Involvement of protein dynamics in enzyme stability
- 23 September 2001
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 506 (3) , 216-220
- https://doi.org/10.1016/s0014-5793(01)02917-9
Abstract
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.Keywords
This publication has 20 references indexed in Scilit:
- Förster energy transfer from tryptophan to flavin in glucose oxidase enzymeChemical Physics Letters, 1998
- Developments and applications of biosensors in food analysisTrends in Biotechnology, 1997
- Assay of dehydrogenases with an O2-consuming biosensorEnzyme and Microbial Technology, 1994
- Mechanism-based strategies for protein thermostabilizationTrends in Biotechnology, 1993
- Crystal Structure of Glucose Oxidase from Aspergillus niger Refined at 2·3 Å ReslutionJournal of Molecular Biology, 1993
- Effects of carbohydrate depletion on the structure, stability and activity of glucose oxidase from Aspergillus nigerBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Analysis of diffusion effects on immobilized enzymes on porous supports with reversible Michaelis-Menten kineticsEnzyme and Microbial Technology, 1986
- FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULESPhotochemistry and Photobiology, 1973
- Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scaleBiochemistry, 1973