@article{KapplerTanudyayaSchmittTippkoetteretal.2007,
  author    = {Kappler-Tanudyaya, Nathalie and Schmitt, Heike and Tippk{\"o}tter, Nils and Meyer, Lina and Lenzen, Sigurd and Ulber, Roland},
  title     = {Combination of biotransformation and chromatography for the isolation and purification of mannoheptulose},
  series = {Biotechnology Journal},
  volume    = {2},
  journal   = {Biotechnology Journal},
  number    = {6},
  issn      = {1860-7314},
  doi       = {10.1002/biot.200700004},
  pages     = {692 -- 699},
  year      = {2007},
  abstract  = {Mannoheptulose is a seven-carbon sugar. It is an inhibitor of glucose-induced insulin secretion due to its ability to selectively inhibit the enzyme glucokinase. An improved procedure for mannoheptulose isolation from avocados is described in this study (based upon the original method by La Forge). The study focuses on the combination of biotransformation and downstream processing (preparative chromatography) as an efficient method to produce a pure extract of mannoheptulose. The experiments were divided into two major phases. In the first phase, several methods and parameters were compared to optimize the mannoheptulose extraction with respect to efficiency and purity. In the second phase, a mass balance of mannoheptulose over the whole extraction process was undertaken to estimate the yield and efficiency of the total extraction process. The combination of biotransformation and preparative chromatography allowed the production of a pure mannoheptulose extract. In a biological test, the sugar inhibited the glucokinase enzyme activity efficiently.},
  language  = {en}
}
@article{SchiffelsSelmer2019,
  author    = {Schiffels, Johannes and Selmer, Thorsten},
  title     = {Combinatorial assembly of ferredoxin-linked modules in Escherichia coli yields a testing platform for Rnf-complexes},
  series = {Biotechnology and Bioengineering},
  journal   = {Biotechnology and Bioengineering},
  number    = {accepted article},
  publisher = {Wiley},
  address   = {Weinheim},
  doi       = {10.1002/bit.27079},
  pages     = {1 -- 36},
  year      = {2019},
  language  = {en}
}
@article{BalakrishnanAndreiSelmerSelmeretal.2010,
  author    = {Balakrishnan, Karthikeyan and Andrei-Selmer, Luminita-Cornelia and Selmer, Thorsten and Bacher, Michael and Dodel, Richard},
  title     = {Comparison of Intravenous Immunoglobulins for Naturally Occurring Autoantibodies against Amyloid-β},
  series = {Journal of Alzheimer's Disease},
  volume    = {20},
  journal   = {Journal of Alzheimer's Disease},
  number    = {1},
  isbn      = {1387-2877},
  pages     = {135 -- 143},
  year      = {2010},
  language  = {en}
}
@article{WulfhorstDuweMerseburgetal.2016,
  author    = {Wulfhorst, Helene and Duwe, Anna-Maria and Merseburg, Johannes and Tippk{\"o}tter, Nils},
  title     = {Compositional analysis of pretreated (beech) wood using differential scanning calorimetry and multivariate data analysis},
  series = {Tetrahedron},
  volume    = {72},
  journal   = {Tetrahedron},
  number    = {46},
  publisher = {Elsevier},
  address   = {Amsterdam},
  doi       = {10.1016/j.tet.2016.04.029},
  pages     = {7329 -- 7334},
  year      = {2016},
  abstract  = {The composition of plant biomass varies depending on the feedstock and pre-treatment conditions and influences its processing in biorefineries. In order to ensure optimal process conditions, the quantitative proportion of the main polymeric components of the pre-treated biomass has to be determined. Current standard procedures for biomass compositional analysis are complex, the measurements are afflicted with errors and therefore often not comparable. Hence, new powerful analytical methods are urgently required to characterize biomass. In this contribution, Differential Scanning Calorimetry (DSC) was applied in combination with multivariate data analysis (MVA) to detect the cellulose content of the plant biomass pretreated by Liquid Hot Water (LHW) and Organosolv processes under various conditions. Unlike conventional techniques, the developed analytic method enables the accurate quantification of monosaccharide content of the plant biomass without any previous sample preparation. It is easy to handle and avoids errors in sample preparation.},
