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@ARTICLE{Capo:878105,
      author       = {Capo, Alessandro and Natalello, Antonino and Marienhagen,
                      Jan and Pennacchio, Angela and Camarca, Alessandra and Di
                      Giovanni, Stefano and Staiano, Maria and D'Auria, Sabato and
                      Varriale, Antonio},
      title        = {{S}tructural features of the glutamate-binding protein from
                      {C}orynebacterium glutamicum},
      journal      = {International journal of biological macromolecules},
      volume       = {162},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2020-02636},
      pages        = {903 - 912},
      year         = {2020},
      note         = {Biotechnologie 1},
      abstract     = {L-glutamate (Glu) is the major excitatory transmitter in
                      mammalian brain. Inadequate concentration of Glu in the
                      brain correlates to mood disorder. In industry, Glu is used
                      as a flavour enhancer in food and in foodstuff processing. A
                      high concentration of Glu has several effects on human
                      health such as hypersensitive effects, headache and stomach
                      pain. The presence of Glu in food can be detected by
                      different analytical methods based on chromatography, or
                      capillary electrophoresis or amperometric techniques. We
                      have isolated and characterized a glutamate-binding protein
                      (GluB) from the Gram-positive bacteria Corynebacterium
                      glutamicum. Together with GluC protein, GluD protein and the
                      cytoplasmic protein GluA, GluB permits the transport of Glu
                      in/out of cell.In this study, we have investigated the
                      binding features of GluB as well as the effect of
                      temperature on its structure both in the absence and in the
                      presence of Glu. The results have showed that GluB has a
                      high affinity and selectivity versus Glu (nanomolar range)
                      and the presence of the ligand induces a higher thermal
                      stability of the protein structure.},
      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:32593757},
      UT           = {WOS:000577953700004},
      doi          = {10.1016/j.ijbiomac.2020.06.197},
      url          = {https://juser.fz-juelich.de/record/878105},
}