@article{SelmerMiechDierksetal.1998, author = {Selmer, Thorsten and Miech, Claudia and Dierks, Thomas and Figura, Kurt von}, title = {Arylsulfatase from Klebsiella pneumoniae Carries a Formylglycine Generated from a Serine / Miech, Claudia ; Dierks, Thomas ; Selmer, Thorsten ; Figura, Kurt von ; Schmidt, Bernd}, series = {Journal of Biological Chemistry. 273 (1998), H. 9}, journal = {Journal of Biological Chemistry. 273 (1998), H. 9}, isbn = {1083-351X}, pages = {4835 -- 4837}, year = {1998}, language = {en} } @article{InfantinoPaulssenMostaccietal.2016, author = {Infantino, Angelo and Paulßen, Elisabeth and Mostacci, Domiziano and Schaffer, Paul and Trinczek, Michael and Hoehr, Cornelia}, title = {Assessment of the production of medical isotopes using the Monte Carlo code FLUKA: Simulations against experimental measurements}, series = {Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms}, volume = {366}, journal = {Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1872-9584}, doi = {10.1016/j.nimb.2015.10.067}, pages = {117 -- 123}, year = {2016}, abstract = {The Monte Carlo code FLUKA is used to simulate the production of a number of positron emitting radionuclides, ¹⁸F, ¹³N, ⁹⁴Tc, ⁴⁴Sc, ⁶⁸Ga, ⁸⁶Y, ⁸⁹Zr, ⁵²Mn, ⁶¹Cu and ⁵⁵Co, on a small medical cyclotron with a proton beam energy of 13 MeV. Experimental data collected at the TR13 cyclotron at TRIUMF agree within a factor of 0.6 ± 0.4 with the directly simulated data, except for the production of ⁵⁵Co, where the simulation underestimates the experiment by a factor of 3.4 ± 0.4. The experimental data also agree within a factor of 0.8 ± 0.6 with the convolution of simulated proton fluence and cross sections from literature. Overall, this confirms the applicability of FLUKA to simulate radionuclide production at 13 MeV proton beam energy.}, language = {en} } @article{ReugelsBoggettiScheeretal.2006, author = {Reugels, Alexander M. and Boggetti, Barbara and Scheer, Nico and Campos-Ortega, Jos{\´e} A.}, title = {Asymmetric localization of Numb:EGFP in dividing neuroepithelial cells during neurulation in Danio rerio}, series = {Developmental Dynamics}, volume = {235}, journal = {Developmental Dynamics}, number = {4}, issn = {1097-0177}, doi = {10.1002/dvdy.20699}, pages = {934 -- 948}, year = {2006}, language = {en} } @article{BiselliVanderPolDeGooijeretal.1996, author = {Biselli, Manfred and Van der Pol, Jens J. and De Gooijer, Cornelis D. and Wandrey, Christian}, title = {Automation of selective assays for on-line bioprocess monitoring by flow-injection analysis / van der Pol, Jens J. ; de Gooijer, Cornelis D. ; Biselli, Manfred ; Wandrey, Christian ; Tramper, Johannes}, series = {Trends in Biotechnology. 14 (1996), H. 12}, journal = {Trends in Biotechnology. 14 (1996), H. 12}, isbn = {0167-7799}, pages = {471 -- 477}, year = {1996}, language = {en} } @article{HandtkeSchroeterJuergenetal.2014, author = {Handtke, Stefan and Schroeter, Rebecca and J{\"u}rgen, Britta and Methling, Karen and Schl{\"u}ter, Rabea and Albrecht, Dirk and Hijum, Sacha A. F. T. van and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Schweder, Thomas and Hecker, Michael and Voigt, Birgit}, title = {Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress}, series = {PLOS one}, volume = {9}, journal = {PLOS one}, number = {1}, publisher = {PLOS}, address = {San Francisco}, issn = {1932-6203}, doi = {10.1371/journal.pone.0085625}, pages = {e85625}, year = {2014}, abstract = {Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.}, language = {en} } @article{SelmerJennemannBaueretal.1999, author = {Selmer, Thorsten and Jennemann, Richard and Bauer, Bernhard L. and Bertalanffy, Helmut}, title = {Basidiolipids from Agaricus are novel immune adjuvants / Jennemann, R. ; Bauer, BL. ; Bertalanffy, H. ; Selmer, T. ; Wiegandt, H.}, series = {Immunobiology. 200 (1999), H. 2}, journal = {Immunobiology. 200 (1999), H. 2}, isbn = {0171-2985}, pages = {277 -- 289}, year = {1999}, language = {en} } @article{BiselliThoemmesKulaetal.1994, author = {Biselli, Manfred and Th{\"o}mmes, J. and Kula, M.-R. and Wandrey, Christian}, title = {Batch kinetic data of hybridoma growth and productivity as a basis for the simulation of antibody production in various culture systems / Th{\"o}mmes, J. ; Biselli, M. ; Kula, M.-R. ; Wandrey, C.