  language  = {en}
}
@article{HagerHentschkeHojdisetal.2015,
  author    = {Hager, Jonathan and Hentschke, Reinhard and Hojdis, Nils and Karimi-Varzaneh, Hossein Ali},
  title     = {Computer Simulation of Particle-Particle Interaction in a Model Polymer Nanocomposite},
  series = {Macromolecules},
  volume    = {48},
  journal   = {Macromolecules},
  number    = {24},
  issn      = {1520-5835},
  doi       = {10.1021/acs.macromol.5b01864},
  pages     = {9039 -- 9049},
  year      = {2015},
  language  = {en}
}
@article{BaeckerBegingBisellietal.2009,
  author    = {B{\"a}cker, Matthias and Beging, Stefan and Biselli, Manfred and Poghossian, Arshak and Wang, J. and Zang, Werner and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Concept for a solid-state multi-parameter sensor system for cell-culture monitoring},
  series = {Electrochimica Acta. 54 (2009), H. 25 Sp. Iss. SI},
  journal   = {Electrochimica Acta. 54 (2009), H. 25 Sp. Iss. SI},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {0013-4686},
  pages     = {6107 -- 6112},
  year      = {2009},
  language  = {en}
}
@article{HaegerGrankinWagner2023,
  author    = {Haeger, Gerrit and Grankin, Alina and Wagner, Michaela},
  title     = {Construction of an Aspergillus oryzae triple amylase deletion mutant as a chassis to evaluate industrially relevant amylases using multiplex CRISPR/Cas9 editing technology},
  series = {Applied Research},
  journal   = {Applied Research},
  number    = {Early View},
  publisher = {Wiley-VCH},
  issn      = {2702-4288},
  doi       = {10.1002/appl.202200106},
  pages     = {1 -- 15},
  year      = {2023},
  abstract  = {Aspergillus oryzae is an industrially relevant organism for the secretory production of heterologous enzymes, especially amylases. The activities of potential heterologous amylases, however, cannot be quantified directly from the supernatant due to the high background activity of native α-amylase. This activity is caused by the gene products of amyA, amyB, and amyC. In this study, an in vitro CRISPR/Cas9 system was established in A. oryzae to delete these genes simultaneously. First, pyrG of A. oryzae NSAR1 was mutated by exploiting NHEJ to generate a counter-selection marker. Next, all amylase genes were deleted simultaneously by co-transforming a repair template carrying pyrG of Aspergillus nidulans and flanking sequences of amylase gene loci. The rate of obtained triple knock-outs was 47\%. We showed that triple knockouts do not retain any amylase activity in the supernatant. The established in vitro CRISPR/Cas9 system was used to achieve sequence-specific knock-in of target genes. The system was intended to incorporate a single copy of the gene of interest into the desired host for the development of screening methods. Therefore, an integration cassette for the heterologous Fpi amylase was designed to specifically target the amyB locus. The site-specific integration rate of the plasmid was 78\%, with exceptional additional integrations. Integration frequency was assessed via qPCR and directly correlated with heterologous amylase activity. Hence, we could compare the efficiency between two different signal peptides. In summary, we present a strategy to exploit CRISPR/Cas9 for gene mutation, multiplex knock-out, and the targeted knock-in of an expression cassette in A. oryzae. Our system provides straightforward strain engineering and paves the way for development of fungal screening systems.},
  language  = {en}
}
@article{Scherer2006,
  author    = {Scherer, Ulrich W.},
  title     = {Controlled ion track etching / J. George; M. Irkens ; S. Neumann ; U. W. Scherer ; A. Srivastava ; D. Sinha ; D. Fink},
