@article{SchererTuerlerGaeggeleretal.1988, author = {Scherer, Ulrich W. and T{\"u}rler, A. and G{\"a}ggeler, H. W. and Jost, D. T.}, title = {Determination of the Partial Electron-Capture- and Spontaneous-Fission Half-Lives of 254No / A. T{\"u}rler, H.W. G{\"a}ggeler, D.T. Jost, P. Armbruster, W. Br{\"u}chle, H. Folger, F.P. Heßberger, S. Hofmann,}, series = {Zeitschrift f{\"u}r Physik A Hadrons and Nuclei. 331 (1988), H. 3}, journal = {Zeitschrift f{\"u}r Physik A Hadrons and Nuclei. 331 (1988), H. 3}, isbn = {0939-7922}, pages = {363 -- 364}, year = {1988}, language = {en} } @article{KueppersSteffenHellmuthetal.2014, author = {K{\"u}ppers, Tobias and Steffen, Victoria and Hellmuth, Hendrik and O'Connell, Timothy and Bongaerts, Johannes and Maurer, Karl-Heinz and Wiechert, Wolfgang}, title = {Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer}, series = {Microbial cell factories}, volume = {13}, journal = {Microbial cell factories}, publisher = {BioMed Central}, address = {London}, issn = {1475-2859 (E-Journal)}, doi = {10.1186/1475-2859-13-46}, pages = {Article No. 46}, year = {2014}, language = {en} } @article{MolinnusMuschallikGonzalezetal.2018, author = {Molinnus, Denise and Muschallik, Lukas and Gonzalez, Laura Osorio and Bongaerts, Johannes and Wagner, Torsten and Selmer, Thorsten and Siegert, Petra and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Development and characterization of a field-effect biosensor for the detection of acetoin}, series = {Biosensors and Bioelectronics}, volume = {115}, journal = {Biosensors and Bioelectronics}, publisher = {Elsevier}, address = {Amsterdam}, doi = {10.1016/j.bios.2018.05.023}, pages = {1 -- 6}, year = {2018}, abstract = {A capacitive electrolyte-insulator-semiconductor (EIS) field-effect biosensor for acetoin detection has been presented for the first time. The EIS sensor consists of a layer structure of Al/p-Si/SiO₂/Ta₂O₅/enzyme acetoin reductase. The enzyme, also referred to as butane-2,3-diol dehydrogenase from B. clausii DSM 8716T, has been recently characterized. The enzyme catalyzes the (R)-specific reduction of racemic acetoin to (R,R)- and meso-butane-2,3-diol, respectively. Two different enzyme immobilization strategies (cross-linking by using glutaraldehyde and adsorption) have been studied. Typical biosensor parameters such as optimal pH working range, sensitivity, hysteresis, linear concentration range and long-term stability have been examined by means of constant-capacitance (ConCap) mode measurements. Furthermore, preliminary experiments have been successfully carried out for the detection of acetoin in diluted white wine samples.}, language = {en} } @article{TurekKettererClassenetal.2007, author = {Turek, Monika and Ketterer, Lothar and Claßen, Melanie and Berndt, Heinz and Elbers, Gereon and Kr{\"u}ger, Peter and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Development and Electrochemical Investigations of an EIS-(Electrolyte-Insulator-Semiconductor) based Biosensor for Cyanide Detection}, series = {Sensors}, volume = {7}, journal = {Sensors}, number = {8}, isbn = {1424-8220}, pages = {1415 -- 1426}, year = {2007}, language = {en} } @article{SeifarthGossmannGrosseetal.2015, author = {Seifarth, Volker and Goßmann, Matthias and Grosse, J. O. and Becker, C. and Heschel, I. and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l}, title = {Development of a Bioreactor to Culture Tissue Engineered Ureters Based on the Application of Tubular OPTIMAIX 3D Scaffolds}, series = {Urologia Internationalis}, volume = {2015}, journal = {Urologia Internationalis}, number = {95}, publisher = {Karger}, address = {Basel}, issn = {0042-1138}, doi = {10.1159/000368419}, pages = {106 -- 113}, year = {2015}, language = {en} } @article{DuenkelmannKolterJungNitscheetal.2002, author = {D{\"u}nkelmann, Pascal and Kolter-Jung, Doris and Nitsche, Adam and Demir, Ayhan S. and Siegert, Petra and Lingen, Bettina and Baumann, Martin and Pohl, Martina and M{\"u}ller, Michael}, title = {Development of a donor-acceptor concept for enzymatic cross-coupling reactions of adehydes : the first asymmetric cross-benzoin condensation}, series = {Journal of the American Chemical Society}, volume = {Vol. 124}, journal = {Journal of the American Chemical Society}, issn = {1520-5126 (E-Journal); 0002-7863 (Print)}, pages = {12084 -- 12085}, year = {2002}, language = {en} } @article{BiselliMeissnerSchroederetal.1999, author = {Biselli, Manfred and Meissner, Petra and Schr{\"o}der, Bernd and Herfurth, Cornelia}, title = {Development of a fixed bed bioreactor for the expansion of human hematopoietic progenitor cells / Meissner, Petra ; Schr{\"o}der, Bernd ; Herfurth, Cornelia ; Biselli, Manfred}, series = {Cytotechnology. 