Study of thermal and chemical effects on cellulase enzymes: Viscosity measurements

N. Ghaouar*, A. Aschi, L. Belbahri, S. Trabelsi, A. Gharbi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

The behaviour of cellulase enzymes in phosphate saline buffer has been studied over a wide range of temperatures and enzyme concentrations by using viscosity measurements. To characterize the conformation change of cellulase versus temperature and chemical denaturants, such as guanidinium chloride (GdmCl) and urea, the information about the intrinsic viscosity and the hydrodynamic radius are necessary. The dependence of the intrinsic viscosity and the hydrodynamic radius in its random coil conformation on temperature and denaturant concentration were studied. Our results and discussions are limited to the dilute regime of concentration because of abnormalities in conformation observed in the very dilute regime due to the presence of capillary absorption effects.

Original languageEnglish
Pages (from-to)4246-4252
Number of pages7
JournalPhysica B: Condensed Matter
Volume404
Issue number21
DOIs
Publication statusPublished - 2009
Externally publishedYes

Keywords

  • Cellulases
  • Critical concentration
  • Denaturation
  • Fluidity
  • Hydrodynamic radius
  • Viscosity

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