  series = {Radiation Effects and Defects in Solids. 161 (2006), H. 3},
  journal   = {Radiation Effects and Defects in Solids. 161 (2006), H. 3},
  pages     = {161 -- 175},
  year      = {2006},
  language  = {en}
}
@article{SelmerLukatelaKraussetal.1998,
  author    = {Selmer, Thorsten and Lukatela, G. and Krauss, N. and Theis, K.},
  title     = {Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis / Lukatela, G. ; Krauss, N. ; Theis, K. ; Selmer, T. ; Gieselmann, V. ; Figura, K. von ; Saenger,},
  series = {Biochemistry. 37 (1998), H. 11},
  journal   = {Biochemistry. 37 (1998), H. 11},
  pages     = {3654 -- 3664},
  year      = {1998},
  language  = {en}
}
@article{HemmerlingMerschenzQuackWunderlich1988,
  author    = {Hemmerling, H.-J. and Merschenz-Quack, Angelika and Wunderlich, H.},
  title     = {Crystal structures of indeno[1,2-d]imidazoles. XIth European Crystallographic Meeting, Vienna 1988},
  series = {Zeitschrift f{\"u}r Kristallographie - Crystalline Materials},
  volume    = {185},
  journal   = {Zeitschrift f{\"u}r Kristallographie - Crystalline Materials},
  number    = {H. 1-4},
  issn      = {2196-7105 (E-Books); 2194-4946 (Print)},
  pages     = {256},
  year      = {1988},
  language  = {en}
}
@article{LauthHoelderichWagenblast1995,
  author    = {Lauth, Jakob and Hoelderich, W. and Wagenblast, G.},
  title     = {Crystalline zeolites containing indigo dyes},
  series = {Zeolites. 15 (1995), H. 1},
  journal   = {Zeolites. 15 (1995), H. 1},
  isbn      = {0144-2449},
  pages     = {86},
  year      = {1995},
  language  = {en}
}
@article{BiselliNollJelineketal.2002,
  author    = {Biselli, Manfred and Noll, Thomas and Jelinek, Nanni and Schmidt, Sebastian},
  title     = {Cultivation of Hematopoietic Stem and Progenitor Cells: biochemical Engineering Aspects / Thomas Noll, Nanni Jelinek, Sebastian Schmidt, Manfred Biselli und Christian Wandrey},
  series = {Tools and Applications of Biochemical Engineering Science},
  journal   = {Tools and Applications of Biochemical Engineering Science},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {3-540-42250-1},
  pages     = {111 -- 128},
  year      = {2002},
  language  = {en}
}
@article{BiselliHilbertNoll2001,
  author    = {Biselli, Manfred and Hilbert, U. and Noll, T.},
  title     = {Cultivation of Human HCMV Specific Lymphocytes - An Example for Adoptive Immunotherapy / Hilbert, U. ; Biselli, M. ; Noll, T.},
  series = {Animal cell technology : from target to market ; Tyl{\"o}sand, Sweden, June 10 - 14, 2001 / ed. by E. Lindner-Olsson ...},
  journal   = {Animal cell technology : from target to market ; Tyl{\"o}sand, Sweden, June 10 - 14, 2001 / ed. by E. Lindner-Olsson ...},
  publisher = {Kluwer},
  address   = {Dordrecht},
  isbn      = {1-4020-0264-5},
  pages     = {558 -- 561},
  year      = {2001},
  language  = {en}
}
@article{Schnitzler2009,
  author    = {Schnitzler, Thomas},
  title     = {Cultivation of hybridoma cell line CF-10H5 (DSMZ ACC477)},
  series = {Application notes / Sartorius stedim biotech},
  journal   = {Application notes / Sartorius stedim biotech},
  pages     = {1 -- 4},
  year      = {2009},
  language  = {en}
}
@book{LauthDingerdissenSteuerle1996,
  author    = {Lauth, Jakob and Dingerdissen, Uwe and Steuerle, Ulrich},
  title     = {Cup catalyst and process for producing aziridines : [Internationale Pantentanmeldung WO9633018] ; Ver{\"o}ffentlichungsdatum: 1996-10-24 / Anmelder: BASF AG ; Dingerdissen, Uwe ; Lauth, Guenther ; Steuerle, Ulrich. Erfinder: Dingerdissen, Uwe ; Lauth, Guenther ; Steuerle, Ulrich},
  publisher = {[Weltorganisation f{\"u}r geistiges Eigentum]},
  address   = {[Genf]},
  year      = {1996},
  language  = {en}
}
@article{HendersonMclaughlinScheeretal.2015,
  author    = {Henderson, Colin J. and Mclaughlin, Lesley A. and Scheer, Nico and Stanley, Lesley A. and Wolf, C. Roland},