30 (1999), H. 1}, journal = {Cytotechnology. 30 (1999), H. 1}, isbn = {0920-9069}, pages = {227 -- 234}, year = {1999}, language = {en} } @article{PilasIkenSelmeretal.2015, author = {Pilas, Johanna and Iken, Heiko and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Development of a multi-parameter sensor chip for the simultaneous detection of organic compounds in biogas processes}, series = {Physica status solidi (a)}, volume = {212}, journal = {Physica status solidi (a)}, number = {6}, publisher = {Wiley}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201431894}, pages = {1306 -- 1312}, year = {2015}, abstract = {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.}, language = {en} } @article{AboulnagaZouSelmeretal.2018, author = {Aboulnaga, E. A. and Zou, H. and Selmer, Thorsten and Xian, M.}, title = {Development of a plasmid-based, tunable, tolC-derived expression system for application in Cupriavidus necator H16}, series = {Journal of Biotechnology}, volume = {274}, journal = {Journal of Biotechnology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0168-1656}, doi = {10.1016/j.jbiotec.2018.03.007}, pages = {15 -- 27}, year = {2018}, abstract = {Cupriavidus necator H16 gains increasing attention in microbial research and biotechnological application due to its diverse metabolic features. Here we present a tightly controlled gene expression system for C. necator including the pBBR1-vector that contains hybrid promoters originating from C. necator native tolC-promoter in combination with a synthetic tetO-operator. The expression of the reporter gene from these plasmids relies on the addition of the exogenous inducer doxycycline (dc). The novel expression system offers a combination of advantageous features as; (i) high and dose-dependent recombinant protein production, (ii) tight control with a high dynamic range (On/Off ratio), which makes it applicable for harmful pathways or for toxic protein production, (iii) comparable cheap inducer (doxycycline, dc), (iv) effective at low inducer concentration, that makes it useful for large scale application, (v) rapid, diffusion controlled induction, and (vi) the inducer does not interfere within the cell metabolism. As applications of the expression system in C. necator H16, the growth ability on glycerol was enhanced by constitutively expressing the E. coli glpk gene-encoding for glycerol kinase. Likewise, we used the system to overcome the expression toxicity of mevalonate pathway in C. necator H16. With this system, the mevalonate-genes were successfully introduced in the host and the recombinant strains could produce about 200 mg/l mevalonate.}, language = {en} } @article{BiselliHambachRunstadleretal.1992, author = {Biselli, Manfred and Hambach, B. and Runstadler, P. W. and Wandrey, Christian}, title = {Development of a reactor-integrated aeration system for cultivation of animal cells in fluidized beds / Hambach, B. ; Biselli, M. ; Runstadler, P.W. ; Wandrey, C.}, series = {Animal cell technology : developments, processes, and products ; ESACT, European Society for Animal Cell Technology, the 11th meeting / Ed. R. E. Spier}, journal = {Animal cell technology : developments, processes, and products ; ESACT, European Society for Animal Cell Technology, the 11th meeting / Ed. R. E. Spier}, publisher = {Butterworth-Heinemann}, address = {Oxford}, isbn = {0750604212}, pages = {381 -- 385}, year = {1992}, 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{BiselliVanderPolJokschetal.1992, author = {Biselli, Manfred and Van der Pol, Jens J. and Joksch, B. and Eberhardt, R.}, title = {Development of an enzymatic multichannel flow injection analysis system for monitoring mammalian cell fermentations / Van der Pol, J.J.; Joksch, B.; Eberhardt, R.; Biselli, M.; Wandrey, C., Tramper, J.}, series = {Biosensors : fundamentals, technologies and applications ; contributions to the BMFT status seminar with international participation May, 12 to 14, 1991, Internationales Bildungs-Centrum Bogensee/Brandenburg, Germany / org. by ZIM-Zentralinstitut f{\"u}r Molekularbiologie, Berlin-Buch and GBF, Braunschweig. Ed. by F. Scheller}, journal = {Biosensors : fundamentals, technologies and applications ; contributions to the BMFT status seminar with international participation May, 12 to 14, 1991, Internationales Bildungs-Centrum Bogensee/Brandenburg, Germany / org. by ZIM-Zentralinstitut f{\"u}r Molekularbiologie, Berlin-Buch and GBF, Braunschweig. Ed. by F. Scheller}, publisher = {VCH}, address = {Weinheim}, isbn = {3527284370}, pages = {349 -- 352}, year = {1992}, language = {en} } @article{BaumannJahnke1986, author = {Baumann, Marcus and Jahnke, J.