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Literature summary for 3.2.1.21 extracted from

  • Bruins, M.E.; Meersman, F.; Janssen, A.E.; Heremans, K.; Boom, R.M.
    Increased susceptibility of beta-glucosidase from the hyperthermophile Pyrococcus furiosus to thermal inactivation at higher pressures (2009), FEBS J., 276, 109-117.
    View publication on PubMed

General Stability

General Stability Organism
enzyme is highly piezostable and thermostable, with increased enzyme inactivation at 25°C and pressures from 100 to 300 MPa. At a constant pressure of 400 MPa, no enzyme inactivation occurrs. Enzyme has an unfolding pressure of 800 MPa at 85°C. Two-step inactivation process due to pressure, which is most pronounced at low temperatures. An increase in pH from 5.5 to 6.5 has a stabilizing effect Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q51723
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
no thermal unfolding at 200 MPa and 400 MPa Pyrococcus furiosus
122
-
melting point at 50 MPa in Tris buffer, pH 7.5 Pyrococcus furiosus