TY - JOUR A1 - Selmer, Thorsten A1 - Andrei, Paula I. T1 - p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol JF - European Journal of Biochemistry. 268 (2001), H. 5 Y1 - 2001 SN - 0014-2956 SP - 1363 EP - 1372 ER - TY - JOUR A1 - Biselli, Manfred A1 - Born, C. A1 - Wandrey, C. T1 - Oxygen transfer from the gasphase to the immobilized cells in membrane aerated fluidized beds / Born, C. ; Biselli, M. ; Wandrey, C. JF - Animal cell technology : basic & applied aspects : proceedings of the Eighth Annual Meeting of the Japanese Association for Animal Cell Technology, Iizuka, Fukuoka, Japan, November 6-10, 1995 / edited by K. Funatsu, Y. Shirai, and T. Matsushita Y1 - 1995 SN - 0-7923-4486-3 N1 - Japanese Association for Animal Cell Technology. ; Meeting ; <8 ; 1995 : ; Iizuka-shi, Japan> SP - 83 EP - 87 PB - Kluwer Acad. Press CY - Boston ER - TY - JOUR A1 - Unden, G. A1 - Becker, S. A1 - Bongaerts, Johannes A1 - Schirawski, J. A1 - Six, S. T1 - Oxygen regulated gene expression in facultatively anaerobic bacteria JF - Antonie van Leeuwenhoek Y1 - 1994 SN - 0003-6072 (Print) ; 1572-9699 (online) VL - Vol. 66 IS - Iss. 1-3 SP - 3 EP - 22 ER - TY - JOUR A1 - Selmer, Thorsten A1 - Buckel, Wolfgang T1 - Oxygen Exchange between Acetate and the Catalytic Glutamate Residue in Glutaconate CoA-transferase from Acidaminococcus fermentans. IMPLICATIONS FOR THE MECHANISM OF CoA-ESTER HYDROLYSIS JF - Journal of Biological Chemistry. 274 (1999), H. 30 Y1 - 1999 SN - 1083-351X SP - 20772 EP - 20778 ER - TY - PAT A1 - Jeromin, Günter Erich T1 - Organische Radikale, deren Herstellung und Verwendung : Offenlegungsschrift DE10056740A1 ; Offenlegungstag: 23.05.2002 Y1 - 2002 N1 - Volltext über Datenbank: http://publikationen.dpma.de/ PB - Deutsches Patent- und Markenamt CY - München ER - TY - BOOK A1 - Jeromin, Günter Erich T1 - Organische Chemie : Ein praxisbezogenes Lehrbuch. Korr. Nachdr. der 2. Aufl. Y1 - 2008 SN - 3-8171-1732-9 PB - Deutsch CY - Frankfurt am Main ER - TY - BOOK A1 - Jeromin, Günter Erich T1 - Organische Chemie : ein praxisbezogenes Lehrbuch. - 2. Aufl. Y1 - 2006 SN - 3-8171-1732-9 PB - Deutsch CY - Frankfurt am Main ER - TY - JOUR A1 - Penner, Crystal A1 - Usherovich, Samuel A1 - Niedermeier, Jana A1 - Bélanger-Champagne, Camille A1 - Trinczek, Michael A1 - Paulßen, Elisabeth A1 - Hoehr, Cornelia T1 - Organic Scintillator-Fibre Sensors for Proton Therapy Dosimetry: SCSF-3HF and EJ-260 JF - electronics N2 - In proton therapy, the dose from secondary neutrons to the patient can contribute to side effects and the creation of secondary cancer. A simple and fast detection system to distinguish between dose from protons and neutrons both in pretreatment verification as well as potentially in vivo monitoring is needed to minimize dose from secondary neutrons. Two 3 mm long, 1 mm diameter organic scintillators were tested for candidacy to be used in a proton–neutron discrimination detector. The SCSF-3HF (1500) scintillating fibre (Kuraray Co. Chiyoda-ku, Tokyo, Japan) and EJ-260 plastic scintillator (Eljen Technology, Sweetwater, TX, USA) were irradiated at the TRIUMF Neutron Facility and the Proton Therapy Research Centre. In the proton beam, we compared the raw Bragg peak and spread-out Bragg peak response to the industry standard Markus chamber detector. Both scintillator sensors exhibited quenching at high LET in the Bragg peak, presenting a peak-to-entrance ratio of 2.59 for the EJ-260 and 2.63 for the SCSF-3HF fibre, compared to 3.70 for the Markus chamber. The SCSF-3HF sensor demonstrated 1.3 times the sensitivity to protons and 3 times the sensitivity to neutrons as compared to the EJ-260 sensor. Combined with our equations relating neutron and proton contributions to dose during proton irradiations, and the application of Birks’ quenching correction, these fibres provide valid candidates for inexpensive and replicable proton-neutron discrimination detectors Y1 - 2022 U6 - https://doi.org/10.3390/electronics12010011 SN - 2079-9292 N1 - This article belongs to the Special Issue "Applications of Optical Fiber Sensors" VL - 12 IS - 1 PB - MDPI CY - Basel ER - TY - JOUR A1 - Hoffstadt, Kevin A1 - Nikolausz, Marcell A1 - Krafft, Simone A1 - Bonatelli, Maria A1 - Kumar, Vivekanantha A1 - Harms, Hauke A1 - Kuperjans, Isabel T1 - Optimization of the ex situ biomethanation of hydrogen and carbon dioxide in a novel meandering plug flow reactor: start-up phase and flexible operation JF - Bioengineering KW - methanation KW - plug flow reactor KW - bubble column KW - biomethane KW - P2G Y1 - 2024 U6 - https://doi.org/10.3390/bioengineering11020165 SN - 2306-5354 VL - 11 IS - 2 PB - MDPI CY - Basel ER - TY - JOUR A1 - Degering, Christian A1 - Eggert, Thorsten A1 - Puls, Michael A1 - Bongaerts, Johannes A1 - Evers, Stefan A1 - Maurer, Karl-Heinz A1 - Jaeger, Karl-Erich T1 - Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides JF - Applied and environmental microbiology N2 - Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains. Y1 - 2010 U6 - https://doi.org/10.1128/AEM.01146-10 SN - 1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print) VL - 76 IS - 19 SP - 6370 EP - 6378 PB - American Society for Microbiology CY - Washington, DC ER -