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@ARTICLE{Weber:872773,
      author       = {Weber, Joanna and Petrović, Dušan and Strodel, Birgit and
                      Smits, Sander H. J. and Kolkenbrock, Stephan and Leggewie,
                      Christian and Jaeger, Karl-Erich},
      title        = {{I}nteraction of carbohydrate-binding modules with
                      poly(ethylene terephthalate)},
      journal      = {Applied microbiology and biotechnology},
      volume       = {103},
      number       = {12},
      issn         = {1432-0614},
      address      = {New York},
      publisher    = {Springer},
      reportid     = {FZJ-2020-00251},
      pages        = {4801 - 4812},
      year         = {2019},
      abstract     = {Poly(ethylene terephthalate) (PET) is one of the most
                      widely applied synthetic polymers, but its hydrophobicity is
                      challenging for many industrial applications.
                      Biotechnological modification of PET surface can be achieved
                      by PET hydrolyzing cutinases. In order to increase the
                      adsorption towards their unnatural substrate, the enzymes
                      are fused to carbohydrate-binding modules (CBMs) leading to
                      enhanced activity. In this study, we identified novel PET
                      binding CBMs and characterized the CBM-PET interplay. We
                      developed a semi-quantitative method to detect CBMs bound to
                      PET films. Screening of eight CBMs from diverse families for
                      PET binding revealed one CBM that possesses a high affinity
                      towards PET. Molecular dynamics (MD) simulations of the
                      CBM–PET interface revealed tryptophan residues forming an
                      aromatic triad on the peptide surface. Their interaction
                      with phenyl rings of PET is stabilized by additional
                      hydrogen bonds formed between amino acids close to the
                      aromatic triad. Furthermore, the ratio of hydrophobic to
                      polar contacts at the interface was identified as an
                      important feature determining the strength of PET binding of
                      CBMs. The interaction of CBM tryptophan residues with PET
                      was confirmed experimentally by tryptophan quenching
                      measurements after addition of PET nanoparticles to CBM. Our
                      findings are useful for engineering PET hydrolyzing enzymes
                      and may also find applications in functionalization of PET.},
      cin          = {ICS-6 / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)IMET-20090612},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30993383},
      UT           = {WOS:000469192100012},
      doi          = {10.1007/s00253-019-09760-9},
      url          = {https://juser.fz-juelich.de/record/872773},
}