Analysis of protein gels formed by interfacial partitioning

R. Borbás, S. Turza, J. Szamos, É Kiss

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13 Citations (Scopus)

Abstract

A special combination of alcoholic precipitation and salting out of proteins was described as three-phase partitioning (TPP). Proteins are accumulated in a coherent middle phase in the partitioning system composed of tert-butanol, ammonium sulphate and water. Partitioning systems with various ratios of components were investigated. The composition and the mechanical properties of the middle phase were determined in model systems using bovine serum albumin or ovalbumin. Quantitative analysis revealed that beside the protein content (2-10wt%) other components of the middle phase formed two immiscible liquid phases. The stress-deformation relationship obtained by uniaxial compression showed the elastic behaviour of the middle phase. The results suggested that the middle phase formed in TPP is an emulsion gel. A possible mechanism of the formation of an emulsion gel was outlined.

Original languageEnglish
Pages (from-to)705-713
Number of pages9
JournalColloid and Polymer Science
Volume279
Issue number7
DOIs
Publication statusPublished - Jul 24 2001

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Keywords

  • Emulsion gel
  • Protein separation
  • Stress-deformation behaviour of bovine serum albumin and ovalbumin gels
  • Three-phase partitioning

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Polymers and Plastics
  • Colloid and Surface Chemistry
  • Materials Chemistry

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