TY - JOUR
A1 - Feuerriegel, Uwe
A1 - Künsch, M.
A1 - Stahlberg, R.
A1 - Steiger, F.
T1 - Massen- und Energiebilanz des Thermoselect-Verfahrens
JF - Thermoselect-Verfahren zur Ent- und Vergasung von Abfällen / Franz J. Schweitzer [Hrsg.]
Y1 - 1994
SN - 3-924511-47-0
PB - EF-Verl. für Energie- u. Umwelttechnik
CY - Berlin
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
A1 - Klose, W.
A1 - Sloboshanin, S.
A1 - Goebel, H. [u.a.]
T1 - Deactivation of a palladium-supported alumina catalyst by hydrogen sulfide during the oxidation of methane
JF - Langmuir: the ACS journal of surfaces and colloids. 10 (1994), H. 10
Y1 - 1994
SN - 0743-74363
SP - 3567
EP - 3570
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
A1 - Klose, W.
T1 - Reaktionskinetik der katalytischen Methan-Oxidation und experimentelle Untersuchungen zur Desaktivierung eines Palladium-Trägerkatalysators durch Schwefelwasserstoff. Klose, W. ; Feuerriegel, U.
JF - Chemie - Ingenieur - Technik. 65 (1993), H. 10
Y1 - 1993
SN - 0009-286X
N1 - engl. Titel: Reaction Kinetics of Catalytic Methane Oxidation and Deactivation of a Palladium Catalyst by Hydrogen Sulfide During Catalytic Oxidation of Methane
SP - 1242
EP - 1243
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
A1 - Klose, W.
T1 - Untersuchungen zum Mechanismus der Desaktivierung eines Palladium-Trägerkatalysators durch Vergiftung mit Schwefelwasserstoff
JF - Chemie - Ingenieur - Technik. 70 (1998), H. 4
Y1 - 1998
SN - 0009-286X
N1 - Artikel in Englisch unter Chemical engineering & technology. 21(1998)7. S. 562-564
SP - 449
EP - 452
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
A1 - Klose, W.
T1 - Investigations into the Mechanism of the Deactivation of a Palladium-Supported Catalyst by Hydrogen Sulfide Poisoning. Klose, W. ; Feuerriegel, U.
JF - Chemical engineering & technology. 21 (1998), H. 7
Y1 - 1998
SN - 0930-7516
N1 - gleicher Artikel in Deutsch In: Chem.Ing.Tech 70(1998) No S. 449-452 u.d.T.: Untersuchungen zum Mechanismus der Desaktivierung eines Palladium-Trägerkatalysators durch Vergiftung mit Schwefelwasserstoff
SP - 562
EP - 564
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
A1 - Hoffmann, Ulrich
A1 - Walenzik, C.
A1 - Kögel, J.
T1 - Für Scale-up´s und Betriebsmuster, Projekt Trocknungstechnik an der FH Aachen
JF - CITplus : das Praxismagazin für Verfahrenstechnik und Apparatebau. 4 (2001)
Y1 - 2001
SN - 1436-2597
SP - 24
EP - 25
ER -
TY - BOOK
A1 - Feuerriegel, Uwe
T1 - Zur Desaktivierung eines Desaktivierung eines Palladium-Trägerkatalysators durch Schwefel¬wasserstoff bei der katalytischen Methanoxidation
Y1 - 1993
N1 - Dissertation
PB - Univ.-Gesamthochsch.
