ABSTRACTISOLATED soy proteins (ISP) from broken (mechanical action) or damaged (fungi) seeds had denaturation enthalpies (AH) and temperatures at peak maximum (T max) similar to those of ISP from normal seeds by DSC. They had different composition and/or conformation as measured by surface hydrophobic@ (So and Se) and SH and SS content. Also, damaged seeds produced ISP with less 7S fractions (due to fewer α and β subunits) and 11S fractions, suggesting proteo‐lysis. 7S and 11S fractions had different Tmax and ΔH, SH and SS contents and surface hydrophobicity. Also 7S proteins from damaged seeds showed less a and β‐subunits. The 11S proteins from broken and damaged seeds maintained gel forming properties in spite of structural differences. Isolation and characterization of 7S and 11S fractions partially accounted for changes in physicochemical properties of
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