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  • Artikel: DFG Deutsche Nationallizenzen  (6)
  • 1985-1989  (6)
Datenquelle
  • Artikel: DFG Deutsche Nationallizenzen  (6)
Materialart
Erscheinungszeitraum
Jahr
  • 1
    Digitale Medien
    Digitale Medien
    Covalent modification of proteins in Bacillus subtilis during the process of sporulation, germination and outgrowth (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 57 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Cells of Bacillus subtilis 168+ were labeled with 32P-orthophosphate during the process of sporulation, germination and outgrowth. By two-dimensional gel electrophoresis, at least 30 protein species were found to be radioactively labeled; 30% of these were modified by phosphorylation. Significant changes in the protein phosphorylation pattern during growth and cellular differentiation could be demonstrated. Using γ-32P-ATP evidence for an ATP-dependent protein kinase was also obtained. Under these conditions 4 proteins with a molecular mass of 109 600; 103 100; 73 300 and 32 200 Da were found to be phosphorylated.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03226.x
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Changes in the cell envelope structure of Clostridium sp. strain EM1 during massive production of α-amylase and pullulanase (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 41 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Marked changes in cell envelope structure were observed when Clostridium sp. strain EM1 cells grown in continuous culture under glucose limitation were compared with cells grown under starch limitation. The increase in the level of extracellular α-amylase and pullulanase during starch-limited growth was parallelled by degradation of the cell-envelope layer and the formation of blebs and a high number of vesicles, which apparently originated from the cytoplasmic membrane. These vesicles were covered by a delicate layer of small particles and were shown to be released into the culture fluid. It is assumed that the overproduction of enzyme destined to remain associated with the cells led to these changes.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02195.x
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    In vivo phosphorylation of proteins in Clostridium sphenoides (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 27 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Cell contents of Clostridium sphenoides, labeled with [32P]orthophosphate under strict anaerobic conditions, were analyzed by two-dimensional gel electrophoresis. Autoradiography of these gels demonstrated the presence of at least 15 32P-labeled protein species, of which Mr and iso-electric point were determined. Treatment of the radioactively labeled cell contents with alkaline phosphatase and acid phosphatase showed that all these proteins were modified by phosphorylation. These findings demonstrate for the first time the presence of phosphorproteins in a strictly anaerobic bacterium.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb01653.x
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  • 4
    Digitale Medien
    Digitale Medien
    Conditions for the overproduction and excretion of thermostable α-amylase and pullulanase from Clostridium thermohydrosulfuricum DSM 567 (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 75-81 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary Conditions in continuous culture were identified under which thermostable α-amylase and pullulanase were overproduced and excreted by Clostridium thermohydrosulfuricum DSM 567. Maximal amounts of these enzymes were formed at a dilution rate of 0.05/h at pH of 6.5 and under starch limitation. Unlike the results obtained in batch culture, more than 90% of the enzymes were released into the culture fluid. In addition, the concentration of these enzymes was raised 50- to 100-fold. A shift in fermentation products (more lactate and less acetate production) was observed, when the concentration of ferrous ions in the medium was decreased from 23 μM to 6.5 μM.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00257257
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  • 5
    Digitale Medien
    Digitale Medien
    Identification of a starch degrading anaerobic thermophile producing thermostable α-amylase and pullulanase (1989)
    Springer
    Applied microbiology and biotechnology 30 (1989), S. 422-425 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary A thermophilic bacterium which was recently isolated and designated Clostridium sp. EM1 has been now identified and characterized. On the basis of its physiological characeristics and DNA-DNA homology data, the strain was designated as Clostridium thermosulfurogenes (DSM 3896). The guanine-plus-cytosine (G+C) content (mol%) of the DNA was determined to be 37%.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00296634
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  • 6
    Digitale Medien
    Digitale Medien
    Highly active and thermostable amylases and pullulanases from various anaerobic thermophiles (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 192-198 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary High concentrations of amylases and pullulanases were formed by continuous cultivation of Thermoanaerobacter finnii, Thermobacteroides acetoethylicus, Thermoanaerobacter ethanolicus and Clostridium thermosaccharolyticum in chemostats under starch limitation. 70% to 98% of these enzymes were transported and released into the culture fluid. These extracellular enzymes were extremely thermostable under aerobic conditions and in the absence of substrate and metal ions. The amylases and pullulanases from the first three organisms had an optimal temperature of 90°C. The enzymes from C. thermosaccharolyticum were most active at 75°C. The pH optima of the amylolytic enzymes from the microorganisms investigated ranged between 5 and 6. The addition of calcium ions in vitro significantly enhanced pullulanase activity from T. finnii and C. thermosaccharolyticum. The influence of other metal ions and cyclodextrins on the activities of the amylolytic enzymes is also described.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00251944
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