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Breuer, Lars ; Raue, Markus ; Kirschbaum, M. ; Mang, Thomas ; Schöning, Michael Josef ; Thoelen, R. ; Wagner, Torsten
Poly(N-isopropylacrylamide) (PNIPAAm) hydrogel films with incorporated graphene oxide (GO) were developed and tested as light-stimulated actuators. GO dispersions were synthesized via Hummers method and characterized toward their optical properties and photothermal energy conversion. The hydrogels were prepared by means of photopolymerization. In addition, the influence of GO within the hydrogel network on the lower critical solution temperature (LCST) was investigated by differential scanning calorimetry (DSC). The optical absorbance and the response to illumination were determined as a function of GO concentration for thin hydrogel films. A proof of principle for the stimulation with light was performed.
An enzyme-based multi-parameter biosensor is developed for monitoring the concentration of formate, d-lactate, and l-lactate in biological samples. The sensor is based on the specific dehydrogenation by an oxidized β-nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenase (formate dehydrogenase, d-lactic dehydrogenase, and l-lactic dehydrogenase, respectively) in combination with a diaphorase from Clostridium kluyveri (EC 1.8.1.4). The enzymes are immobilized on a platinum working electrode by cross-linking with glutaraldehyde (GA). The principle of the determination scheme in case of l-lactate is as follows: l-lactic dehydrogenase (l-LDH) converts l-lactate into pyruvate by reaction with NAD+. In the presence of hexacyanoferrate(III), the resulting reduced β-nicotinamide adenine dinucleotide (NADH) is then regenerated enzymatically by diaphorase. The electrochemical detection is based on the current generated by oxidation of hexacyanoferrate(II) at an applied potential of +0.3 V vs. an Ag/AgCl reference electrode. The biosensor will be electrochemically characterized in terms of linear working range and sensitivity. Additionally, the successful practical application of the sensor is demonstrated in an extract from maize silage.
Seifarth, Volker ; Goßmann, Matthias ; Grosse, J. O. ; Becker, C. ; Heschel, I. ; Artmann, Gerhard ; Temiz Artmann, Aysegül
Raue, Markus ; Wambach, M. ; Glöggler, S. ; Grefen, Dana ; Kaufmann, R. ; Abetz, C. ; Georgopanos, P. ; Handge, U. A. ; Mang, Thomas ; Blümich, B. ; Abetz, V.
Handtke, Stefan ; Volland, Sonja ; Methling, Karen ; Albrecht, Dirk ; Becher, Dörte ; Nehls, Jenny ; Bongaerts, Johannes ; Maurer, Karl-Heinz ; Lalk, Michael ; Liesegang, Heiko ; Voigt, Birgit ; Daniel, Rolf ; Hecker, Michael
Members of the species Bacillus pumilus get more and more in focus of the biotechnological industry as potential new production strains. Based on exoproteome analysis, B. pumilus strain Jo2, possessing a high secretion capability, was chosen for an omics-based investigation. The proteome and metabolome of B. pumilus cells growing either in minimal or complex medium was analyzed. In total, 1542 proteins were identified in growing B. pumilus cells, among them 1182 cytosolic proteins, 297 membrane and lipoproteins and 63 secreted proteins. This accounts for about 43% of the 3616 proteins encoded in the B. pumilus Jo2 genome sequence. By using GC–MS, IP-LC/MS and H NMR methods numerous metabolites were analyzed and assigned to reconstructed metabolic pathways. In the genome sequence a functional secretion system including the components of the Sec- and Tat-secretion machinery was found. Analysis of the exoproteome revealed secretion of about 70 proteins with predicted secretion signals. In addition, selected production-relevant genome features such as restriction modification systems and NRPS clusters of B. pumilus Jo2 are discussed.
Frotscher, Ralf ; Goßmann, Matthias ; Raatschen, Hans-Jürgen ; Temiz Artmann, Aysegül ; Staat, Manfred
We present an electromechanically coupled Finite Element model for cardiac tissue. It bases on the mechanical model for cardiac tissue of Hunter et al. that we couple to the McAllister-Noble-Tsien electrophysiological model of purkinje fibre cells. The corresponding system of ordinary differential equations is implemented on the level of the constitutive equations in a geometrically and physically nonlinear version of the so-called edge-based smoothed FEM for plates. Mechanical material parameters are determined from our own pressure-deflection experimental setup. The main purpose of the model is to further examine the experimental results not only on mechanical but also on electrophysiological level down to ion channel gates. Moreover, we present first drug treatment simulations and validate the model with respect to the experiments.
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.