CY - Kassel
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
T1 - Energetische Verwertung von Kunststoffabfällen
JF - Chemie und Technologie makromolekularer Stoffe :, 16. Kolloquium. / Fachhochschule / Fachbereich Chemieingenieurwesen. 20. November 1998 an der FH Aachen, Fachbereich Chemieingenieurwesen
Y1 - 1998
N1 - FH-Texte. 69; In Jülich unter der Signatur: 61 ZOW 405-16
SP - 169
EP - 189
PB - Fachhochschule Aachen
CY - Aachen
ER -
TY - JOUR
A1 - Feuerriegel, Uwe
T1 - Trennen und Trocknen. FH Aachen verfügt über einen Zentrifugentrockner im Technikumsmaßstab
JF - Lebensmitteltechnik. 33 (2001), H. 7-8
Y1 - 2001
SN - 0047-4290
SP - 22
EP - 23
ER -
TY - BOOK
A1 - Feuerriegel, Uwe
T1 - Verfahrenstechnik mit EXCEL: Verfahrenstechnische Berechnungen effektiv durchführen und professionell dokumentieren
Y1 - 2016
SN - 978-3-658-02902-9
U6 - https://doi.org/10.1007/978-3-658-02903-6
N1 - 152 Abbildungen, 94 Abbildungen in Farbe
Gedruckt in der Bibliothek unter der Signatur: 21 ZNK 11
PB - Springer Fachmedien
CY - Wiesbaden
ER -
TY - JOUR
A1 - Feng, Yong-Qing
A1 - Seibler, Jost
A1 - Alami, Raouf
A1 - Eisen, Andrew
A1 - Westerman, Karen A.
A1 - Leboulch, Philippe
A1 - Fiering, Steven
A1 - Bouhassira, Eric E.
T1 - Site-specific chromosomal integration in mammalian cells: highly efficient CRE recombinase-mediated cassette exchange
JF - Journal of Molecular Biology
Y1 - 1999
U6 - https://doi.org/10.1006/jmbi.1999.3113
SN - 0022-2836
VL - 292
IS - 4
SP - 779
EP - 785
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 - Everaers, Ralf
A1 - Karimi-Varzaneh, Hossein Ali
A1 - Fleck, Franz
A1 - Hojdis, Nils
A1 - Svaneborg, Carsten
T1 - Kremer–Grest Models for Commodity Polymer Melts: Linking Theory, Experiment, and Simulation at the Kuhn Scale
JF - Macromolecules
N2 - The Kremer–Grest (KG) polymer model is a standard model for studying generic polymer properties in molecular dynamics simulations. It owes its popularity to its simplicity and computational efficiency, rather than its ability to represent specific polymers species and conditions. Here we show that by tuning the chain stiffness it is possible to adapt the KG model to model melts of real polymers. In particular, we provide mapping relations from KG to SI units for a wide range of commodity polymers. The connection between the experimental and the KG melts is made at the Kuhn scale, i.e., at the crossover from the chemistry-specific small scale to the universal large scale behavior. We expect Kuhn scale-mapped KG models to faithfully represent universal properties dominated by the large scale conformational statistics and dynamics of flexible polymers. In particular, we observe very good agreement between entanglement moduli of our KG models and the experimental moduli of the target polymers.
Y1 - 2020
U6 - https://doi.org/10.1021/acs.macromol.9b02428
SN - 1520-5835
VL - 53
IS - 6
SP - 1901
EP - 1916
PB - ACS Publications
CY - Washington, DC
ER -
TY - CHAP
A1 - Engel, Mareike
A1 - Thieringer, Julia
A1 - Tippkötter, Nils
T1 - Linking bioprocess engineering and electrochemistry for sustainable biofuel production
T2 - Young Researchers Symposium, YRS 2016. Proceedings
N2 - Electromicrobial engineering is an emerging, highly interdisciplinary research area linking bioprocesses with electrochemistry. In this work, microbial electrosynthesis (MES) of biobutanol is carried out during acetone-butanol-ethanol (ABE) fermentations with Clostridium acetobutylicum. A constant electric potential of −600mV (vs. Ag/AgCl) with simultaneous addition of the soluble redox mediator neutral red is used in order to study the electron transfer between the working electrode and the bacterial cells. The results show an earlier initiation of solvent production for all fermentations with applied potential compared to the conventional ABE fermentation. The f inal butanol concentration can be more than doubled by the application of a negative potential combined with addition of neutral red. Moreover a higher biofilm formation on the working electrode compared to control cultivations has been observed. In contrast to previous studies, our results also indicate that direct electron transfer (DET) might be possible with C. acetobutylicum. The presented results make microbial butanol production economically attractive and therefore support the development of sustainable production processes in the chemical industry aspired by the “Centre for resource-efficient chemistry and raw material change” as well as the the project “NanoKat” working on nanostructured catalysts in Kaiserslautern.
