Abstract
Acrylamide (AA), a common carcinogen, has been found in many dietary products.. This study aimed to explore the interaction of soybean protein isolate (SPI) with AA and further research the different effects of SPI on the AA release due to interactions in the in vitro digestion model. Analysis of variance was used to analyze the data. The results suggested that AA could bind with SPI in vitro, leading to the variation in SPI structure. The intrinsic fluorescence of SPI was quenched by AA via static quenching. The non-covalent (van der Waals forces and hydrogen bonding) and covalent bonds were the main interaction forces between SPI and AA. Furthermore, the release of AA significantly decreased due to its interaction with SPI under simulated gastrointestinal conditions. SPI had different effects on the AA release rate after different treatments. The thermal (80, 85, 90, and 95 °C for either 10 or 20 min) and ultrasound (200, 300, and 400 W for either 15, 30, or 60 min) treatments of SPI were useful in reducing the release of AA. However, the high pressure-homogenized (30, 60, 90, and 120 MPa once, twice, or thrice) treatments of SPI were unfavorable for reducing the release of AA.