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Träfflista för sökning "WFRF:(Holst Olle) ;pers:(de Maré Lena)"

Sökning: WFRF:(Holst Olle) > De Maré Lena

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1.
  • de Maré, Lena, et al. (författare)
  • A cultivation technique for E. coli fed-batch cultivations operating close to the maximum oxygen transfer capacity of the reactor
  • 2005
  • Ingår i: Biotechnology Letters. - : Springer Science and Business Media LLC. - 0141-5492 .- 1573-6776. ; 27:14, s. 983-990
  • Tidskriftsartikel (refereegranskat)abstract
    • A cultivation strategy combining the advantages of temperature-limited fed-batch and probing feeding control is presented. The technique was evaluated in fed-batch cultivations with E. coli BL21(DE3) producing xylanase in a 3 liter bioreactor. A 20% increase in cell mass was achieved and the usual decrease in specific enzyme activity normally observed during the late production phase was diminished with the new technique. The method was further tested by growing E. coli W3110 in a larger bioreactor (50 l). It is a suitable cultivation technique when the O2 transfer capacity of the reactor is reached and it is desired to continue to produce the recombinant protein.
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2.
  • de Maré, Lena, et al. (författare)
  • Temperature limited fed-batch cultivation with a probing feeding strategy for Escherichia coli
  • 2004
  • Ingår i: Computer Applications in Biotechnology 2004. - 008044251X ; , s. 73-79
  • Konferensbidrag (refereegranskat)abstract
    • A cultivation strategy combining the advantages of temperature limitedfed-batch and probing control is presented.This is a suitable way to produce recombinant proteins while minimizing therelease of endotoxins which complicates the downstream processing.The downside with the temperature limited fed-batch technique has been the difficulty to achieve a controlled excess of glucose inthe reactor without the accumulation of acetic acid when usingstandard sensors.A method using a probing feeding strategy withdown-pulses is here suggested. The technique is investigated insimulations and experiments.
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3.
  • Ramchuran, Santosh, et al. (författare)
  • Production of heterologous thermostable glycoside hydrolases and the presence of host-cell proteases in substrate limited fed-batch cultures of Escherichia coli BL21(DE3)
  • 2002
  • Ingår i: Applied Microbiology and Biotechnology. - : Springer Science and Business Media LLC. - 1432-0614 .- 0175-7598. ; 60:4, s. 408-416
  • Tidskriftsartikel (refereegranskat)abstract
    • Metabolic stress is a phenomenon often discussed in conjunction with recombinant protein production in Escherichia coli. This investigation shows how heterologous protein production, and the presence of host cell proteases is related to: i) IPTG induction, ii) cell mass concentration at the time of induction and iii) the presence of metabolites (glutamic acid or those from TSB) during the post induction phase of high-cell-density (HCD) fed-batch cultivations. Two thermostable xylanase variants and one thermostable cellulase, all originating from Rhodothermus marinus were expressed in E. coli strain BL21 (DE3). A three-fold difference in the specific activity of both xylanase variants [between 7000 and 21000 U / (g cdw)], was observed under the different conditions tested. Upon induction at high cell-mass concentrations employing a nutrient feed devoid of the metabolites above, the specific activity of the xylanase variants, was initially higher but decreased 2-3 h into the post induction phase and simultaneously protease activity was detected. Furthermore, protease activity was detected in all induced cultivations employing this nutrient feed, but was undetected in uninduced control cultivations (final cell mass concentration of 40 g/L), as well as in induced cultivations employing metabolite supplemented nutrient feeds. By contrast, maximum specific cellulase activity [between 700 and 900 U / (g cdw)] remained relatively unaffected in all cases. We have established that detectable host cell proteases was not the primary reason for the post-induction activity decrease observed under certain conditions, and possible causes for the differing production levels of heterologous proteins are discussed.
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