Y1 - 2016
N1 - Young Researchers Symposium, YRS 2016, 14th - 15th April 2016, Fraunhofer-Zentrum Kaiserslautern
SP - 49
EP - 53
PB - Fraunhofer Verlag
CY - Karlsruhe
ER -
TY - JOUR
A1 - Engel, Mareike
A1 - Holtmann, Dirk
A1 - Ulber, Roland
A1 - Tippkötter, Nils
T1 - Increased Biobutanol Production by Mediator‐Less Electro‐Fermentation
JF - Biotechnology Journal
N2 - A future bio-economy should not only be based on renewable raw materials but also in the raise of carbon yields of existing production routes. Microbial electrochemical technologies are gaining increased attention for this purpose. In this study, the electro-fermentative production of biobutanol with C. acetobutylicum without the use of exogenous mediators is investigated regarding the medium composition and the reactor design. It is shown that the use of an optimized synthetic culture medium allows higher product concentrations, increased biofilm formation, and higher conductivities compared to a synthetic medium supplemented with yeast extract. Moreover, the optimization of the reactor system results in a doubling of the maximum product concentrations for fermentation products. When a working electrode is polarized at −600 mV vs. Ag/AgCl, a shift from butyrate to acetone and butanol production is induced. This leads to an increased final solvent yield of Yᴀᴃᴇ = 0.202 gg⁻¹ (control 0.103 gg⁻¹), which is also reflected in a higher carbon efficiency of 37.6% compared to 23.3% (control) as well as a fourfold decrease in simplified E-factor to 0.43. The results are promising for further development of biobutanol production in bioelectrochemical systems in order to fulfil the principles of Green Chemistry.
Y1 - 2018
U6 - https://doi.org/10.1002/biot.201800514
SN - 1860-7314
VL - 14
IS - 4
PB - Wiley-VCH
CY - Weinheim
ER -
TY - JOUR
A1 - Engel, Mareike
A1 - Gemünde, Andre
A1 - Holtmann, Dirk
A1 - Müller-Renno, Christine
A1 - Ziegler, Christiane
A1 - Tippkötter, Nils
A1 - Ulber, Roland
T1 - Clostridium acetobutylicum’s connecting world: cell appendage formation in bioelectrochemical systems
JF - ChemElectroChem
N2 - Bacterial cell appendix formation supports cell-cell interaction, cell adhesion and cell movement. Additionally, in bioelectrochemical systems (BES), cell appendages have been shown to participate in extracellular electron transfer. In this work, the cell appendix formation of Clostridium acetobutylicum in biofilms of a BES are imaged and compared with conventional biofilms. Under all observed conditions, the cells possess filamentous appendages with a higher number and density in the BES. Differences in the amount of extracellular polymeric substance in the biofilms of the electrodes lead to the conclusion that the cathode can be used as electron donor and the anode as electron acceptor by C. acetobutylicum. When using conductive atomic force microscopy, a current response of about 15 nA is found for the cell appendages from the BES. This is the first report of conductivity for clostridial cell appendices and represents the basis for further studies on their role for biofilm formation and electron transfer.
Y1 - 2019
U6 - https://doi.org/10.1002/celc.201901656
SN - 2196-0216
VL - 7
IS - 2
SP - 414
EP - 420
PB - Wiley
CY - Weinheim
ER -
TY - JOUR
A1 - Engel, Mareike
A1 - Bayer, Hendrik
A1 - Holtmann, Dirk
A1 - Tippkötter, Nils
A1 - Ulber, Roland
T1 - Flavin secretion of Clostridium acetobutylicum in a bioelectrochemical system - Is an iron limitation involved?
JF - Bioelectrochemistry
Y1 - 2019
U6 - https://doi.org/10.1016/j.bioelechem.2019.05.014
SN - 1567-5394
IS - In Press, Accepted Manuscript
PB - Elsevier
CY - Amsterdam
ER -