@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{TippkoetterWollnySucketal.2014, author = {Tippk{\"o}tter, Nils and Wollny, Steffen and Suck, Kirstin and Sohling, Ulrich and Ruf, Friedrich and Ulber, Roland}, title = {Recycling of spent oil bleaching earth as source of glycerol for the anaerobic production of acetone, butanol, and ethanol with Clostridium diolis and lipolytic Clostridium lundense}, series = {Engineering in Life Sciences}, volume = {14}, journal = {Engineering in Life Sciences}, number = {4}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1618-2863}, doi = {10.1002/elsc.201300113}, pages = {425 -- 432}, year = {2014}, abstract = {A major part of edible oil is subjected to bleaching procedures, primarily with minerals applied as adsorbers. Their recycling is currently done either by regaining the oil via organic solvent extraction or by using the spent bleaching earth (SBE) as additive for animal feed, etc. As a new method, the reutilization of the by-product SBE for the microbiologic formation of acetone, butanol, and ethanol (ABE) is presented as proof-of-concept. The SBE was taken from a palm oil cleaning process. The recycling concept is based on the application of lipolytic clostridia strains. Due to considerably long fermentation times, co-fermentation with Candida rugosa and enzymatic hydrolyses of the bound oil with a subsequent clostridia fermentation are shown as alternative routes. Anaerobic fermentations under comparison of different clostridia strains were performed with glycerol media, enzymatically hydrolyzed palm oil and SBE. Solutes, side product compositions and productivities were quantified via HPLC. A successful production of ABE solutes from SBE has been done with a yield of 0.15 g butanol per gram of bound glycerol. Thus, the biotechnological recycling of the waste stream is possible in principle. Inhibition of the substrate suspension has been observed. A chromatographic ion-exchange of substrates increased the biomass concentration.}, language = {en} } @article{BaeckerDellePoghossianetal.2011, author = {B{\"a}cker, Matthias and Delle, L. and Poghossian, Arshak and Biselli, Manfred and Zang, Werner and Wagner, P. and Sch{\"o}ning, Michael Josef}, title = {Electrochemical sensor array for bioprocess monitoring}, series = {Electrochimica Acta (2011)}, volume = {56}, journal = {Electrochimica Acta (2011)}, number = {26}, publisher = {Elsevier}, address = {Amsterdam}, pages = {9673 -- 9678}, year = {2011}, language = {en} } @article{BaeckerRaueSchusseretal.2012, author = {B{\"a}cker, Matthias and Raue, Markus and Schusser, Sebastian and Jeitner, C. and Breuer, L. and Wagner, P. and Poghossian, Arshak and F{\"o}rster, Arnold and Mang, Thomas and Sch{\"o}ning, Michael Josef}, title = {Microfluidic chip with integrated microvalves based on temperature- and pH-responsive hydrogel thin films}, series = {Physica Status Solidi (a)}, volume = {209}, journal = {Physica Status Solidi (a)}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201100763}, pages = {839 -- 845}, year = {2012}, abstract = {Two types of microvalves based on temperature-responsive poly(N-isopropylacrylamide) (PNIPAAm) and pH-responsive poly(sodium acrylate) (PSA) hydrogel films have been developed and tested. The PNIPAAm and PSA hydrogel films were prepared by means of in situ photopolymerization directly inside the fluidic channel of a microfluidic chip fabricated by combining Si and SU-8 technologies. The swelling/shrinking properties and height changes of the PNIPAAm and PSA films inside the fluidic channel were studied at temperatures of deionized water from 14 to 36 °C and different pH values (pH 3-12) of Titrisol buffer, respectively. Additionally, in separate experiments, the lower critical solution temperature (LCST) of the PNIPAAm hydrogel was investigated by means of a differential scanning calorimetry (DSC) and a surface plasmon resonance (SPR) method. Mass-flow measurements have shown the feasibility of the prepared hydrogel films to work as an on-chip integrated temperature- or pH-responsive microvalve capable to switch the flow channel on/off.