  title     = {Cytochrome b5 Is a Major Determinant of Human Cytochrome P450 CYP2D6 and CYP3A4 Activity In Vivo s},
  series = {Molecular Pharmacology},
  volume    = {87},
  journal   = {Molecular Pharmacology},
  number    = {4},
  publisher = {ASPET},
  address   = {Bethesda},
  issn      = {1521-0111},
  doi       = {10.1124/mol.114.097394},
  pages     = {733 -- 739},
  year      = {2015},
  language  = {en}
}
@article{FeuerriegelKloseSloboshaninetal.1994,
  author    = {Feuerriegel, Uwe and Klose, W. and Sloboshanin, S. and Goebel, H. [u.a.]},
  title     = {Deactivation of a palladium-supported alumina catalyst by hydrogen sulfide during the oxidation of methane},
  series = {Langmuir: the ACS journal of surfaces and colloids. 10 (1994), H. 10},
  journal   = {Langmuir: the ACS journal of surfaces and colloids. 10 (1994), H. 10},
  isbn      = {0743-74363},
  pages     = {3567 -- 3570},
  year      = {1994},
  language  = {en}
}
@article{ScheerKapelyukhRodeetal.2015,
  author    = {Scheer, Nico and Kapelyukh, Yury and Rode, Anja and Oswald, Stefan and Busch, Diana and Mclaughlin, Lesley A. and Lin, De and Henderson, Colin J. and Wolf, C. Roland},
  title     = {Defining Human Pathways of Drug Metabolism In Vivo through the Development of a Multiple Humanized Mouse Model},
  series = {Drug Metabolism and Disposition},
  volume    = {43},
  journal   = {Drug Metabolism and Disposition},
  number    = {11},
  publisher = {ASPET},
  address   = {Bethesda},
  issn      = {1521-009x},
  doi       = {10.1124/dmd.115.065656},
  pages     = {1679 -- 1690},
  year      = {2015},
  language  = {en}
}
@article{KapelyukhHendersonScheeretal.2019,
  author    = {Kapelyukh, Yury and Henderson, Colin James and Scheer, Nico and Rode, Anja and Wolf, Charles Roland},
  title     = {Defining the contribution of CYP1A1 and CYP1A2 to drug metabolism using humanized CYP1A1/1A2 and Cyp1a1/Cyp1a2 KO mice},
  series = {Drug Metabolism and Disposition},
  journal   = {Drug Metabolism and Disposition},
  number    = {Early view},
  doi       = {10.1124/dmd.119.087718},
  pages     = {43 Seiten},
  year      = {2019},
  language  = {en}
}
@article{ScheerMclaughlinRodeetal.2014,
  author    = {Scheer, Nico and Mclaughlin, Lesley A. and Rode, Anja and MacLeod, Alastair Kenneth and Henderson, Colin J. and Wolf, Roland C.},
  title     = {Deletion of thirty murine cytochrome P450 genes results in viable mice with compromised drug metabolism},
  series = {Drug Metabolism and Disposition},
  volume    = {42},
  journal   = {Drug Metabolism and Disposition},
  number    = {6},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-009X},
  doi       = {10.1124/dmd.114.057885},
  pages     = {1022 -- 1030},
  year      = {2014},
  abstract  = {In humans, 75\% of all drugs are metabolized by the cytochrome P450-dependent monooxygenase system. Enzymes encoded by the CYP2C, CYP2D, and CYP3A gene clusters account for ∼80\% of this activity. There are profound species differences in the multiplicity of cytochrome P450 enzymes, and the use of mouse models to predict pathways of drug metabolism is further complicated by overlapping substrate specificity between enzymes from different gene families. To establish the role of the hepatic and extrahepatic P450 system in drug and foreign chemical disposition, drug efficacy, and toxicity, we created a unique mouse model in which 30 cytochrome P450 genes from the Cyp2c, Cyp2d, and Cyp3a gene clusters have been deleted. Remarkably, despite a wide range of putative important endogenous functions, Cyp2c/2d/3a KO mice were viable and fertile, demonstrating that these genes have evolved primarily as detoxification enzymes. Although there was no overt phenotype, detailed examination showed Cyp2c/2d/3a KO mice had a smaller body size (15\%) and larger livers (20\%). Changes in hepatic morphology and a decreased blood glucose (30\%) were also noted. A five-drug cocktail of cytochrome P450 isozyme probe substrates were used to evaluate changes in drug pharmacokinetics; marked changes were observed in either the pharmacokinetics or metabolites formed from Cyp2c, Cyp2d, and Cyp3a substrates, whereas the metabolism of the Cyp1a substrate caffeine was unchanged. Thus, Cyp2c/2d/3a KO mice provide a powerful model to study the in vivo role of the P450 system in drug metabolism and efficacy, as well as in chemical toxicity.},
