Surface Properties and Emulsification Behavior of Denatured Soy Proteins

I. NIR*, Y. FELDMAN, A. ASERIN, N. GARTI

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

Abstract

Soy protein isolate was physically (heat pretreatment) and chemically (urea, guanidine·HCl, and cleavage of SS bonds) modified in order to dissociate subunits, unfold the protein and improve surface properties: hydrophobicity, emulsification capability, and stability. Heat pretreatment as well as chemical treatment with urea or guanidine·HCl or reduction of disulphide bonds, will improve emulsification performance in comparison to native soy protein isolate. Significant differences in reduction of surface tension of water in the presence of native and modified proteins were observed (45 and 35 dynes/cm respectively). Measurements of fluorescence indicated that the relative hydrophobicity of the soy protein was also improved (from 600 to 1360) after heat pretreatment or contacting the soy protein with 8M urea solution.

Original languageEnglish
Pages (from-to)606-610
Number of pages5
JournalJournal of Food Science
Volume59
Issue number3
DOIs
StatePublished - May 1994

Keywords

  • denaturation
  • emulsification
  • protein
  • rheology
  • soy

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