}, title = {Die marine Planktonalge Phaeocystis globosa / Jahnke, J. ; Baumann, M.}, series = {Mikrokosmos. 75 (1986), H. 12}, journal = {Mikrokosmos. 75 (1986), H. 12}, isbn = {0026-3680}, pages = {357 -- 359}, year = {1986}, language = {de} } @article{KowollikSchnitzlerBisellietal.2010, author = {Kowollik, S. and Schnitzler, Thomas and Biselli, Manfred and Krueger, R. and Zang, Werner and Peuscher, A. and Schillberg, S. and Fischer, R.}, title = {Die Rolle des Respirationsquotienten in der Zellkulturfermentation}, series = {Chemie Ingenieur Technik}, volume = {82}, journal = {Chemie Ingenieur Technik}, number = {9}, isbn = {Chemie Ingenieur Tec}, pages = {1505 -- 1506}, year = {2010}, language = {de} } @article{BiselliNoll1998, author = {Biselli, Manfred and Noll, T.}, title = {Dielectric spectroscopy in the cultivation of suspended and immobilized hybridoma cells / Noll, T.; Biselli, M.}, series = {Journal of Biotechnology. 63 (1998), H. 3}, journal = {Journal of Biotechnology. 63 (1998), H. 3}, isbn = {0168-1656}, pages = {187 -- 198}, year = {1998}, language = {en} } @article{CapitainRossJonesMoehringetal.2020, author = {Capitain, Charlotte and Ross-Jones, Jesse and M{\"o}hring, Sophie and Tippk{\"o}tter, Nils}, title = {Differential scanning calorimetry for quantification of polymer biodegradability in compost}, series = {International Biodeterioration \& Biodegradation}, volume = {149}, journal = {International Biodeterioration \& Biodegradation}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0964-8305}, doi = {10.1016/j.ibiod.2020.104914}, pages = {In Press, Article number 104914}, year = {2020}, abstract = {The objective of this study is the establishment of a differential scanning calorimetry (DSC) based method for online analysis of the biodegradation of polymers in complex environments. Structural changes during biodegradation, such as an increase in brittleness or crystallinity, can be detected by carefully observing characteristic changes in DSC profiles. Until now, DSC profiles have not been used to draw quantitative conclusions about biodegradation. A new method is presented for quantifying the biodegradation using DSC data, whereby the results were validated using two reference methods. The proposed method is applied to evaluate the biodegradation of three polymeric biomaterials: polyhydroxybutyrate (PHB), cellulose acetate (CA) and Organosolv lignin. The method is suitable for the precise quantification of the biodegradability of PHB. For CA and lignin, conclusions regarding their biodegradation can be drawn with lower resolutions. The proposed method is also able to quantify the biodegradation of blends or composite materials, which differentiates it from commonly used degradation detection methods.}, language = {en} } @article{JahnkeBaumann1987, author = {Jahnke, J. and Baumann, Marcus}, title = {Differentiation between Phaeocystis pouchetii (Har.) Lagerheim and Phaeocystis globosa Scherffel}, series = {Hydrobiological bulletin}, volume = {Vol. 21}, journal = {Hydrobiological bulletin}, number = {Iss. 2}, issn = {0165-1404 (Print); 1573-5125 (E-Journal)}, pages = {141 -- 147}, year = {1987}, language = {en} } @article{BiselliSchroederHerfurthetal.1997, author = {Biselli, Manfred and Schr{\"o}der, B. and Herfurth, C. and Meißner, P.}, title = {Differentiation of bone marrow cells immobilized on microcarriers in a fluidized bed reactor / Schr{\"o}der, B. ; Herfurth, C. ; Meißner, P. ; Biselli, M. ; Link, H. ; Wandrey, C.}, series = {Animal cell technology : from vaccines to genetic medicine ; [Vilamoura, Portugal, May 1996] / ed. by Manuel J. T. Carrondo}, journal = {Animal cell technology : from vaccines to genetic medicine ; [Vilamoura, Portugal, May 1996] / ed. by Manuel J. T. Carrondo}, publisher = {Kluwer}, address = {Dordrecht}, isbn = {0-7923-4321-2}, pages = {589 -- 593}, year = {1997}, language = {en} } @article{KotterHeeringRiekert1982, author = {Kotter, Michael and Heering, J. and Riekert, L.}, title = {Diffusion and catalytic reaction in zeolite ZSM-5 / J. Heering ; M. Kotter ; L. Riekert}, series = {Chemical engineering science . 37 (1982), H. 4}, journal = {Chemical engineering science . 37 (1982), H. 4}, isbn = {0009-2509}, pages = {581 -- 584}, year = {1982}, language = {en} } @article{PrielmeierSpeedyVardagetal.1989, author = {Prielmeier, Franz and Speedy, R. J. and Vardag, T. and Lang, E. W.}, title = {Diffusion in simple fluids / R. J. Speedy; F. X. Prielmeier; T. Vardag; E. W. Lang; H.-D. L{\"u}demann}, series = {Molecular Physics. 66 (1989), H. 3}, journal = {Molecular Physics. 66 (1989), H. 3}, isbn = {0026-8976}, pages = {577 -- 590}, year = {1989}, language = {en} }