@article{ElbersPfefferFrieseletal.1993,
  author    = {Elbers, Gereon and Pfeffer, H.-U. and Friesel, J. and Beier, Reinhold},
  title     = {Pilotuntersuchungen gem{\"a}ß dem Verordnungsentwurf nach \S 40, Abs. 2 des Bundesimmissionsschutzgesetzes / H.-U. Pfeffer, J. Friesel, G. Elbers, R. Beier, K. Ellermann},
  series = {Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung : Vortr{\"a}ge und Berichte zum Kolloquium "Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung - Bilanz und Perspektiven" am 11. November 1993 in Essen / [Hrsg.: Landesanstalt f{\"u}r Immissionsschutz Nordrhein-Westfalen. Red. Bearb.: Robert Niesenhaus]},
  journal   = {Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung : Vortr{\"a}ge und Berichte zum Kolloquium "Drei Jahrzehnte Luftqualit{\"a}ts{\"u}berwachung - Bilanz und Perspektiven" am 11. November 1993 in Essen / [Hrsg.: Landesanstalt f{\"u}r Immissionsschutz Nordrhein-Westfalen. Red. Bearb.: Robert Niesenhaus]},
  address   = {Essen},
  pages     = {117},
  year      = {1993},
  language  = {de}
}
@article{RibitschKarlBirnerGruenbergeretal.2010,
  author    = {Ribitsch, Doris and Karl, Wolfgang and Birner-Gruenberger, Ruth and Gruber, Karl and Eiteljoerg, Inge and Remler, Peter and Wieland, Susanne and Siegert, Petra and Maurer, Karl-Heinz and Schwab, Helmut},
  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{AdelsThoennessenMonakhova2024,
  author    = {Adels, Klaudia and Th{\"o}nnessen, Vera and Monakhova, Yulia},
  title     = {Complementary instrumental techniques applied to pain relieving tablets in an undergraduate laboratory experiment},
  series = {Journal of Chemical Education},
  journal   = {Journal of Chemical Education},
  publisher = {ACS},
  issn      = {0021-9584 (Print)},
  doi       = {10.1021/acs.jchemed.4c00681},
  pages     = {11 Seiten},
  year      = {2024},
  abstract  = {Several unconnected laboratory experiments are usually offered for students in instrumental analysis lab. To give the students a more rational overview of the most common instrumental techniques, a new laboratory experiment was developed. Marketed pain relief drugs, familiar consumer products with one to three active components, namely, acetaminophen (paracetamol), acetylsalicylic acid (ASA), and caffeine, were selected. Common analytical methods were compared regarding the performance of qualitative and quantitative analysis of unknown tablets: UV-visible (UV-vis), infrared (IR), and nuclear magnetic resonance (NMR) spectroscopies, as well as high-performance liquid chromatography (HPLC). The students successfully uncovered the composition of formulations, which were divided into three difficulty categories. Students were shown that in addition to simple mixtures handled in theoretical classes, the composition of complex drug products can also be uncovered. By comparing the performance of different techniques, students deepen their understanding and compare the efficiency of analytical methods in the context of complex mixtures. The laboratory experiment can be adjusted for graduate level by including extra tasks such as method optimization, validation, and 2D spectroscopic techniques.},
  language  = {en}
}
@article{RaueWambachGloeggleretal.2014,
  author    = {Raue, Markus and Wambach, M. and Gl{\"o}ggler, Stefan and Grefen, Dana and Kaufmann, R. and Abetz, C. and Georgopanos, Prokopios and Handge, U. A. and Mang, Thomas and Bl{\"u}mich, Bernhard and Abetz, V.},
  title     = {Investigation of historical hard rubber ornaments of Charles Goodyear},
  series = {Macromolecular chemistry and physics},
  volume    = {Vol. 215},
  journal   = {Macromolecular chemistry and physics},
  number    = {No. 3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1022-1352},
  pages     = {245 -- 254},
  year      = {2014},
  language  = {en}
}