Exploring the unfolding mechanism of γ-glutamyltranspeptidases: The case of the thermophilic enzyme from Geobacillus thermodenitrificans

► The thermal and chemical stability of GthGT and its T353A mutant has been reported. ► An intermediate has been detected during the thermal unfolding of GthGT and T353A. ► Mature GthGT is more susceptible at acidic pH to chemical denaturation than T353A. ► Electrostatics are important for the stability of GthGT.