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@ARTICLE{Molitor:866201,
      author       = {Molitor, Rebecka and Bollinger, Alexander and Kubicki,
                      Sonja and Loeschcke, Anita and Jaeger, Karl‐Erich and
                      Thies, Stephan},
      title        = {{A}gar plate‐based screening methods for the
                      identification of polyester hydrolysis by {P}seudomonas
                      species},
      journal      = {Microbial biotechnology},
      volume       = {13},
      number       = {1},
      issn         = {1751-7915},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2019-05372},
      pages        = {274-284},
      year         = {2020},
      abstract     = {Hydrolases acting on polyesters like cutin,
                      polycaprolactone or polyethylene terephthalate (PET) are of
                      interest for several biotechnological applications like
                      waste treatment, biocatalysis and sustainable polymer
                      modifications. Recent studies suggest that a large variety
                      of such enzymes are still to be identified and explored in a
                      variety of microorganisms, including bacteria of the genus
                      Pseudomonas. For activity‐based screening, methods have
                      been established using agar plates which contain
                      nanoparticles of polycaprolactone or PET prepared by solvent
                      precipitation and evaporation. In this protocol article, we
                      describe a straightforward agar plate‐based method using
                      emulsifiable artificial polyesters as substrates, namely
                      Impranil® DLN and liquid polycaprolactone diol (PLD).
                      Thereby, the currently quite narrow set of screening
                      substrates is expanded. We also suggest optional
                      pre‐screening with short‐chain and
                      middle‐chain‐length triglycerides as substrates to
                      identify enzymes with lipolytic activity to be further
                      tested for polyesterase activity. We applied these assays to
                      experimentally demonstrate polyesterase activity in bacteria
                      from the P. pertucinogena lineage originating from
                      contaminated soils and diverse marine habitats.},
      cin          = {IMET / IBG-1},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31016871},
      UT           = {WOS:000596580200024},
      doi          = {10.1111/1751-7915.13418},
      url          = {https://juser.fz-juelich.de/record/866201},
}