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@ARTICLE{Fricke:886113,
      author       = {Fricke, Philipp Moritz and Link, Tobias and Gätgens,
                      Jochem and Sonntag, Christiane and Otto, Maike and Bott,
                      Michael and Polen, Tino},
      title        = {{A} tunable l-arabinose-inducible expression plasmid for
                      the acetic acid bacterium {G}luconobacter oxydans},
      journal      = {Applied microbiology and biotechnology},
      volume       = {104},
      number       = {21},
      issn         = {1432-0614},
      address      = {New York},
      publisher    = {Springer},
      reportid     = {FZJ-2020-04276},
      pages        = {9267 - 9282},
      year         = {2020},
      note         = {Biotechnologie 1},
      abstract     = {The acetic acid bacterium (AAB) Gluconobacter oxydans
                      incompletely oxidizes a wide variety of carbohydrates and is
                      therefore used industrially for oxidative
                      biotransformations. For G. oxydans, no system was available
                      that allows regulatable plasmid-based expression. We found
                      that the l-arabinose-inducible PBAD promoter and the
                      transcriptional regulator AraC from Escherichia coli MC4100
                      performed very well in G. oxydans. The respective
                      pBBR1-based plasmids showed very low basal expression of the
                      reporters β-glucuronidase and mNeonGreen, up to 480-fold
                      induction with $1\%$ l-arabinose, and tunability from 0.1 to
                      $1\%$ l-arabinose. In G. oxydans 621H, l-arabinose was
                      oxidized by the membrane-bound glucose dehydrogenase, which
                      is absent in the multi-deletion strain BP.6. Nevertheless,
                      AraC-PBAD performed similar in both strains in the
                      exponential phase, indicating that a gene knockout is not
                      required for application of AraC-PBAD in wild-type G.
                      oxydans strains. However, the oxidation product arabinonic
                      acid strongly contributed to the acidification of the growth
                      medium in 621H cultures during the stationary phase, which
                      resulted in drastically decreased reporter activities in
                      621H (pH 3.3) but not in BP.6 cultures (pH 4.4). These
                      activities could be strongly increased quickly solely by
                      incubating stationary cells in d-mannitol-free medium
                      adjusted to pH 6, indicating that the reporters were hardly
                      degraded yet rather became inactive. In a pH-controlled
                      bioreactor, these reporter activities remained high in the
                      stationary phase (pH 6). Finally, we created a multiple
                      cloning vector with araC-PBAD based on pBBR1MCS-5. Together,
                      we demonstrated superior functionality and good tunability
                      of an AraC-PBAD system in G. oxydans that could possibly
                      also be used in other AAB.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32974745},
      UT           = {WOS:000572606200002},
      doi          = {10.1007/s00253-020-10905-4},
      url          = {https://juser.fz-juelich.de/record/886113},
}