Abstract
The effects of heat treatment on soymilk protein denaturation were studied by differential scanning calorimetry (DSC) and electrophoresis. Transition behavior of soymilk was studied by DSC. Three endotherms were found in DSC heating curves; the transition observed at around 70°C is attributed to the denaturation of 7S (b-conglycinin) and the transition at around 90°C is to 11S (glycinin). The denaturation temperature increased with the increasing soymilk protein content. The change of electrophoretic patterns after heat treatments indicated that soy proteins were dissociated into subunits, some of which coalesced. When the heating temperature is below their denaturation temperature, the protein fractions cannot completely be denatured even after heat exposure for extended periods of time.
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Zhang, H., Takenaka, M. & Isobe, S. DSC and electrophoretic studies on soymilk protein denaturation. Journal of Thermal Analysis and Calorimetry 75, 719–726 (2004). https://doi.org/10.1023/B:JTAN.0000027168.18317.78
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DOI: https://doi.org/10.1023/B:JTAN.0000027168.18317.78