}, series = {Animal cell technology : products of today, prospects for tomorrow ; ESACT, European Society for Animal Cell Technology, the 12th meeting / Ed. R. E. Spier}, journal = {Animal cell technology : products of today, prospects for tomorrow ; ESACT, European Society for Animal Cell Technology, the 12th meeting / Ed. R. E. Spier}, publisher = {Butterworth-Heinemann}, address = {Oxford}, isbn = {0750618450}, pages = {513 -- 517}, year = {1994}, language = {en} } @article{BurgerLindnerRumpfetal.2022, author = {Burger, Ren{\´e} and Lindner, Simon and Rumpf, Jessica and Do, Xuan Tung and Diehl, Bernd W.K. and Rehahn, Matthias and Monakhova, Yulia and Schulze, Margit}, title = {Benchtop versus high field NMR: Comparable performance found for the molecular weight determination of lignin}, series = {Journal of Pharmaceutical and Biomedical Analysis}, volume = {212}, journal = {Journal of Pharmaceutical and Biomedical Analysis}, number = {Article number: 114649}, publisher = {Elsevier}, address = {New York, NY}, isbn = {0731-7085}, doi = {10.1016/j.jpba.2022.114649}, year = {2022}, abstract = {Lignin is a promising renewable biopolymer being investigated worldwide as an environmentally benign substitute of fossil-based aromatic compounds, e.g. for the use as an excipient with antioxidant and antimicrobial properties in drug delivery or even as active compound. For its successful implementation into process streams, a quick, easy, and reliable method is needed for its molecular weight determination. Here we present a method using 1H spectra of benchtop as well as conventional NMR systems in combination with multivariate data analysis, to determine lignin's molecular weight (Mw and Mn) and polydispersity index (PDI). A set of 36 organosolv lignin samples (from Miscanthus x giganteus, Paulownia tomentosa and Silphium perfoliatum) was used for the calibration and cross validation, and 17 samples were used as external validation set. Validation errors between 5.6\% and 12.9\% were achieved for all parameters on all NMR devices (43, 60, 500 and 600 MHz). Surprisingly, no significant difference in the performance of the benchtop and high-field devices was found. This facilitates the application of this method for determining lignin's molecular weight in an industrial environment because of the low maintenance expenditure, small footprint, ruggedness, and low cost of permanent magnet benchtop NMR systems.}, language = {en} } @article{IdingDuennwaldGreineretal.2000, author = {Iding, Hans and D{\"u}nnwald, Thomas and Greiner, Lasse and Liese, Andreas and M{\"u}ller, Michael and Siegert, Petra and Gr{\"o}tzinger, Joachim and Demir, Ayhan S. and Pohl, Martina}, title = {Benzoylformate Decarboxylase from Pseudomonas putida as Stable Catalyst for the Synthesis of Chiral 2-Hydroxy Ketones}, series = {Chemistry - a European journal}, volume = {Vol. 6}, journal = {Chemistry - a European journal}, number = {Iss. 8}, issn = {1521-3765 (E-Journal); 0947-6539 (Print)}, pages = {1483 -- 1495}, year = {2000}, language = {en} } @article{SelmerNetzPohletal.2002, author = {Selmer, Thorsten and Netz, Daili Jacqueline Aguilar and Pohl, Regula and Beck-Sickinger, Annette G.}, title = {Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus / Netz, Daili Jacqueline Aguilar ; Pohl, Regula ; Beck-Sickinger, Annette G. ; Selmer, Thorsten ; Pierik, Antonio J. ; Carmo de Frei}, series = {Journal of Molecular Biology. 319 (2002), H. 3}, journal = {Journal of Molecular Biology. 319 (2002), H. 3}, isbn = {0022-2836}, pages = {745 -- 756}, year = {2002}, language = {en} } @article{FalkenbergKohnBottetal.2023, author = {Falkenberg, Fabian and Kohn, Sophie and Bott, Michael and Bongaerts, Johannes and Siegert, Petra}, title = {Biochemical characterisation of a novel broad pH spectrum subtilisin from Fictibacillus arsenicus DSM 15822ᵀ}, series = {FEBS Open Bio}, volume = {13}, journal = {FEBS Open Bio}, number = {11}, publisher = {Wiley}, address = {Hoboken, NJ}, issn = {2211-5463}, doi = {10.1002/2211-5463.13701}, pages = {2035 -- 2046}, year = {2023}, abstract = {Subtilisins from microbial sources, especially from the Bacillaceae family, are of particular interest for biotechnological applications and serve the currently growing enzyme market as efficient and novel biocatalysts. Biotechnological applications include use in detergents, cosmetics, leather processing, wastewater treatment and pharmaceuticals. To identify a possible candidate for the enzyme market, here we cloned the gene of the subtilisin SPFA from Fictibacillus arsenicus DSM 15822ᵀ (obtained through a data mining-based