  language  = {en}
}
@article{PrielmeierRadkowitschLangetal.1986,
  author    = {Prielmeier, Franz and Radkowitsch, H. and Lang, E. W. and L{\"u}demann, H.-D.},
  title     = {Density dependence of the molecular dynamics of fluid CH3F and CF3H studied by NMR / H. Radkowitsch, F. X. Prielmeier, E. W. Lang and H.-D. L{\"u}demann},
  series = {Physica B+C. 139-140 (1986)},
  journal   = {Physica B+C. 139-140 (1986)},
  isbn      = {0921-4526},
  pages     = {96 -- 99},
  year      = {1986},
  language  = {en}
}
@article{KotterRiekertWeyland1983,
  author    = {Kotter, Michael and Riekert, L. and Weyland, F.},
  title     = {Deposition of ternary oxides as active components by impregnation of porous carriers},
  series = {Preparation of Catalysts III : scientific bases for the preparation of heterogeneous catalysts ; proceedings of the Third International Symposium, Louvain-la-Neuve, September 6-9, 1982 / ed.: G. Poncelet ... - (Studies in surface science and catalysis ; 16)},
  journal   = {Preparation of Catalysts III : scientific bases for the preparation of heterogeneous catalysts ; proceedings of the Third International Symposium, Louvain-la-Neuve, September 6-9, 1982 / ed.: G. Poncelet ... - (Studies in surface science and catalysis ; 16)},
  publisher = {Elsevier},
  address   = {Amsterdam [u.a.]},
  isbn      = {0-444-42184-X},
  pages     = {521 -- 530},
  year      = {1983},
  language  = {en}
}
@article{KalbeHoeckerBerndt1989,
  author    = {Kalbe, Jochen and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Design of enzyme reactors as chromatographic columns for racemic resolution of amino acid esters},
  series = {Chromatographia},
  volume    = {28},
  journal   = {Chromatographia},
  number    = {3-4},
  isbn      = {0009-5893},
  doi       = {10.1007/BF02319646},
  pages     = {193 -- 196},
  year      = {1989},
  language  = {en}
}
@article{LeursMezoOehlschlaegeretal.2012,
  author    = {Leurs, Ulrike and Mezo, Gabor and {\"O}hlschl{\"a}ger, Peter and Orban, Erika and Marquard, Andrea and Manea, Marilena},
  title     = {Design, synthesis, in vitro stability and cytostatic effect of multifunctional anticancer drug-bioconjugates containing GnRH-III as a targeting moiety},
  series = {Peptide Science},
  volume    = {98},
  journal   = {Peptide Science},
  number    = {1},
  publisher = {Wiley},
  address   = {New York, NY},
  issn      = {1097-0282},
  doi       = {10.1002/bip.21640},
  pages     = {1 -- 10},
  year      = {2012},
  abstract  = {Bioconjugates containing the GnRH-III hormone decapeptide as a targeting moiety are able to deliver chemotherapeutic agents specifically to cancer cells expressing GnRH receptors, thereby increasing their local efficacy while limiting the peripheral toxicity. However, the number of GnRH receptors on cancer cells is limited and they desensitize under continuous hormone treatment. A possible approach to increase the receptor mediated tumor targeting and consequently the cytostatic effect of the bioconjugates would be the attachment of more than one chemotherapeutic agent to one GnRH-III molecule. Here we report on the design, synthesis and biochemical characterization of multifunctional bioconjugates containing GnRH-III as a targeting moiety and daunorubicin as a chemotherapeutic agent. Two different drug design approaches were pursued. The first one was based on the bifunctional [4Lys]-GnRH-III (Glp-His-Trp-Lys-His-Asp-Trp-Lys-Pro-Gly-NH2) containing two lysine residues in positions 4 and 8, whose ϵ-amino groups were used for the coupling of daunorubicin. In