}, language = {en} } @article{WeldenPoghossianVahidpouretal.2022, author = {Welden, Melanie and Poghossian, Arshak and Vahidpour, Farnoosh and Wendlandt, Tim and Keusgen, Michael and Wege, Christina and Sch{\"o}ning, Michael Josef}, title = {Towards multi-analyte detection with field-effect capacitors modified with tobacco mosaic virus bioparticles as enzyme nanocarriers}, series = {Biosensors}, volume = {12}, journal = {Biosensors}, number = {1}, publisher = {MDPI}, address = {Basel}, issn = {2079-6374}, doi = {10.3390/bios12010043}, pages = {Artikel 43}, year = {2022}, abstract = {Utilizing an appropriate enzyme immobilization strategy is crucial for designing enzyme-based biosensors. Plant virus-like particles represent ideal nanoscaffolds for an extremely dense and precise immobilization of enzymes, due to their regular shape, high surface-to-volume ratio and high density of surface binding sites. In the present work, tobacco mosaic virus (TMV) particles were applied for the co-immobilization of penicillinase and urease onto the gate surface of a field-effect electrolyte-insulator-semiconductor capacitor (EISCAP) with a p-Si-SiO₂-Ta₂O₅ layer structure for the sequential detection of penicillin and urea. The TMV-assisted bi-enzyme EISCAP biosensor exhibited a high urea and penicillin sensitivity of 54 and 85 mV/dec, respectively, in the concentration range of 0.1-3 mM. For comparison, the characteristics of single-enzyme EISCAP biosensors modified with TMV particles immobilized with either penicillinase or urease were also investigated. The surface morphology of the TMV-modified Ta₂O₅-gate was analyzed by scanning electron microscopy. Additionally, the bi-enzyme EISCAP was applied to mimic an XOR (Exclusive OR) enzyme logic gate.}, language = {en} } @article{WagnerBegingRotteretal.2007, author = {Wagner, Torsten and Beging, Stefan and Rotter, L. and Poghossian, Arshak and Biselli, Manfred and Zang, Werner and Sch{\"o}ning, Michael Josef}, title = {Online-Messsysteme f{\"u}r die automatisierte Charakterisierung von feldeffektbasierten Biosensoren}, series = {8. Dresdner Sensor-Symposium : Sensoren f{\"u}r Umwelt, Klima und Sicherheit, Biosensoren und Biosysteme, Sensoren und Sensorsysteme f{\"u}r die Prozesstechnik, Trends in der Sensortechnik, Materialentwicklung f{\"u}r die Sensorik; 8. Dresdner Sensor-Symposium, 10. - 12. Dezember 2007, Dresden / Gerald Gerlach ... (Hg.)}, journal = {8. Dresdner Sensor-Symposium : Sensoren f{\"u}r Umwelt, Klima und Sicherheit, Biosensoren und Biosysteme, Sensoren und Sensorsysteme f{\"u}r die Prozesstechnik, Trends in der Sensortechnik, Materialentwicklung f{\"u}r die Sensorik; 8. Dresdner Sensor-Symposium, 10. - 12. Dezember 2007, Dresden / Gerald Gerlach ... (Hg.)}, publisher = {TUDpress, Verl. der Wissenschaften}, address = {Dresden}, isbn = {978-3-940046-45-1}, pages = {257 -- 260}, year = {2007}, language = {de} } @article{TeumerCapitainRossJonesetal.2018, author = {Teumer, T. and Capitain, C. and Ross-Jones, J. and Tippk{\"o}tter, Nils and R{\"a}dle, M. and Methner, F.-J.}, title = {In-line Haze Monitoring Using a Spectrally Resolved Back Scattering Sensor}, series = {BrewingScience}, volume = {71}, journal = {BrewingScience}, number = {5/6}, publisher = {Fachverlag Hans Carl}, address = {N{\"u}rnberg}, issn = {1613-2041}, pages = {49 -- 55}, year = {2018}, abstract = {In the present work an optical sensor in combination with a spectrally resolved detection device for in-line particle-size-monitoring for quality control in beer production is presented. The principle relies on the size and wavelength dependent backscatter of growing particles in fluids. Measured interference structures of