@article{WiesenTippkoetterMuffleretal.2015, author = {Wiesen, Sebastian and Tippk{\"o}tter, Nils and Muffler, Kai and Suck, Kirstin and Sohling, Ulrich and Ruf, Friedrich and Ulber, Roland}, title = {Adsorption of fatty acids to layered double hydroxides in aqueous systems}, series = {Adsorption}, volume = {21}, journal = {Adsorption}, number = {6-7}, publisher = {Springer}, address = {Berlin}, pages = {459 -- 466}, year = {2015}, abstract = {Due to their anion exchange characteristics, layered double hydroxides (LDHs) are suitable for the detoxification of aqueous, fatty acid containing fermentation substrates. The aim of this study is to examine the adsorption mechanism, using crude glycerol from plant oil esterification as a model system. Changes in the intercalation structure in relation to the amount of fatty acids adsorbed are monitored by X-ray diffraction and infra-red spectroscopy. Additionally, calcination of LDH is investigated in order to increase the binding capacity for fatty acids. Our data propose that, at ambient temperature, fatty acids can be bound to the hydrotalcite by adsorption or in addition by intercalation, depending on fatty acid concentration. The adsorption of fatty acids from crude glycerol shows a BET-like behavior. Above a fatty acid concentration of 3.5 g L-1, intercalation of fatty acids can be shown by the appearance of an increased interlayer spacing. This observation suggests a two phase adsorption process. Calcination of LDHs allows increasing the binding capacity for fatty acids by more than six times, mainly by reduction of structural CO32-.}, language = {en} } @article{TippkoetterDuweWiesenetal.2014, author = {Tippk{\"o}tter, Nils and Duwe, Anna-Maria and Wiesen, Sebastian and Sieker, Tim and Ulber, Roland}, title = {Enzymatic hydrolysis of beech wood lignocellulose at high solid contents and its utilization as substrate for the production of biobutanol and dicarboxylic acids}, series = {Bioresource Technology}, volume = {167}, journal = {Bioresource Technology}, publisher = {Elsevier}, address = {Amsterdam}, doi = {10.1016/j.biortech.2014.06.052}, pages = {447 -- 455}, year = {2014}, abstract = {The development of a cost-effective hydrolysis for crude cellulose is an essential part of biorefinery developments. To establish such high solid hydrolysis, a new solid state reactor with static mixing is used. However, concentrations >10\% (w/w) cause a rate and yield reduction of enzymatic hydrolysis. By optimizing the synergetic activity of cellulolytic enzymes at solid concentrations of 9\%, 17\% and 23\% (w/w) of crude Organosolv cellulose, glucose concentrations of 57, 113 and 152 g L⁻¹ are reached. However, the glucose yield decreases from 0.81 to 0.72gg⁻¹ at 17\% (w/w). Optimal conditions for hydrolysis scale-up under minimal enzyme addition are identified. As result, at 23\% (w/w) crude cellulose the glucose yield increases from 0.29 to 0.49gg⁻¹. As proof of its applicability, biobutanol, succinic and itaconic acid are produced with the crude hydrolysate. The potential of the substrate is proven e.g. by a high butanol yield of 0.33gg⁻¹.}, language = {en} } @article{MuschallikMolinnusBongaertsetal.2017, author = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten}, title = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme}, series = {Journal of Biotechnology}, volume = {258}, journal = {Journal of Biotechnology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0168-1656}, doi = {10.1016/j.jbiotec.2017.07.020}, pages = {41 -- 50}, year = {2017}, abstract = {The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43\%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.