Investigation on the interaction of acrylamide with soy protein isolate: Exploring the binding mechanism in vitro

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 (S...

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Bibliographic Details
Published inJournal of food science Vol. 86; no. 6; pp. 2766 - 2777
Main Authors Shen, Yu, Zhao, Sijia, Liu, Qingbo, Jiang, Yujun, Dong, Heliang, Feng, Wenxiao, Liu, Tianxu, Xu, Honghua, Shao, Meili
Format Journal Article
LanguageEnglish
Published United States Wiley Subscription Services, Inc 01.06.2021
Subjects
Acrylamide
Binding
Bioavailability
Carcinogens
Fluorescence
fluorescence quenching
Health risks
Human body
Hydrogen bonding
Hydrogen bonds
Hydrophobicity
Infrared spectroscopy
Protein structure
Proteins
Quenching
Risk assessment
Secondary structure
soy protein isolate
Van der Waals forces
vitro binding mechanism
soy protein isolate
acrylamide
fluorescence quenching
vitro binding mechanism
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Summary: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.
Bibliography:Funding information
National Natural Science Foundation of China, Grant Numbers: 31471682 and 31801518.
ISSN:0022-1147
1750-3841
DOI:10.1111/1750-3841.15733