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@ARTICLE{JThiele:856114,
      author       = {J. Thiele, Martin and Davari, Mehdi D. and König, Melanie
                      and Hofmann, Isabell and Junker, Niklas and Mirzaei
                      Garakani, Tayebeh and Vojcic, Ljubica and Fitter, Jörg and
                      Schwaneberg, Ulrich},
      title        = {{E}nzyme-{P}olyelectrolyte {C}omplexes {B}oost the
                      {C}atalytic {P}erformance of {E}nzymes},
      journal      = {ACS catalysis},
      volume       = {8},
      issn         = {2155-5435},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2018-05760},
      pages        = {10876–10887},
      year         = {2018},
      abstract     = {Understanding interactions between polymers and enzymes to
                      boost enzymatic activity is of high importance for
                      application of enzymes in multicomponent systems, such as
                      laundry, food, pharmaceuticals, or cosmetics. Proteases are
                      widely used in industries and increased performance in the
                      presence of polymers has been reported. Boosting of enzymes
                      activity by polymers and understanding of the molecular
                      principles is of high interest in biomedical and
                      biotechnological applications. A molecular understanding of
                      the boosting effect of poly(acrylic acid) (PAA) and
                      poly(l-γ-glutamic acid) (γ-PGA) for a nonspecific
                      subtilisin protease (Protein Database (PDB) ID: 1ST3) was
                      generated through biophysical characterization (fluorescence
                      correlation and circular dichroism spectroscopies,
                      isothermal titration calorimetry), molecular dynamics
                      simulations, and protease reengineering (site-saturation
                      mutagenesis). Our study revealed that enthalpically driven
                      interactions via key amino acid residues close to the
                      protease Ca2+ binding sites cause the boosting effect in
                      protease activity. On the molecular level electrostatic
                      interactions results in the formation of
                      protease-polyelectrolyte complexes. Site-saturation
                      mutagenesis on positions S76, I77, A188, V238, N242, and
                      K245 yielded an increased proteolytic performance against a
                      complex protein mixture (trademark CO-3; up to $∼300\%$
                      and $∼70\%)$ in the presence of PAA and γ-PGA. Being able
                      to fine-tune interactions between proteins and negatively
                      charged polymers through integrative use of computational
                      design, protein re-engineering and biophysical
                      characterization proved to be an efficient workflow to
                      improve protease performance.},
      cin          = {ICS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-5-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000449723900099},
      doi          = {10.1021/acscatal.8b02935},
      url          = {https://juser.fz-juelich.de/record/856114},
}