Involvement of protein dynamics in enzyme stability. The case of glucose oxidase.
Dynamics of glucose oxidase immobilized and in solution were compared through their tryptophan fluorescence spectra, decay times and quenching by acrylamide. Energy barrier for thermal inactivation and melting temperature of both soluble and immobilized enzyme were also measured. Data show that the fluctuation amplitude is at the origin of protein instability.
Haouz
A
A
Laboratoire de Biologie Physico-Chimique, Université Denis Diderot, 2 place Jussieu, 75251 Cedex 05, Paris, France.
Glandières
J M
JM
Alpert
B
B
D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D005949:Glucose Oxidase / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry
D004800:Enzymes, Immobilized; D011506:Proteins; D014364:Tryptophan; D005949:Glucose Oxidase