Influence of pH and Ionic Strength on Heat-Induced Formation and Rheological Properties of Soy Protein Gels in Relation to Denaturation and Their Protein Compositions

J.M.S. Renkema, H. Gruppen, T. van Vliet

Research output: Contribution to journalArticleAcademicpeer-review

165 Citations (Scopus)

Abstract

The influence of pH and ionic strength on gel formation and gel properties of soy protein isolate (SPI) in relation to denaturation and protein aggregation/precipitation was studied. Denaturation proved to be a prerequisite for gel formation under all conditions of pH and ionic strength studied. Gels exhibited a low stiffness at pH >6 and a high stiffness at pH 5 less protein and especially fewer acidic polypeptides take part in the network, coinciding with less stiff gels. At pH 7.6, extensive rearrangements in the network structure took place during prolonged heating, whereas at pH 3.8 rearrangements did not occur.
Original languageEnglish
Pages (from-to)6064-6071
JournalJournal of Agricultural and Food Chemistry
Volume50
Issue number21
DOIs
Publication statusPublished - 2002

Keywords

  • soybean beta-conglycinin
  • molecular-structure
  • gelation
  • glycinin
  • subunits
  • solubility
  • isolate
  • 7s
  • association
  • behavior

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