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O'Connell, Timothy ; Siegert, Petra ; Evers, Stefan ; Bongaerts, Johannes ; Weber, Thomas ; Maurer, Karl-Heinz ; Bessler, Cornelius
Siegert, Petra ; Baumstark, Rebecca ; Kluin, Cornelia ; O'Connell, Timothy ; Maurer, Karl-Heinz ; Hellmuth, Hendrik
Lagerstabiles flüssiges Wasch- oder Reinigungsmittel enthaltend Proteasen [Offenlegungsschrift]
(2011)
Wieland, Susanne ; Siegert, Petra ; Spitz, Astrid ; Maurer, Karl-Heinz ; O'Connell, Timothy ; Prüser, Inken ; Schiedel, Marc-Steffen ; Eiting, Thomas ; Sendor-Müller, Dorota ; Bastigkeit, Thorsten ; Benda, Konstantin ; Müller, Sven
Siegert, Petra ; Schwaneberg, Ulrich ; Martinez Moya, Ronny ; Merkel, Marion ; Spitz, Astrid ; Wieland, Susanne ; Hellmuth, Hendrik ; Maurer, Karl-Heinz
Siegert, Petra ; Merkel, Marion ; Kluin, Cornelia ; Maurer, Karl-Heinz ; O'Connell, Timothy ; Wieland, Susanne ; Hellmuth, Hendrik
Maurer, Karl-Heinz ; O'Connell, Timothy ; Siegert, Petra ; Weber, Thomas ; Tondera, Susanne ; Hellmuth, Hendrik
Siegert, Petra ; Evers, Stefan ; Marion, Merkel ; Mussmann, Nina ; Hellmuth, Hendrik ; O'Connell, Timothy ; Maurer, Karl-Heinz ; Schwaneberg, Ulrich ; Martinez, Ronny ; Jakob, Felix
Iding, Hans ; Dünnwald, Thomas ; Greiner, Lasse ; Liese, Andreas ; Müller, Michael ; Siegert, Petra ; Grötzinger, Joachim ; Demir, Ayhan S. ; Pohl, Martina
Siegert, Petra ; Iding, Hans ; Baumann, Martin ; McLeish, Michael J. ; Kenyon, George L. ; Pohl, Martina
Dünkelmann, Pascal ; Kolter-Jung, Doris ; Nitsche, Adam ; Demir, Ayhan S. ; Siegert, Petra ; Lingen, Bettina ; Baumann, Martin ; Pohl, Martina ; Müller, Michael
Siegert, Petra ; Pohl, Martina ; Kneen, Malea M. ; Pogozheva, Irina D. ; Kenyon, George L. ; McLeish, Michael J.
Siegert, Petra ; McLeish, Michael J. ; Baumann, Martin ; Iding, Hans ; Kneen, Malea M. ; Kenyon, George L. ; Pohl, Martina
Wendorff, Marion ; Eggert, Thorsten ; Pohl, Martina ; Dresen, Carola ; Müller, Michael ; Jaeger, Karl-Erich ; Sprenger, Georg A. ; Schürmann, Melanie ; Schürmann, Martin ; Johnen, Sandra ; Sprenger, Gerda ; Sahm, Hermann ; Inoue, Tomoyuki ; Schörken, Ulrich ; Breittaupt, Holger ; Frölich, Bettina ; Heim, Petra ; Iding, Hans ; Juchem, Bettina ; Siegert, Petra ; Kula, Maria-Regina ; Weckbecker, Andrea ; Hummel, Werner ; Fessner, Wolf-Dieter ; Elling, Lothar ; Wolberg, Michael ; Bode, Silke ; Feldmann, Ralf ; Geilenkirchen, Petra ; Schubert, Thomas ; Walter, Lydia ; Dünnwald, Thomas ; Demir, Ayhan S. ; Kolter-Jung, Doris ; Nitsche, Adam ; Dünkelmann, Pascal ; Cosp, Annabel ; Lingen, Bettina
C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli
(2010)
Ribitsch, D. ; Karl, W. ; Birner-Gruenberger, R. ; Gruber, K. ; Eiteljoerg, I. ; Remler, P. ; Wieland, S. ; Siegert, Petra ; Maurer, Karl-Heinz ; Schwab, H.
Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477.
This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7–11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.