}, language = {en} } @article{FigueroaMirandaFengShiuetal.2018, author = {Figueroa-Miranda, Gabriela and Feng, Lingyan and Shiu, Simon Chi-Chin and Dirkzwager, Roderick Marshall and Cheung, Yee-Wai and Tanner, Julian Alexander and Sch{\"o}ning, Michael Josef and Offenh{\"a}usser, Andreas and Mayer, Dirk}, title = {Aptamer-based electrochemical biosensor for highly sensitive and selective malaria detection with adjustable dynamic response range and reusability}, series = {Sensor and Actuators B: Chemical}, volume = {255}, journal = {Sensor and Actuators B: Chemical}, number = {P1}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0925-4005}, doi = {10.1016/j.snb.2017.07.117}, pages = {235 -- 243}, year = {2018}, abstract = {Malaria infection remains a significant risk for much of the population of tropical and subtropical areas, particularly in developing countries. Therefore, it is of high importance to develop sensitive, accurate and inexpensive malaria diagnosis tests. Here, we present a novel aptamer-based electrochemical biosensor (aptasensor) for malaria detection by impedance spectroscopy, through the specific recognition between a highly discriminatory DNA aptamer and its target Plasmodium falciparum lactate dehydrogenase (PfLDH). Interestingly, due to the isoelectric point (pI) of PfLDH, the aptasensor response showed an adjustable detection range based on the different protein net-charge at variable pH environments. The specific aptamer recognition allows sensitive protein detection with an expanded detection range and a low detection limit, as well as a high specificity for PfLDH compared to analogous proteins. The specific feasibility of the aptasensor is further demonstrated by detection of the target PfLDH in human serum. Furthermore, the aptasensor can be easily regenerated and thus applied for multiple usages. The robustness, sensitivity, and reusability of the presented aptasensor make it a promising candidate for point-of-care diagnostic systems.}, language = {en} } @article{MoraisGomesSilvaetal.2017, author = {Morais, Paulo V. and Gomes, Vanderley F., Jr. and Silva, Anielle C. A. and Dantas, Noelio O. and Sch{\"o}ning, Michael Josef and Siqueira, Jos{\´e} R., Jr.}, title = {Nanofilm of ZnO nanocrystals/carbon nanotubes as biocompatible layer for enzymatic biosensors in capacitive field-effect devices}, series = {Journal of Materials Science}, volume = {52}, journal = {Journal of Materials Science}, number = {20}, publisher = {Springer}, address = {Berlin}, issn = {1573-4803}, doi = {10.1007/s10853-017-1369-y}, pages = {12314 -- 12325}, year = {2017}, abstract = {The incorporation of nanomaterials that are biocompatible with different types of biological compounds has allowed the development of a new generation of biosensors applied especially in the biomedical field. In particular, the integration of film-based nanomaterials employed in field-effect devices can be interesting to develop biosensors with enhanced properties. In this paper, we studied the fabrication of sensitive nanofilms combining ZnO nanocrystals and carbon nanotubes (CNTs), prepared by means of the layer-by-layer (LbL) technique, in a capacitive electrolyte-insulator-semiconductor (EIS) structure for detecting glucose and urea. The ZnO nanocrystals were incorporated in a polymeric matrix of poly(allylamine) hydrochloride (PAH), and arranged with multi-walled CNTs in a LbL PAH-ZnO/CNTs film architecture onto EIS chips. The electrochemical characterizations were performed by capacitance-voltage and constant capacitance measurements, while the morphology of the films was characterized by atomic force microscopy. The enzymes glucose oxidase and urease were immobilized on film's surface for detection of glucose and urea, respectively. In order to obtain glucose and urea biosensors with optimized amount of sensitive films, we investigated the ideal number of bilayers for each detection system. The glucose biosensor showed better sensitivity and output signal for an LbL PAH-ZnO/CNTs nanofilm with 10 bilayers. On the other hand, the urea biosensor presented enhanced properties even for the first bilayer, exhibiting high sensitivity and output signal. The presence of the LbL PAH-ZnO/CNTs films led to biosensors with better sensitivity and enhanced response signal, demonstrating that the adequate use of nanostructured films is feasible for proof-of-concept biosensors with improved properties that may be employed for biomedical applications.