the second drug design, the native GnRH-III (Glp-His-Trp-Ser-His-Asp-Trp-Lys-Pro-Gly-NH2) was used as a scaffold; an additional lysine residue was coupled to the ϵ-amino group of 8Lys in order to generate two free amino groups available for conjugation of daunorubicin. The in vitro stability/degradation of all synthesized compounds was investigated in human serum, as well as in the presence of rat liver lysosomal homogenate. Their cellular uptake was determined on human breast cancer cells and the cytostatic effect was evaluated on human breast, colon and prostate cancer cell lines. Compared with a monofunctional compound, both drug design approaches resulted in multifunctional bioconjugates with increased cytostatic effect.},
  language  = {en}
}
@article{SchmichEdererEbert1992,
  author    = {Schmich, Peter and Ederer, Hanns J. and Ebert, Klaus H.},
  title     = {Detection and identification of free radicals in hydrocarbon pyrolysis by an iodine trapping method},
  series = {Industrial \& Engineering Chemistry Research. 31 (1992), H. 1},
  journal   = {Industrial \& Engineering Chemistry Research. 31 (1992), H. 1},
  isbn      = {1520-5045},
  pages     = {29 -- 37},
  year      = {1992},
  language  = {en}
}
@article{WeldenSeverinsPoghossianetal.2022,
  author    = {Welden, Melanie and Severins, Robin and Poghossian, Arshak and Wege, Christina and Bongaerts, Johannes and Siegert, Petra and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Detection of acetoin and diacetyl by a tobacco mosaic virus-assisted field-effect biosensor},
  series = {Chemosensors},
  volume    = {10},
  journal   = {Chemosensors},
  number    = {6},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2227-9040},
  doi       = {10.3390/chemosensors10060218},
  pages     = {Artikel 218},
  year      = {2022},
  abstract  = {Acetoin and diacetyl have a major impact on the flavor of alcoholic beverages such as wine or beer. Therefore, their measurement is important during the fermentation process. Until now, gas chromatographic techniques have typically been applied; however, these require expensive laboratory equipment and trained staff, and do not allow for online monitoring. In this work, a capacitive electrolyte-insulator-semiconductor sensor modified with tobacco mosaic virus (TMV) particles as enzyme nanocarriers for the detection of acetoin and diacetyl is presented. The enzyme acetoin reductase from Alkalihalobacillus clausii DSM 8716ᵀ is immobilized via biotin-streptavidin affinity, binding to the surface of the TMV particles. The TMV-assisted biosensor is electrochemically characterized by means of leakage-current, capacitance-voltage, and constant capacitance measurements. In this paper, the novel biosensor is studied regarding its sensitivity and long-term stability in buffer solution. Moreover, the TMV-assisted capacitive field-effect sensor is applied for the detection of diacetyl for the first time. The measurement of acetoin and diacetyl with the same sensor setup is demonstrated. Finally, the successive detection of acetoin and diacetyl in buffer and in diluted beer is studied by tuning the sensitivity of the biosensor using the pH value of the measurement solution.},
  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}
}
@inproceedings{TakenagaHerreraWerneretal.2013,
  author    = {Takenaga, Shoko and Herrera, Cony F. and Werner, Frederik and Biselli, Manfred and Schnitzler, Thomas and Sch{\"o}ning, Michael Josef and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten},
  title     = {Detection of the metabolic activity of cells by differential measurements based on a single light-addressable potentiometric sensor chip},
  series = {11. Dresdner Sensor-Symposium : 9.-11.12.2013},
  booktitle = {11. Dresdner Sensor-Symposium : 9.-11.12.2013},
  organization    = {Dresdner Sensor-Symposium <11, 2013>},
  isbn      = {978-3-9813484-5-3},
  pages     = {63 -- 67},
  year      = {2013},
  language  = {en}
