SDS and were active even at NaCl concentrations of 5 M. The four proteases demonstrate potential for future biotechnological applications. KW - Biotechnological application KW - Bacillaceae KW - Subtilisin KW - Subtilases KW - Halotolerant protease Y1 - 2023 U6 - https://doi.org/10.1007/s00253-023-12553-w SN - 1432-0614 N1 - Corresponding author: Petra Siegert VL - 107 SP - 3939 EP - 3954 PB - Springer Nature CY - Berlin ER - TY - JOUR A1 - Falkenberg, Fabian A1 - Rahba, Jade A1 - Fischer, David A1 - Bott, Michael A1 - Bongaerts, Johannes A1 - Siegert, Petra T1 - Biochemical characterization of a novel oxidatively stable, halotolerant, and high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T JF - FEBS Open Bio N2 - 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. KW - Alkalihalobacillus okhensis KW - detergent protease KW - halotolerant protease KW - high-alkaline subtilisin KW - oxidative stable protease Y1 - 2022 U6 - https://doi.org/10.1002/2211-5463.13457 SN - 2211-5463 N1 - Corresponding author: Petra Siegert VL - 12 IS - 10 SP - 1729 EP - 1746 PB - Wiley CY - Hoboken, NJ ER - TY - JOUR A1 - Falkenberg, Fabian A1 - Kohn, Sophie A1 - Bott, Michael A1 - Bongaerts, Johannes A1 - Siegert, Petra T1 - Biochemical characterisation of a novel broad pH spectrum subtilisin from Fictibacillus arsenicus DSM 15822ᵀ JF - FEBS Open Bio N2 - 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. KW - Bacillaceae KW - Biotechnological application KW - Broad pH spectrum KW - Subtilases KW - Subtilisin Y1 - 2023 U6 - https://doi.org/10.1002/2211-5463.13701 SN - 2211-5463 N1 - Corresponding author: Petra Siegert VL - 13 IS - 11 SP - 2035 EP - 2046 PB - Wiley CY - Hoboken, NJ ER - TY - JOUR A1 - Falkenberg, Fabian A1 - Bott, Michael A1 - Bongaerts, Johannes A1 - Siegert, Petra T1 - Phylogenetic survey of the subtilase family and a data-mining-based search for new subtilisins from Bacillaceae JF - Frontiers in Microbiology N2 - The subtilase family (S8), a member of the clan SB of serine proteases are ubiquitous in all kingdoms of life and fulfil different physiological functions. Subtilases are divided in several groups and especially subtilisins are of interest as they are used in various industrial sectors. Therefore, we searched for new subtilisin sequences of the family Bacillaceae using a data mining approach. The obtained 1,400 sequences were phylogenetically classified in the context of the subtilase family. This required an updated comprehensive overview of the different groups within this family. To fill this gap, we conducted a phylogenetic survey of the S8 family with characterised holotypes derived from the MEROPS database. The analysis revealed the presence of eight previously uncharacterised groups and 13 subgroups within the S8 family. The sequences that emerged from the data mining with the set filter parameters were mainly assigned to the subtilisin subgroups of true subtilisins, high-alkaline subtilisins, and phylogenetically intermediate subtilisins and represent an excellent source for new subtilisin candidates. Y1 - 2022 U6 - https://doi.org/10.3389/fmicb.2022.1017978 SN - 1664-302X VL - 2022 IS - 13 PB - Frontiers CY - Lausanne ER - TY - JOUR A1 - Fagan, Andrew J. A1 - Bitz, Andreas A1 - Björkman-Burtscher, Isabella M. A1 - Collins, Christopher M. A1 - Kimbrell, Vera A1 - Raaijmakers, Alexander J. E. T1 - 7T MR Safety JF - Journal of Magnetic Resonance Imaging (JMRI) Y1 - 2021 U6 - https://doi.org/10.1002/jmri.27319 SN - 1522-2586 VL - 53 IS - 2 SP - 333 EP - 346 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Fabo, Sabine T1 - Babel heute : der internationale Dialog zwischen Kunst und Medien JF - UNESCO heute : Zeitschrift der Deutschen Unesco-Kommission Y1 - 1992 SN - 0937-924X VL - 39 (1992) SP - 379 EP - 381 ER - TY - JOUR A1 - Fabo, Sabine T1 - Ephemeriden : Mode, Kunst, Medien ; Strategien des Flüchtigen JF - Kunstforum international Y1 - 1998 SN - 0177-3674 VL - 1998 IS - 141 SP - 162 EP - 171 ER - TY - JOUR A1 - Fabo, Sabine T1 - Arts and media : towards an universal understanding JF - Leonardo Y1 - 1993 SN - 0024-094X VL - 26(1993) IS - 4 SP - 316 EP - 319 ER - TY - JOUR A1 - Fabo, Sabine T1 - Über Nahtgenossen und andere Verdächtige : Parasitenmode JF - Spex : das Magazin für Popkultur (2003) Y1 - 2003 SN - 0178-6830 SP - 64 EP - 65 ER - TY - JOUR A1 - Fabo, Sabine T1 - Roaratorio : John Cage JF - Diagonal : Zeitschrift der Universität Siegen Y1 - 1992 SN - 0938-7161 VL - 4(1992) IS - Heft "Experimente" SP - 201 EP - 210 CY - Siegen ER - TY - JOUR A1 - Fabo, Sabine T1 - Joseph Beuys und das Kapital : zur Erweiterung eines Begriffs JF - Diagonal : Zeitschrift der Universität Siegen Y1 - 1991 SN - 0938-7161 VL - 2 (1991) IS - Heft "Geld" SP - 145 EP - 152 ER - TY - JOUR A1 - Fabo, Sabine T1 - Entgrenzung und Vereinnahmung : zum Verhältnis von Kunst und Kunstbetrieb in den 80er Jahren JF - Aufbruch in die Neunziger : Ideen, Entwicklungen, Perspektiven der achtziger Jahre / Christian W. Thomsen (Hrsg.) Y1 - 1991 SN - 3-7701-2512-6 N1 - DuMont-Taschenbücher ; 254 SP - 303 EP - 333 PB - DuMont CY - Köln ER - TY - JOUR A1 - Fabo, Sabine ED - Mohr, Klaus T1 - Pepräsentatives Dösen JF - Idiopendent Lyfestile (Boxhorn ; 27) Y1 - 2013 SN - 1864-2535 SP - 134 EP - 139 PB - FH CY - Aachen ER - TY - JOUR A1 - Fabo, Sabine ED - Mohr, Klaus T1 - Sisyphus wird Steiff JF - Prädikat spießig (Boxhorn ; 21) N2 - Eine Reise durch die fremde Welt eines Kaufhaus-Schaufensters. Plüschtiere mit eingebauter Bewegungstechnik - knuffig oder nur eine Ausformulierung des Ernst des Lebens? Y1 - 2010 SN - 1864-2535 VL - 2010 SP - 58 EP - 61 PB - FH Aachen, Fachbereich Gestaltung CY - Aachen ER - TY - JOUR A1 - Fabo, Sabine T1 - Marti Guixé : Parasitisierung durch das Objekt als Fata Morgana der Funktion JF - Kunstforum international Y1 - 2007 SN - 0177-3674 N1 - Ein Gespräch von Sabine Fabo VL - 2007 IS - 185 SP - 164 ER - TY - JOUR A1 - Fabo, Sabine ED - Wirth, Jacob T1 - Das Parasitäre in der Pandemie JF - Parasite Art Y1 - 2022 IS - Issue 2 SP - 8 EP - 11 PB - Parasite Art ER - TY - JOUR A1 - Fabo, Sabine T1 - Chicks off speed JF - hello! (Boxhorn ; 19) KW - Hühnerzucht KW - Unterhaltung Y1 - 2013 SN - 1864-2535 VL - 2009 SP - 19 EP - 21 PB - FH Aachen, Fachbereich Gestaltung CY - Aachen ER - TY - JOUR A1 - Fabo, Sabine T1 - Sturz aus der Vogelperspektive JF - Sehsturz (Boxhorn ; 12) Y1 - 2005 VL - 2005 SP - 12 PB - FH Aachen, Fachbereich Gestaltung CY - Aachen ER -