backscattered light are compared with calculated theoretical values, based on Mie-Theory, and fitted with a linear least square method to obtain particle size distributions. For this purpose, a broadband light source in combination with a process-CCD-spectrometer (charge ? coupled device spectrometer) and process adapted fiber optics are used. The goal is the development of an easy and flexible measurement device for in-line-monitoring of particle size. The presented device can be directly installed in product fill tubes or vessels, follows CIP- (cleaning in place) and removes the need of sample taking. A proof of concept and preliminary results, measuring protein precipitation, are presented.}, language = {en} } @article{RoeschKratzHeringetal.2016, author = {R{\"o}sch, C. and Kratz, F. and Hering, T. and Trautmann, S. and Umanskaya, N. and Tippk{\"o}tter, Nils and M{\"u}ller-Renno, C.M. and Ulber, Roland and Hannig, M. and Ziegler, C.}, title = {Albumin-lysozyme interactions: cooperative adsorption on titanium and enzymatic activity}, series = {Colloids and Surfaces B: Biointerfaces}, volume = {149}, journal = {Colloids and Surfaces B: Biointerfaces}, number = {1}, publisher = {Elsevier}, address = {Amsterdam}, doi = {10.1016/j.colsurfb.2016.09.048}, pages = {115 -- 121}, year = {2016}, abstract = {The interplay of albumin (BSA) and lysozyme (LYZ) adsorbed simultaneously on titanium was analyzed by gel electrophoresis and BCA assay. It was found that BSA and lysozyme adsorb cooperatively. Additionally, the isoelectric point of the respective protein influences the adsorption. Also, the enzymatic activity of lysozyme and amylase (AMY) in mixtures with BSA was considered with respect to a possible influence of protein-protein interaction on enzyme activity. Indeed, an increase of lysozyme activity in the presence of BSA could be observed. In contrast, BSA does not influence the activity of amylase.}, language = {en} } @article{MolinnusBaeckerSiegertetal.2015, author = {Molinnus, Denise and B{\"a}cker, Matthias and Siegert, Petra and Willenberg, H. and Poghossian, Arshak and Keusgen, M. and Sch{\"o}ning, Michael Josef}, title = {Detection of Adrenaline Based on Substrate Recycling Amplification}, series = {Procedia Engineering}, volume = {120}, journal = {Procedia Engineering}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1877-7058}, doi = {10.1016/j.proeng.2015.08.708}, pages = {540 -- 543}, year = {2015}, abstract = {An amperometric enzyme biosensor has been applied for the detection of adrenaline. The adrenaline biosensor has been prepared by modification of an oxygen electrode with the enzyme laccase that operates at a broad pH range between pH 3.5 to pH 8. The enzyme molecules were immobilized via cross-linking with glutaraldehyde. The sensitivity of the developed adrenaline biosensor in different pH buffer solutions has been studied.}, language = {en} } @article{TippkoetterWollnyKampeisetal.2011, author = {Tippk{\"o}tter, Nils and Wollny, S. and Kampeis, P. and Oster, J. and Schneider, H. and Ulber, Roland}, title = {Magnetseparation von Proteinen : Separation von Zielmolek{\"u}len durch hochselektive Aptamere}, series = {GIT Labor-Fachzeitschrift}, volume = {55}, journal = {GIT Labor-Fachzeitschrift}, number = {10}, publisher = {Wiley}, address = {Weinheim}, pages = {666}, year = {2011}, abstract = {Durch die Kombination von Oligonukleotid-Liganden (Aptameren) hoher Bindungsaffinit{\"a}ten mit hochselektiv abtrennbaren magnetisierbaren Mikropartikeln wird eine einstufige Separation von Zielmolek{\"u}len aus mikrobiologischen Produktionsans{\"a}tzen m{\"o}glich. Die Aptamere werden hierf{\"u}r reversibel auf den Partikeloberfl{\"a}chen gebunden und f{\"u}r die spezifische Isolierung von Bioprodukten eingesetzt. Die Abtrennung der beladenen Partikel erfolgt durch einen neuen Rotor-Stator-Separator mit Hochgradient-Magnetfeld.}, language = {de} }