Solvent-induced lysozyme gels: Effects of system composition and temperature on structural and dynamic characteristics

Marcelo A. Da Silva, Imad A. Farhat, Elizabeth P G Arêas, John R. Mitchell

Research output: Contribution to journalArticlepeer-review

15 Citations (SciVal)

Abstract

The gelation process of lysozyme in water/tetramethylurea in the presence of salt was investigated as a function of temperature and system composition by rheology, infrared spectroscopy, and microcalorimetry. Times and temperatures of gelation were determined from the variation of the storage (G′) and loss (G″) moduli. It was found that gelation times follow exponential decays with both protein and tetramethylurea (TMU) concentrations and with temperature. The activation energy for the overall process shows a linear dependence on TMU mass fraction. A strongly increased β-sheet content and reduced α-helix occur with the increase of TMU concentration in the binary solvent. Also, a linear decrease of lysozyme denaturation temperature and enthalpy on TMU concentration is found for the TMU mass fraction up to 0.5, above which no denaturation signal can be detected.

Original languageEnglish
Pages (from-to)443-454
Number of pages12
JournalBiopolymers
Volume83
Issue number5
Early online date26 Jun 2006
DOIs
Publication statusPublished - 5 Dec 2006

Keywords

  • Differential scanning calorimetry
  • Globular protein
  • Infrared spectroscopy
  • Rheology
  • Sol-gel processes

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology
  • Biochemistry
  • Biophysics

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