Ribitsch, D. ; Heumann, S. ; Karl, W. ; Gerlach, J. ; Leber, R. ; Birner-Gruenberger, R. ; Gruber, K. ; Eiteljoerg, I. ; Remler, P. ; Siegert, Petra ; Lange, J. ; Maurer, Karl-Heinz ; Berg, G. ; Guebitz, G. M. ; Schwab, H.
A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3.
From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.
Jakob, Felix ; Martinez, Ronny ; Mandawe, John ; Hellmuth, Hendrik ; Siegert, Petra ; Maurer, Karl-Heinz ; Schwaneberg, Ulrich
Martinez, Ronny ; Jakob, Felix ; Tu, Ran ; Siegert, Petra ; Maurer, Karl-Heinz ; Schwaneberg, Ulrich
Whitehead, Mark ; Öhlschläger, Peter ; Almajhdi, Fahad N. ; Alloza, Leonor ; Marzábal, Pablo ; Meyers, Ann E. ; Hitzeroth, Inga I. ; Rybicki, Edward P.
Schöning, Michael Josef ; Biselli, Manfred ; Selmer, Thorsten ; Öhlschläger, Peter ; Baumann, Marcus ; Förster, Arnold ; Poghossian, Arshak
"Biologie trifft Mikroelektronik", das Motto des Instituts für Nano- und Biotechnologien (INB) an der FH Aachen, unterstreicht die zunehmende Bedeutung interdisziplinär geprägter Forschungsaktivitäten. Der thematische Zusammenschluss grundständiger Disziplinen, wie die Physik, Elektrotechnik, Chemie, Biologie sowie die Materialwissenschaften, lässt neue Forschungsgebiete entstehen, ein herausragendes Beispiel hierfür ist die Nanotechnologie: Hier werden neue Werkstoffe und Materialien entwickelt, einzelne Nanopartikel oder Moleküle und deren Wechselwirkung untersucht oder Schichtstrukturen im Nanometerbereich aufgebaut, die neue und vorher nicht bekannte Eigenschaften hervorbringen.
Vor diesem Hintergrund bündelt das im Jahre 2006 gegründete INB die an der FH Aachen vorhandenen Kompetenzen von derzeit insgesamt sieben Laboratorien auf den Gebieten der Halbleitertechnik und Nanoelektronik, Nanostrukturen und DNA-Sensorik, der Chemo- und Biosensorik, der Enzymtechnologie, der Mikrobiologie und Pflanzenbiotechnologie, der Zellkulturtechnik, sowie der Roten Biotechnologie synergetisch. In der Nano- und Biotechnologie steckt außergewöhnliches Potenzial! Nicht zuletzt deshalb stellen sich die Forscher der Herausforderung, in diesem Bereich gemeinsam zu forschen und Schnittstellen zu nutzen, um so bei der Gestaltung neuartiger Ideen und Produkte mitzuwirken, die zukünftig unser alltägliches Leben verändern werden.
Im Folgenden werden die verschiedenen Forschungsbereiche kurz zusammenfassend vorgestellt und vorhandene Interaktionen anhand von exemplarisch ausgewählten, aktuellen Forschungsprojekten skizziert.
Nachdenklichkeit über Nachhaltigkeit : wie uns ein neues Wort alte Probleme neu entdecken läßt
(1997)
Differentiation between Phaeocystis pouchetii (Har.) Lagerheim and Phaeocystis globosa Scherffel
(1987)
Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer
(2014)
Küppers, Tobias ; Steffen, Victoria ; Hellmuth, Hendrik ; O'Connell, Timothy ; Bongaerts, Johannes ; Maurer, Karl-Heinz ; Wiechert, Wolfgang
Takenaga, Shoko ; Biselli, Manfred ; Schnitzler, Thomas ; Öhlschläger, Peter ; Wagner, Torsten ; Schöning, Michael Josef
The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17–200 mM) follows a Michaelis–Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.
The light-addressable potentiometric sensor (LAPS) is a semiconductor-based potentiometric sensor using a light probe with an ability of detecting the concentration of biochemical species in a spatially resolved manner. As an important biomedical sensor, research has been conducted to improve its performance, for instance, to realize high-speed measurement. In this work, the idea of facilitating the device-level simulation, instead of using an equivalent-circuit model, is presented for detailed analysis and optimization of the performance of the LAPS. Both carrier distribution and photocurrent response have been simulated to provide new insight into both amplitude-mode and phase-mode operations of the LAPS. Various device parameters can be examined to effectively design and optimize the LAPS structures and setups for enhanced performance.