}, language = {en} } @article{HonarvarfardGamellaPoghossianetal.2017, author = {Honarvarfard, Elham and Gamella, Maria and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Katz, Evgeny}, title = {An enzyme-based reversible Controlled NOT (CNOT) logic gate operating on a semiconductor transducer}, series = {Applied Materials Today}, volume = {9}, journal = {Applied Materials Today}, publisher = {Elsevier}, address = {Amsterdam}, issn = {2352-9407}, doi = {10.1016/j.apmt.2017.08.003}, pages = {266 -- 270}, year = {2017}, abstract = {An enzyme-based biocatalytic system mimicking operation of a logically reversible Controlled NOT (CNOT) gate has been interfaced with semiconductor electronic transducers. Electrolyte-insulator-semiconductor (EIS) structures have been used to transduce chemical changes produced by the enzyme system to an electronically readable capacitive output signal using field-effect features of the EIS device. Two enzymes, urease and esterase, were immobilized on the insulating interface of EIS structure producing local pH changes performing XOR logic operation controlled by various combinations of the input signals represented by urea and ethyl butyrate. Another EIS transducer was functionalized with esterase only, thus performing Identity (ID) logic operation for the ethyl butyrate input. Both semiconductor devices assembled in parallel operated as a logically reversible CNOT gate. The present system, despite its simplicity, demonstrated for the first time logically reversible function of the enzyme system transduced electronically with the semiconductor devices. The biomolecular realization of a CNOT gate interfaced with semiconductors is promising for integration into complex biomolecular networks and future biosensor/biomedical applications.}, language = {en} } @article{RoehlenPilasSchoeningetal.2017, author = {R{\"o}hlen, Desiree and Pilas, Johanna and Sch{\"o}ning, Michael Josef and Selmer, Thorsten}, title = {Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid}, series = {Applied Biochemistry and Biotechnology}, volume = {183}, journal = {Applied Biochemistry and Biotechnology}, publisher = {Springer}, address = {Berlin}, issn = {1559-0291}, doi = {10.1007/s12010-017-2578-1}, pages = {566 -- 581}, year = {2017}, abstract = {Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM-1 (L-malate biosensor) and 0.4 μA mM-1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0-10.0 mM with a sensitivity of 0.09 μA mM-1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates.}, language = {en} } @article{PilasYaziciSelmeretal.2017, author = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate}, series = {Electrochimica Acta}, volume = {251}, journal = {Electrochimica Acta}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0013-4686}, doi = {10.1016/j.electacta.2017.07.119}, pages = {256 -- 262}, year = {2017}, abstract = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.}, language = {en} } @article{SchoppDollGraeseretal.2016, author = {Schopp, Christoph and Doll, Timo and Gr{\"a}ser, Ulrich and Harzheim, Thomas and Heuermann, Holger and Kling, Rainer and Marso, Michael}, title = {Capacitively Coupled High-Pressure Lamp Using Coaxial Line Networks}, series = {IEEE Transactions on Microwave Theory and Techniques}, volume = {64}, journal = {IEEE Transactions on Microwave Theory and Techniques}, number = {10}, publisher = {IEEE}, address = {New York, NY}, issn = {0018-9480}, doi = {10.1109/TMTT.2016.2600326}, pages = {3363 -- 3368}, year = {2016}, abstract = {This paper describes the development of a capacitively coupled high-pressure lamp with input power between 20 and 43 W at 2.45 GHz, using a coaxial line network. Compared with other electrodeless lamp systems, no cavity has to be used and a reduction in the input power is achieved. Therefore, this lamp is an alternative to the halogen incandescent lamp for domestic lighting. To serve the demands of domestic lighting, the filling of the lamp is optimized over all other resulting requirements, such as high efficacy at low induced powers and fast startups. A workflow to develop RF-driven plasma applications is presented, which makes use of the hot S-parameter technique. Descriptions of the fitting process inside a circuit and FEM simulator are given. Results of the combined ignition and operation network from simulations and measurements are compared. An initial prototype is built and measurements of the lamp's lighting properties are presented along with an investigation of the efficacy optimizations using large signal amplitude modulation. With this lamp, an efficacy of 135 lmW -1 is achieved.