}
@article{TippkoetterDeterdingUlber2008,
  author    = {Tippk{\"o}tter, Nils and Deterding, A. and Ulber, Roland},
  title     = {Determination of acetic acid in fermentation broth by gas-diffusion technique},
  series = {Engineering in Life Sciences},
  volume    = {8},
  journal   = {Engineering in Life Sciences},
  number    = {1, Special Issue: Technical Systems for the Use in Life Sciences},
  doi       = {10.1002/elsc.200820227},
  pages     = {62 -- 67},
  year      = {2008},
  abstract  = {Due to the interfering effects of acetic acid in many fermentation processes, a gas-diffusion technique was developed for the online determination of acetic acid. The measurements were accomplished with a flow diffusion analysis (FDA) unit from the TRACE Analytics GmbH, Braunschweig, Germany. The diffusion analysis is based on the UV-absorbance of acetic acid at 205 nm. The measurement was achieved by the separation of an acceptor and a carrier stream (acidified fermentation broth) using a gas permeable polytetrafluoroethylene (PTFE) membrane, whereby broth constituents that would otherwise disturb the UV-measurement of acetic acid, are held back efficiently. Merely, the fermentation by-products, e.g. formic acid, is capable of diffusing through the membrane. While formic acid can disturb the measurement, carbon dioxide does not absorb at 205 nm. The method operates with time-dependent sample enrichment. During the analysis, a small volume of the acceptor stream is stopped for a defined time interval in the acceptor chamber. During this period, the gaseous acetic acid diffuses through the membrane and is enriched in the acceptor chamber. Subsequently after the enrichment, the acceptor stream flows through a UV-detector. The intensity of the signal is proportional to the acetic acid concentration. Online measurements in bioreactors via a sterile filtration probe have been accomplished. A linear calibration in the range of 0.5-5.0 g/L acetic acid with a relative standard deviation of <5 \% was obtained. A sampling rate of 8 samples per hour was possible. The system was applied for the determination of acetic acid in E. coli fermentation broth. The instrument is easy to clean, very user-friendly and does not require any toxic or expensive reagents.},
  language  = {en}
}
@article{WernerKrumbeSchumacheretal.2011,
  author    = {Werner, Frederik and Krumbe, Christoph and Schumacher, Katharina and Groebel, Simone and Spelthahn, Heiko and Stellberg, Michael and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Keusgen, Michael and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Determination of the extracellular acidification of Escherichia coli by a light-addressable potentiometric sensor},
  series = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  journal   = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1862-6319},
  pages     = {1340 -- 1344},
  year      = {2011},
  language  = {en}
}
@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}
}
@inproceedings{HeringUlberTippkoetter2016,
  author    = {Hering, T. and Ulber, Roland and Tippk{\"o}tter, Nils},
  title     = {Development of a screening system for antimicrobial surfaces},
  series = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  booktitle = {New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany},
  publisher = {DECHEMA},
  address   = {Frankfurt am Main},
  pages     = {129},
  year      = {2016},
  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{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}
}
@article{PrielmeierLangSpeedyetal.1987,
  author    = {Prielmeier, Franz and Lang, E. W. and Speedy, R. J. and L{\"u}demann, H.-D.},
  title     = {Diffusion in supercooled water to 300 MPa},
  series = {Physical Review Letters. 59 (1987), H. 10},
  journal   = {Physical Review Letters. 59 (1987), H. 10},
  isbn      = {0031-9007},
  pages     = {1128 -- 1131},
  year      = {1987},
  language  = {en}
}