Refine
Year of publication
- 2024 (8)
- 2023 (18)
- 2022 (20)
- 2021 (12)
- 2020 (13)
- 2019 (16)
- 2018 (22)
- 2017 (12)
- 2016 (44)
- 2015 (30)
- 2014 (47)
- 2013 (29)
- 2012 (40)
- 2011 (28)
- 2010 (36)
- 2009 (30)
- 2008 (16)
- 2007 (20)
- 2006 (17)
- 2005 (20)
- 2004 (15)
- 2003 (14)
- 2002 (19)
- 2001 (18)
- 2000 (12)
- 1999 (16)
- 1998 (31)
- 1997 (25)
- 1996 (19)
- 1995 (36)
- 1994 (29)
- 1993 (21)
- 1992 (27)
- 1991 (15)
- 1990 (20)
- 1989 (20)
- 1988 (19)
- 1987 (16)
- 1986 (11)
- 1985 (7)
- 1984 (10)
- 1983 (10)
- 1982 (3)
- 1981 (3)
- 1980 (3)
- 1979 (8)
- 1978 (2)
- 1976 (2)
- 1975 (3)
- 1973 (2)
- 1972 (2)
- 1971 (2)
Institute
- Fachbereich Chemie und Biotechnologie (918) (remove)
Language
- English (552)
- German (363)
- Multiple languages (2)
- Spanish (1)
Document Type
- Article (604)
- Patent (119)
- Book (66)
- Conference: Meeting Abstract (55)
- Conference Proceeding (35)
- Part of a Book (21)
- Report (6)
- Doctoral Thesis (4)
- Bachelor Thesis (3)
- Conference Poster (1)
Keywords
- Heparin (3)
- Bacillaceae (2)
- Biorefinery (2)
- Biotechnological application (2)
- Butanol (2)
- Chemometrics (2)
- IR spectroscopy (2)
- NMR spectroscopy (2)
- Principal component analysis (2)
- Standardization (2)
The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.
Modulation of muscle-tendon interaction in the human triceps surae during an energy dissipation task
(2017)
The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33–43%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.
The Pharmacokinetics and Metabolism of Lumiracoxib in Chimeric Humanized and Murinized FRG Mice
(2017)
Background
Culture media containing complex compounds like yeast extract or peptone show numerous disadvantages. The chemical composition of the complex compounds is prone to significant variations from batch to batch and quality control is difficult. Therefore, the use of chemically defined media receives more and more attention in commercial fermentations. This concept results in better reproducibility, it simplifies downstream processing of secreted products and enable rapid scale-up. Culturing bacteria with unknown auxotrophies in chemically defined media is challenging and often not possible without an extensive trial-and-error approach. In this study, a respiration activity monitoring system for shake flasks and its recent version for microtiter plates were used to clarify unknown auxotrophic deficiencies in the model organism Bacillus pumilus DSM 18097.
Results
Bacillus pumilus DSM 18097 was unable to grow in a mineral medium without the addition of complex compounds. Therefore, a rich chemically defined minimal medium was tested containing basically all vitamins, amino acids and nucleobases, which are essential ingredients of complex components. The strain was successfully cultivated in this medium. By monitoring of the respiration activity, nutrients were supplemented to and omitted from the rich chemically defined medium in a rational way, thus enabling a systematic and fast determination of the auxotrophic deficiencies. Experiments have shown that the investigated strain requires amino acids, especially cysteine or histidine and the vitamin biotin for growth.
Conclusions
The introduced method allows an efficient and rapid identification of unknown auxotrophic deficiencies and can be used to develop a simple chemically defined tailor-made medium. B. pumilus DSM 18097 was chosen as a model organism to demonstrate the method. However, the method is generally suitable for a wide range of microorganisms. By combining a systematic combinatorial approach based on monitoring the respiration activity with cultivation in microtiter plates, high throughput experiments with high information content can be conducted. This approach facilitates media development, strain characterization and cultivation of fastidious microorganisms in chemically defined minimal media while simultaneously reducing the experimental effort.