}, language = {en} } @article{AlbannaLuekeSjapicetal.2017, author = {Albanna, Walid and Lueke, Jan Niklas and Sjapic, Volha and Kotliar, Konstantin and Hescheler, J{\"u}rgen and Clusmann, Hans and Sjapic, Sergej and Alpdogan, Serdan and Schneider, Toni and Schubert, Gerrit Alexander and Neumaier, Felix}, title = {Electroretinographic Assessment of Inner Retinal Signaling in the Isolated and Superfused Murine Retina}, series = {Current Eye Research}, journal = {Current Eye Research}, number = {Article in press}, publisher = {Taylor \& Francis}, address = {London}, issn = {1460-2202}, doi = {10.1080/02713683.2017.1339807}, pages = {1 -- 9}, year = {2017}, language = {en} } @article{SeifarthGrosseGrossmannetal.2017, author = {Seifarth, Volker and Grosse, Joachim O. and Grossmann, Matthias and Janke, Heinz Peter and Arndt, Patrick and Koch, Sabine and Epple, Matthias and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l}, title = {Mechanical induction of bi-directional orientation of primary porcine bladder smooth muscle cells in tubular fibrin-poly(vinylidene fluoride) scaffolds for ureteral and urethral repair using cyclic and focal balloon catheter stimulation}, series = {Journal of Biomaterials Applications}, volume = {32}, journal = {Journal of Biomaterials Applications}, number = {3}, publisher = {Sage}, address = {London}, issn = {1530-8022}, doi = {10.1177/0885328217723178}, pages = {321 -- 330}, year = {2017}, language = {en} } @article{SchifferFerrein2016, author = {Schiffer, Stefan and Ferrein, Alexander}, title = {Decision-Theoretic Planning with Fuzzy Notions in GOLOG}, series = {International Journal of Uncertainty, Fuzziness and Knowledge-Based Systems}, volume = {24}, journal = {International Journal of Uncertainty, Fuzziness and Knowledge-Based Systems}, number = {Issue Suppl. 2}, publisher = {World Scientific}, address = {Singapur}, issn = {1793-6411}, doi = {10.1142/S0218488516400134}, pages = {123 -- 143}, year = {2016}, abstract = {In this paper we present an extension of the action language Golog that allows for using fuzzy notions in non-deterministic argument choices and the reward function in decision-theoretic planning. Often, in decision-theoretic planning, it is cumbersome to specify the set of values to pick from in the non-deterministic-choice-of-argument statement. Also, even for domain experts, it is not always easy to specify a reward function. Instead of providing a finite domain for values in the non-deterministic-choice-of-argument statement in Golog, we now allow for stating the argument domain by simply providing a formula over linguistic terms and fuzzy uents. In Golog's forward-search DT planning algorithm, these formulas are evaluated in order to find the agent's optimal policy. We illustrate this in the Diner Domain where the agent needs to calculate the optimal serving order.}, language = {en} } @article{TippkoetterRoikaewUlber2008, author = {Tippk{\"o}tter, Nils and Roikaew, W. and Ulber, Roland}, title = {Nitrate removal from whey concentrate with biotechnological regeneration of the waste water}, series = {European dairy magazine : EDM}, journal = {European dairy magazine : EDM}, number = {1}, isbn = {0936-6318}, pages = {30 -- 32}, year = {2008}, language = {en} } @article{TippkoetterStueckmannKrolletal.2009, author = {Tippk{\"o}tter, Nils and St{\"u}ckmann, Henning and Kroll, Stephen and Winkelmann, Gunda and Noack, Udo and Scheper, Thomas and Ulber, Roland}, title = {A semi-quantitative dipstick assay for microcystin}, series = {Analytical and Bioanalytical Chemistry}, volume = {394}, journal = {Analytical and Bioanalytical Chemistry}, number = {3}, publisher = {springer}, address = {Berlin}, issn = {1618-2650}, doi = {10.1007/s00216-009-2750-8}, pages = {863 -- 869}, year = {2009}, abstract = {An immunochromatographic lateral flow dipstick assay for the fast detection of microcystin-LR