Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model
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 va...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/6/1136 |
| _version_ | 1797611771489419264 |
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| author | Yu Shen Mengling Lv Zhenyue Tang Wei Liu Yusong Zhang Fei Teng Xu Wang Meili Shao Yujun Jiang |
| author_facet | Yu Shen Mengling Lv Zhenyue Tang Wei Liu Yusong Zhang Fei Teng Xu Wang Meili Shao Yujun Jiang |
| author_sort | Yu Shen |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T06:33:28Z |
| format | Article |
| id | doaj.art-eedf2987876044c385e9221e927b6c3b |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T06:33:28Z |
| publishDate | 2023-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-eedf2987876044c385e9221e927b6c3b2023-11-17T11:05:15ZengMDPI AGFoods2304-81582023-03-01126113610.3390/foods12061136Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion ModelYu Shen0Mengling Lv1Zhenyue Tang2Wei Liu3Yusong Zhang4Fei Teng5Xu Wang6Meili Shao7Yujun Jiang8Department of Food Science, Northeast Agricultural University, Harbin 150038, ChinaDepartment of Food Science, Northeast Agricultural University, Harbin 150038, ChinaDepartment of Food Science, Northeast Agricultural University, Harbin 150038, ChinaHarbin Customs Technology Center, Harbin 150030, ChinaDepartment of Food Science, Northeast Agricultural University, Harbin 150038, ChinaDepartment of Food Science, Northeast Agricultural University, Harbin 150038, ChinaDepartment of Food Science, Northeast Agricultural University, Harbin 150038, ChinaDepartment of Food Science, Northeast Agricultural University, Harbin 150038, ChinaKey Laboratory of Dairy Science, Ministry of Education, Harbin 150030, ChinaAcrylamide (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.https://www.mdpi.com/2304-8158/12/6/1136soy protein isolateacrylamideinteraction mechanismgastrointestinal digestion simulation |
| spellingShingle | Yu Shen Mengling Lv Zhenyue Tang Wei Liu Yusong Zhang Fei Teng Xu Wang Meili Shao Yujun Jiang Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model Foods soy protein isolate acrylamide interaction mechanism gastrointestinal digestion simulation |
| title | Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model |
| title_full | Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model |
| title_fullStr | Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model |
| title_full_unstemmed | Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model |
| title_short | Soy Protein Isolate Interacted with Acrylamide to Reduce the Release of Acrylamide in the In Vitro Digestion Model |
| title_sort | soy protein isolate interacted with acrylamide to reduce the release of acrylamide in the in vitro digestion model |
| topic | soy protein isolate acrylamide interaction mechanism gastrointestinal digestion simulation |
| url | https://www.mdpi.com/2304-8158/12/6/1136 |
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