search) and expressed it in Bacillus subtilis DB104. After production and purification, the protease showed a molecular mass of 27.57 kDa and a pI of 5.8. SPFA displayed hydrolytic activity at a temperature optimum of 80 °C and a very broad pH optimum between 8.5 and 11.5, with high activity up to pH 12.5. SPFA displayed no NaCl dependence but a high NaCl tolerance, with decreasing activity up to concentrations of 5 m NaCl. The stability enhanced with increasing NaCl concentration. Based on its substrate preference for 10 synthetic peptide 4-nitroanilide substrates with three or four amino acids and its phylogenetic classification, SPFA can be assigned to the subgroup of true subtilisins. Moreover, SPFA exhibited high tolerance to 5\% (w/v) SDS and 5\% H₂O₂ (v/v). The biochemical properties of SPFA, especially its tolerance of remarkably high pH, SDS and H₂O₂, suggest it has potential for biotechnological applications.}, language = {en} } @article{FalkenbergRahbaFischeretal.2022, author = {Falkenberg, Fabian and Rahba, Jade and Fischer, David and Bott, Michael and Bongaerts, Johannes and Siegert, Petra}, title = {Biochemical characterization of a novel oxidatively stable, halotolerant, and high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T}, series = {FEBS Open Bio}, volume = {12}, journal = {FEBS Open Bio}, number = {10}, publisher = {Wiley}, address = {Hoboken, NJ}, issn = {2211-5463}, doi = {10.1002/2211-5463.13457}, pages = {1729 -- 1746}, year = {2022}, abstract = {Halophilic and halotolerant microorganisms represent a promising source of salt-tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T. The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high-alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0-12.0 and temperature 20-80 °C, optimally at pH 9.0-9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58\% of residual activity when incubated at 10 °C with 5\% (v/v) H2O2 for 1 h while stimulated at 1\% (v/v) H2O2. Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m. This study demonstrates the potential of SPAO for biotechnological applications in the future.}, language = {en} } @article{MaggakisKelemenBorkKayseretal.2003, author = {Maggakis-Kelemen, C. and Bork, M. and Kayser, Peter and Biselli, Manfred and Artmann, Gerhard}, title = {Biological and mechanical quality of red blood cells cultured from human umbilical cord blood stem cells}, series = {Medical and biological engineering and computing. 41 (2003), H. 3}, journal = {Medical and biological engineering and computing. 41 (2003), H. 3}, isbn = {0140-0118}, pages = {350 -- 356}, year = {2003}, language = {en} } @article{BiselliHilbertJelineketal.2001, author = {Biselli, Manfred and Hilbert, U. and Jelinek, N. and Schmidt, S.}, title = {Bioprocess development for the cultivation of human T-lymphocytes / Hilbert, U. ; Jelinek, N. Schmidt, S. ; Biselli, M.}, series = {Engineering in Life Sciences. 1 (2001)}, journal = {Engineering in Life Sciences. 1 (2001)}, isbn = {1618-0240}, pages = {20 -- 23}, year = {2001}, language = {en} } @article{AlKaidyDuweHusteretal.2015, author = {Al-Kaidy, Huschyar and Duwe, Anna and Huster, Manuel and Muffler, Kai and Schlegel, Christin and Tim, Sieker and Stadtm{\"u}ller, Ralf and Tippk{\"o}tter, Nils and Ulber, Roland}, title = {Biotechnology and bioprocess engineering - from the first ullmann's article to recent trends}, series = {ChemBioEng Reviews}, volume = {2}, journal = {ChemBioEng Reviews}, number = {3}, publisher = {Wiley}, address = {Weinheim}, doi = {10.1002/cben.201500008}, pages = {175 -- 184}, year = {2015}, abstract = {For several thousand years, biotechnology and its associated technical processes have had a great impact on the development of mankind. Based on empirical methods, in particular for the production of foodstuffs and daily commodities, these disciplines have become one of the most innovative future issues. Due to the increasing detailed understanding of cellular processes, production strains can now be optimized. In combination with modern bioprocesses, a variety of bulk and fine chemicals as well as pharmaceuticals can be produced efficiently. In this article, some of the current trends in biotechnology are discussed.}, language = {en} } @article{RibitschKarlBirnerGruenbergeretal.2010, author = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.