Thermal dissociation and association behavior of soy proteins

Bruce German, Srinivasan Damodaran, John E. Kinsella

Research output: Contribution to journalArticlepeer-review

162 Scopus citations


Solutions of soy proteins or glycinin (11 S) plus conglycinin (7 S) do not aggregate when heated at 100 °C at neutral pH for 30 min. Thermal studies of these proteins using differential scanning calorimetry showed thermal transitions occurring at 92 and 77 °C for 11 S and 7 S, respectively. At temperatures in excess of 90 °C, isolated glycinin (11 S) forms insoluble aggregates that consist exclusively of the basic subunits. Response surface analyses of the solubility of isolated basic subunits indicate that the basic subunit peptides spontaneously coagulate via hydrophobic interactions. The absence of aggregation in whole soy mixtures suggests an interaction between 11 S and 7 S following heating, resulting in either stabilization of the 11S structure or solubilization of the component basic subunits following dissociation. Reversible cross-linking experiments suggested that heating 11 S in the presence of 7 S results in complex formation between dissociated 7S subunits and 11S basic subunits.

Original languageEnglish (US)
Pages (from-to)807-811
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Issue number5
StatePublished - 1982
Externally publishedYes

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)


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