TY  - JOUR
AU  - Capo, Alessandro
AU  - Natalello, Antonino
AU  - Marienhagen, Jan
AU  - Pennacchio, Angela
AU  - Camarca, Alessandra
AU  - Di Giovanni, Stefano
AU  - Staiano, Maria
AU  - D'Auria, Sabato
AU  - Varriale, Antonio
TI  - Structural features of the glutamate-binding protein from Corynebacterium glutamicum
JO  - International journal of biological macromolecules
VL  - 162
SN  - 0141-8130
CY  - New York, NY [u.a.]
PB  - Elsevier
M1  - FZJ-2020-02636
SP  - 903 - 912
PY  - 2020
N1  - Biotechnologie 1
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:32593757
UR  - <Go to ISI:>//WOS:000577953700004
DO  - DOI:10.1016/j.ijbiomac.2020.06.197
UR  - https://juser.fz-juelich.de/record/878105
ER  -