}, title = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli}, series = {Journal of biotechnology}, volume = {150}, journal = {Journal of biotechnology}, number = {3}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2010.09.947}, pages = {408 -- 416}, year = {2010}, abstract = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.}, language = {en} } @article{JablonskiMuenstermannNorketal.2021, author = {Jablonski, Melanie and M{\"u}nstermann, Felix and Nork, Jasmina and Molinnus, Denise and Muschallik, Lukas and Bongaerts, Johannes and Wagner, Torsten and Keusgen, Michael and Siegert, Petra and Sch{\"o}ning, Michael Josef}, title = {Capacitive field-effect biosensor applied for the detection of acetoin in alcoholic beverages and fermentation broths}, series = {physica status solidi (a) applications and materials science}, volume = {218}, journal = {physica status solidi (a) applications and materials science}, number = {13}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.202000765}, pages = {7 Seiten}, year = {2021}, abstract = {An acetoin biosensor based on a capacitive electrolyte-insulator-semiconductor (EIS) structure modified with the enzyme acetoin reductase, also known as butane-2,3-diol dehydrogenase (Bacillus clausii DSM 8716ᵀ), is applied for acetoin detection in beer, red wine, and fermentation broth samples for the first time. The EIS sensor consists of an Al/p-Si/SiO₂/Ta₂O₅ layer structure with immobilized acetoin reductase on top of the Ta₂O₅ transducer layer by means of crosslinking via glutaraldehyde. The unmodified and enzyme-modified sensors are electrochemically characterized by means of leakage current, capacitance-voltage, and constant capacitance methods, respectively.}, language = {en} } @article{HandtkeVollandMethlingetal.2014, author = {Handtke, Stefan and Volland, Sonja and Methling, Karen and Albrecht, Dirk and Becher, D{\"o}rte and Nehls, Jenny and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Liesegang, Heiko and Voigt, Birgit and Daniel, Rolf and Hecker, Michael}, title = {Cell physiology of the biotechnological relevant bacterium Bacillus pumilus - An omics-based approach}, series = {Journal of Biotechnology}, journal = {Journal of Biotechnology}, number = {192(A)}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2014.08.028}, pages = {204 -- 214}, year = {2014}, abstract = {Members of the species Bacillus pumilus get more and more in focus of the biotechnological industry as potential new production strains. Based on exoproteome analysis, B. pumilus strain Jo2, possessing a high secretion capability, was chosen for an omics-based investigation. The proteome and metabolome of B. pumilus cells growing either in minimal or complex medium was analyzed. In total, 1542 proteins were identified in growing B. pumilus cells, among them 1182 cytosolic proteins, 297 membrane and lipoproteins and 63 secreted proteins. This accounts for about 43\% of the 3616 proteins encoded in the B. pumilus Jo2 genome sequence. By using GC-MS, IP-LC/MS and H NMR methods numerous metabolites were analyzed and assigned to reconstructed metabolic pathways. In the genome sequence a functional secretion system including the components of the Sec- and Tat-secretion machinery was found. Analysis of the exoproteome revealed secretion of about 70 proteins with predicted secretion signals. In addition, selected production-relevant genome features such as restriction modification systems and NRPS clusters of B. pumilus Jo2 are discussed.}, language = {en} } @article{KochWunderlichSeibleretal.2008, author = {Koch, Linda and Wunderlich, F. Thomas and Seibler, Jost and K{\"o}nner, A. Christine and Hampel, Brigitte and Irlenbusch, Sigrid and Brabant, Georg and Kahn, C. Ronald and Schwenk, Frieder and Br{\"u}ning, Jens C.}, title = {Central insulin action regulates peripheral glucose and fat metabolism in mice}, series = {The Journal of Clinical Investigation (JCI)}, volume = {118}, journal = {The Journal of Clinical Investigation (JCI)}, number = {6}, issn = {1558-8238}, doi = {10.1172/JCI31073}, pages = {2132 -- 2147}, year = {2008}, language = {en} } @article{PrielmeierNagatomoFrahm1994, author = {Prielmeier, Franz and Nagatomo, Yasushi and Frahm, Jens}, title = {Cerebral blood oxygenation in rat brain during hypoxic hypoxia. Quantitative MRI of effective transverse relaxation rates}, series = {Magnetic Resonance in Medicine. 31 (1994), H. 6}, journal = {Magnetic Resonance in Medicine. 31 (1994), H. 6}, isbn = {0740-3194}, pages = {678 -- 681}, year = {1994}, language = {en} }