Changes in solubility and molecular weight distribution of protein in heat-cured soy protein film were investigated to understand the mechanism of protein−protein interactions that occur during heat treatment. Soy protein films were heated at 65, 80, or 95 °C for 6, 18, or 24 h. The solubility of the proteins decreased with increasing temperature of heat treatment in various buffers. Buffers containing urea, a hydrogen bond-disrupting agent, and 2-mercaptoethanol, a disulfide bond-disrupting agent, dissolved more than 95% of protein in all the heat-treated samples. SDS−PAGE patterns indicated aggregation of proteins during film formation and in heat-treated films. The combined effects of urea and 2-mercaptoethanol suggested that proteins were aggregated primarily through hydrogen bonds and intermolecular disulfide bonds. This aggregation increased molecular weight and decreased film solubility.
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Rangavajhyala et al. (1997) studied this question.
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