Acrylamide (AA), which is a carcinogen in humans, has been a research focus in terms of food risk assessment. However, few published studies have explored protein strategies to reduce the health risks of AA. The objective of this study was to investigate the binding of AA with soy protein isolate (SPI) and elucidate the binding mechanism. The results showed that AA could bind with nontreated, heat-treated, high-pressure homogenization-treated, and ultrasound-treated SPI in vitro. Fourier-transform infrared spectroscopy suggested that secondary structure of SPI changed significantly after binding with AA in the nontreated and different treated groups. Moreover, fluorescence quenching experiments suggested that the quenching of SPI by AA was static quenching and hydrogen bonds, hydrophobic interactions, and van der Waals forces were involved in this process. PRACTICAL APPLICATION: The study of SPI and AA binding could provide a new perspective for reducing the bioaccessibility of AA in human body by using protein. The results showed that SPI could potentially be used as a novel health strategy to reduce the harm of AA in the human body.
Keywords: acrylamide; fluorescence quenching; soy protein isolate; vitro binding mechanism.
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