Literature DB >> 11602248

Involvement of protein dynamics in enzyme stability. The case of glucose oxidase.

A Haouz1, J M Glandières, B Alpert.   

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.

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Year:  2001        PMID: 11602248     DOI: 10.1016/s0014-5793(01)02917-9

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Modification of PEGylated enzyme with glutaraldehyde can enhance stability while avoiding intermolecular crosslinking.

Authors:  D W Ritter; J M Newton; M J McShane
Journal:  RSC Adv       Date:  2014-06-17       Impact factor: 3.361

Review 2.  From Protein Features to Sensing Surfaces.

Authors:  Greta Faccio
Journal:  Sensors (Basel)       Date:  2018-04-15       Impact factor: 3.576

3.  Glucose Determination by Means of Steady-state and Time-course UV Fluorescence in Free or Immobilized Glucose Oxidase.

Authors:  Paola De Luca; Maria Lepore; Marianna Portaccio; Rosario Esposito; Sergio Rossi; Umberto Bencivenga; Damiano Gustavo Mita
Journal:  Sensors (Basel)       Date:  2007-11-05       Impact factor: 3.576

  3 in total

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