Abstract
This study investigated relationship between secondary structure and surface hydrophobicity of soy protein isolate (SPI) subjected to a thermal treatment at 70~90°C. Heat denaturation increased the surface hydrophobicity and surface hydrophobicity decreased as aggregate formed. Heat caused an increase in the relative amount ofα-helix structures and an overall decrease in the amount ofβ-sheet structures when compared with nontreated SPI. The relative amounts of secondary structures varied with time, temperature, and intensity of heat treatment applied. Theβ-sheet structure was most important for its significant role in denaturation of 7S globulin and following formed aggregates and even in denaturation of 11S globulin. The amount ofβ-sheet structure in SPI had an inverse correlation with the surface hydrophobicity when the temperature was kept below 90°C. Besides,β-turn structure increased asβ-7S/B-11S aggregate formated.
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