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The effects of heat treatment on protein structure and in vitro digestibility in whole soybeans with different moisture content (10.68%, 29.70%, 46.29%, and 62.05% wet basis) were investigated. Scanning electronic microscopy presented that thermal treatment destroyed the subcellular structure of soybean seeds and resulted in formation of protein aggregates. When β-conglycinin (7S) was heat-denatured, the protein aggregates were maintained mainly by hydrogen bonds and hydrophobic interactions (non-covalent) for each moisture content. Also, the decrease of the protein solubility and increase of in vitro digestibility were observed. However, when glycinin (11S) was denatured in soybeans with 10.68% and 29.70% moisture content, the insoluble and indigestible protein aggregates with protein oxidation-induced crosslinking and high content of β-sheet were presented; in contrast, for 46.29% and 62.05% moisture content, mild protein oxidation, low content of β-sheet, non-covalent interactions and increased protein digestibility were shown. Non-covalent interactions were shown a positive correlation with gastrointestinal digestibility (r = 0.59, p 0.05). Meanwhile, protein oxidation or β-sheet content was significantly negatively correlated with in vitro protein digestibility (r = -0.69 and -0.61, respectively, p 0.05). Protein structure rather than solubility contributed to difference of in vitro digestibility. The optimum thermal conditions to obtain high-quality digestible protein in whole soybeans are 160 °C for 10.68%, 145 °C for 29.70%, 160 °C for 46.29% and 115 °C/140 °C for 62.05% moisture content. |
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