@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} } @article{Lassonczyk1990, author = {Lassonczyk, Beate}, title = {Characteristics of a fossil soil developed on the basement complex in the northeast Somalia}, series = {Berliner geowissenschaftliche Abhandlungen / Reihe A, Geologie und Pal{\"a}ontologie / hrsg. von d. Geowissenschaftlichen Instituten der Freien u. d. Technischen Universit{\"a}t Berlin. 120 A (1990)}, journal = {Berliner geowissenschaftliche Abhandlungen / Reihe A, Geologie und Pal{\"a}ontologie / hrsg. von d. Geowissenschaftlichen Instituten der Freien u. d. Technischen Universit{\"a}t Berlin. 120 A (1990)}, isbn = {0172-8784}, pages = {713 -- 718}, year = {1990}, language = {en} } @article{SelmerKimDarleyetal.2006, author = {Selmer, Thorsten and Kim, Jihoe and Darley, Daniel and Buckel, Wolfgang}, title = {Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile / Kim, J. ; Darley, D. ; Selmer, T. ; Buckel, W.}, series = {Applied and Environmental Microbiology. 72 (2006), H. 9}, journal = {Applied and Environmental Microbiology. 72 (2006), H. 9}, isbn = {0099-2240}, pages = {6062 -- 6069}, year = {2006}, language = {en} } @article{JossekBongaertsSprenger2001, author = {Jossek, Ralf and Bongaerts, Johannes and Sprenger, Georg A.}, title = {Characterization of a new feedback-resistant 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase AroF of Escherichia coli}, series = {FEMS microbiology letters}, volume = {Vol. 202}, journal = {FEMS microbiology letters}, number = {Iss. 1}, issn = {1574-6968}, pages = {145 -- 148}, year = {2001}, language = {en} } @article{BiselliRechmannFriedrichetal.2007, author = {Biselli, Manfred and Rechmann, Hanrik and Friedrich, Andrea and Forouzan, Dara}, title = {Characterization of photosynthetically active duckweed ( Wolffia australiana ) in vitro culture by Respiration Activity Monitoring System (RAMOS) / Henrik Rechmann, Andrea Friedrich, Dara Forouzan, Stefan Barth, Heide Schnabl, Manfred Biselli und Robert B}, series = {Biotechnology Letters. 29 (2007), H. 6}, journal = {Biotechnology Letters. 29 (2007), H. 6}, isbn = {0141-5492}, pages = {971 -- 977}, year = {2007}, language = {en} } @article{WardoyoNoorElbersetal.2020, author = {Wardoyo, Arinto Y.P. and Noor, Johan A.E. and Elbers, Gereon and Schmitz, Sandra and Flaig, Sascha T. and Budianto, Arif}, title = {Characterizing volcanic ash elements from the 2015 eruptions of bromo and raung volcanoes, Indonesia}, series = {Polish Journal of Environmental Studies}, volume = {29}, journal = {Polish Journal of Environmental Studies}, number = {2}, publisher = {HARD}, address = {Olsztyn}, issn = {2083-5906}, doi = {10.15244/pjoes/99101}, pages = {1899 -- 1907}, year = {2020}, abstract = {The volcanic eruptions of Mt. Bromo and Mt. Raung in East Java, Indonesia, in 2015 perturbed volcanic materials and affected surface-layer air quality at surrounding locations. During the episodes, the volcanic ash from the eruptions influenced visibility, traffic accidents, flight schedules, and human health. In this research, the volcanic ash particles were collected and characterized by relying on the detail of physical observation. We performed an assessment of the volcanic ash elements to characterize the volcanic ash using two different methods which are aqua regia extracts followed by MP-AES and XRF laboratory test