was developed. Colloid gold particles with diameters of 40 nm were used as red-colored antibody labels for the visual detection of the antigen. The new dipstick sensor is capable of detecting down to 5 µg·l-1 (ppb; total inversion of the color signal) or 1 ppb (observation of color grading) of microcystin-LR. The course of the labeling reaction was observed via spectrometric wave shifts caused by the change of particle size during the binding of antibodies. Different stabilizing reagents showed that especially bovine serum albumin (BSA) and casein increase the assays sensitivity and the conjugate stability. Performance of the dipsticks was quantified by pattern processing of capture zone CCD images. Storage stability of dipsticks and conjugate suspensions over 115 days under different conditions were monitored. The ready-to-use dipsticks were successfully tested with microcystin-LR-spiked samples of outdoor drinking- and salt water and applied to the tissue of microcystin-fed mussels.}, language = {en} } @article{RietschPfaffenrotBitzetal.2017, author = {Rietsch, Stefan H. G. and Pfaffenrot, Viktor and Bitz, Andreas and Orzada, Stephan and Brunheim, Sascha and Lazik-Palm, Andrea and Theysohn, Jens M. and Ladd, Mark E. and Quick, Harald H. and Kraff, Oliver}, title = {An 8-channel transceiver 7-channel receive RF coil setup for high SNR ultrahigh-field MRI of the shoulder at 7T}, series = {Medical Physics}, journal = {Medical Physics}, number = {Article in press}, publisher = {Wiley}, address = {Hoboken}, issn = {0094-2405}, doi = {10.1002/mp.12612}, year = {2017}, language = {en} } @article{KotliarHauserOrtneretal.2017, author = {Kotliar, Konstantin and Hauser, Christine and Ortner, Marion and Muggenthaler, Claudia and Diehl-Schmid, Janine and Angermann, Susanne and Hapfelmeier, Alexander and Schmaderer, Christoph and Grimmer, Timo}, title = {Altered neurovascular coupling as measured by optical imaging: a biomarker for Alzheimer's disease}, series = {Scientific Reports}, volume = {7}, journal = {Scientific Reports}, number = {1}, publisher = {Springer Nature}, address = {Cham}, issn = {2045-2322}, doi = {10.1038/s41598-017-13349-5}, pages = {1 -- 11}, year = {2017}, language = {en} } @article{BreuerMangSchoeningetal.2017, author = {Breuer, Lars and Mang, Thomas and Sch{\"o}ning, Michael Josef and Thoelen, Ronald and Wagner, Torsten}, title = {Investigation of the spatial resolution of a laser-based stimulation process for light-addressable hydrogels with incorporated graphene oxide by means of IR thermography}, series = {Sensors and Actuators A: Physical}, volume = {268}, journal = {Sensors and Actuators A: Physical}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0924-4247}, doi = {10.1016/j.sna.2017.11.031}, pages = {126 -- 132}, year = {2017}, language = {en} } @article{DemmerChowdhurySelmeretal.2017, author = {Demmer, Julius K. and Chowdhury, Nilanjan Pal and Selmer, Thorsten and Ermler, Ulrich and Buckel, Wolfgang}, title = {The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile}, series = {Nature Communications}, volume = {8}, journal = {Nature Communications}, number = {1}, issn = {2041-1723}, doi = {10.1038/s41467-017-01746-3}, pages = {1 -- 10}, year = {2017}, language = {en} } @article{WerkhausenAlbrachtCroninetal.2017, author = {Werkhausen, Amelie and Albracht, Kirsten and Cronin, Neil J. and Meier, Rahel and Mojsen-Moeller, Jens and Seynnes, Olivier R.}, title = {Modulation of muscle-tendon interaction in the human triceps surae during an energy dissipation task}, series = {Journal of Experimental Biology}, volume = {220}, journal = {Journal of Experimental Biology}, number = {22}, issn = {0022-0949}, doi = {10.1242/jeb.164111}, pages = {4141 -- 4149}, year = {2017}, language = {en} } @article{FerreinSteinbauer2016, author = {Ferrein, Alexander and Steinbauer, Gerald}, title = {The Interplay of Aldebaran and RoboCup}, series = {KI - K{\"u}nstliche Intelligenz}, volume = {30}, journal = {KI - K{\"u}nstliche Intelligenz}, number = {3-4}, publisher = {Springer}, address = {Berlin}, issn = {1610-1987}, doi = {10.1007/s13218-016-0440-1}, pages = {325 -- 326}, year = {2016}, language = {en} }