Immobilization–stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus

@article{Bolvar2008ImmobilizationstabilizationOA,
  title={Immobilization–stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus},
  author={Juan M. Bol{\'i}var and Felipe Cava and C. Gar{\'c}ia Mateo and Javier Rocha-Martin and Jos{\'e} M Guis{\'a}n and Jos{\'e} Berenguer and Roberto Fernandez-Lafuente},
  journal={Applied Microbiology and Biotechnology},
  year={2008},
  volume={80},
  pages={49-58}
}
The genome of Thermus thermophilus contains two genes encoding putative glutamate dehydrogenases. One of these genes (TTC1211) was cloned and overexpressed in Escherichia coli. The purified enzyme was a trimer that catalyzed the oxidation of glutamate to α-ketoglutarate and ammonia with either NAD+ or NADP+ as cofactors. The enzyme was also able to catalyze the inverse reductive reaction. The thermostability of the enzyme at neutral pH was very high even at 70°C, but at acidic pH values, the… CONTINUE READING
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