of bulk samples. The analysis results showed that the volcanic ash was mixed of many materials, such as Al, Si, P, K, Ca, Ti, V, Cr, Mn, Fe, Ni, and others. Fe, Si, Ca, and Al were found as the major elements, while the others were the trace elements Ba, Cr, Cu, Mn, P, Mn, Ni, Zn, Sb, Sr, and V with the minor concentrations. XRF analyses showed that Fe dominated the elements of the volcanic ash. The XRF analysis showed that Fe was at 35.40\% in Bromo and 43.00\% in Raung of the detected elements in bulk material. The results of aqua regia extracts analyzed by MP-AES were 1.80\% and 1.70\% of Fe element for Bromo and Raung volcanoes, respectively.}, language = {en} } @article{BaumannJahnke1983, author = {Baumann, Marcus and Jahnke, J.}, title = {Chemical and Physical Effects on the Shape and Growth of the Diatom Biddulphia sinensis GREVILLE in Batch Cultures: A Contribution to Bioindication in Plankton Ecology / Jahnke, J. ; Baumann, M.}, series = {Hydrobiological Bulletin . 17 (1983), H. 1}, journal = {Hydrobiological Bulletin . 17 (1983), H. 1}, isbn = {0165-1404}, pages = {5 -- 20}, year = {1983}, language = {en} } @article{SchererZimmermannGoberetal.1993, author = {Scherer, Ulrich W. and Zimmermann, H. P. and Gober, M. K. and Kratz, J. V.}, title = {Chemical Properties of Element 105 in Aqueous Solution: Back Extraction from Triisooctyl Amine into 0.5M HCl / H.P. Zimmermann, M.K. Gober, J.V. Kratz, M. Sch{\"a}del, E. Schimpf, K.E. Gregorich, A. T{\"u}rler, K.R. Czerwinski, N.J. Hannink, B. Kadkhodayan, D.M.}, series = {Radiochimica Acta. 60 (1993)}, journal = {Radiochimica Acta. 60 (1993)}, isbn = {0033-8230}, pages = {11}, year = {1993}, language = {en} } @article{SchererSchaedelBruechleetal.1992, author = {Scherer, Ulrich W. and Sch{\"a}del, M. and Br{\"u}chle, W. and Schimpf, E.}, title = {Chemical Properties of Element 105 in Aqueous Solution: Cation Exchange Separations with \&\#945;-Hydroxyisobutyric Acid / M. Sch{\"a}del, W. Br{\"u}chle, E. Schimpf, H.P. Zimmermann, M.K. Gober, J.V. Kratz, N. Trautmann, H. G{\"a}ggeler, D. Jost, J. Kovacs, U.W. Sche}, series = {Radiochimica Acta. 57 (1992)}, journal = {Radiochimica Acta. 57 (1992)}, isbn = {0033-8230}, pages = {85 -- 92}, year = {1992}, language = {en} } @article{SchererGoberKratzetal.1992, author = {Scherer, Ulrich W. and Gober, M. K. and Kratz, J. V. and Zimmermann, H. P.}, title = {Chemical Properties of Element 105 in Aqueous Solution: Extractions into Diisobutylcarbinol / M.K. Gober, J.V. Kratz, H.P. Zimmermann, M. Sch{\"a}del, W. Br{\"u}chle, E. Schimpf, K.E. Gregorich, A. T{\"u}rler, N.J. Hannink, K.R. Czerwinski, B. Kadkhodayan, D.M. Lee,}, series = {Radiochimica Acta. 57 (1992)}, journal = {Radiochimica Acta. 57 (1992)}, isbn = {0033-8230}, pages = {77 -- 84}, year = {1992}, language = {en} } @article{SchererKratzZimmermannetal.1989, author = {Scherer, Ulrich W. and Kratz, J. V. and Zimmermann, H. P. and Sch{\"a}del, M.}, title = {Chemical Properties of Element 105 in Aqueous Solutions: Halide Complex Formation and Anion Exchange into Triisooctylamine / J.V. Kratz, H.P. Zimmermann, U.W. Scherer, M. Sch{\"a}del, W. Br{\"u}chle, K.E. Gregorich, C.M. Gannett, H.L. Hall, R.A. Henderson, D.M. L}, series = {Radiochimica Acta. 48 (1989)}, journal = {Radiochimica Acta. 48 (1989)}, isbn = {0033-8230}, pages = {121}, year = {1989}, language = {en} }