Abstract: In this work, the effects of high temperature and hydrothermal treatment on the structural and functional properties of soy protein isolate (SPI) were investigated. Under the neutral condition, 1% (mg:mL) soy protein isolate was treated at 70, 90, 120, 150, 170, 200 ℃ for 30 min, respectively, and the changes in protein structure, solubility, surface hydrophobicity, emulsification, and emulsification stability were measured before and after treatment. The fitting of the infrared spectrum showed that the α-helix content of SPI increased, meanwhile the β-sheet content decreased significantly. Moreover, with the treatment temperature increased, the maximum emission wavelength was redshifted and the maximum emission of the samples treated with high temperature and hydrothermal treatment at 200 ℃ occurred the maximum redshift. Especially, as the treatment temperature increased to 90 ℃, the solubility of SPI was increased gradually, which may due to the production of soluble aggregates. The solubility of SPI was the minimum when the treatment temperature was 120 ℃. Furthermore, with the temperature rose, the solubility was increased again until 200 ℃. On the other hand, the Zeta potential of SPI was decreased with the increase of treated temperature, which showed the system was unstable and easy to aggregate. Besides, the particle size and turbidity of SPI treated at 170 ℃ and 200 ℃ was increased obviously which indicating that SPI formed soluble aggregates. The surface hydrophobicity and emulsifying activity indexes of SPI were both increased first and then decreased, and both values reached the maximum when the treatment temperature was 90 ℃. While the emulsification stability increased with the increase of temperature. This research could provide a theoretical and direction for the thermal aggregation modification of plant protein, especially for soybean protein.
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