Study on the binding behavior and functional properties of soybean protein isolate and β-carotene
This study focused on the non-covalent interaction between soybean protein isolate (SPI) and β-carotene (BC). The conformational changes of SPI with β-carotene in varying proportions (BC/SPI: 2%, 4%, 6%, 8%, and 10%) were investigated by multi-spectroscopy and molecular docking. Results showed that...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-09-01
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| Series: | Frontiers in Nutrition |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fnut.2022.984490/full |
| _version_ | 1811275200620134400 |
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| author | Yating Zhang Wenqi Zhao Zhuqing Xing Beibei Zhu Ruiyang Hou Junxi Zhang Taoran Li Zifan Zhang Hongwu Wang Zheng Li |
| author_facet | Yating Zhang Wenqi Zhao Zhuqing Xing Beibei Zhu Ruiyang Hou Junxi Zhang Taoran Li Zifan Zhang Hongwu Wang Zheng Li |
| author_sort | Yating Zhang |
| collection | DOAJ |
| description | This study focused on the non-covalent interaction between soybean protein isolate (SPI) and β-carotene (BC). The conformational changes of SPI with β-carotene in varying proportions (BC/SPI: 2%, 4%, 6%, 8%, and 10%) were investigated by multi-spectroscopy and molecular docking. Results showed that the quenching mode is static quenching and binding affinity increased with temperature. The stoichiometry was 1:1, indicating there was only one binding site in SPI. The binding was based on entropy and primarily driven by hydrophobic interactions and its binding constant was in the order of 104 L⋅mol–1. The addition of the β-carotene affected the secondary structure of SPI resulting in an increase in α-Helix and a decrease in random coil and β-turn content, indicating protein aggregated and hydrophobic interactions occurred. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) verified that no new larger molecular weight substance was formed and no covalent interaction existed. Molecular docking corroborated that electrostatic and hydrophobic interactions were both involved in the formation of complexes, where hydrophobic interaction was the dominant one. Moreover, β-carotene improved 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, foaming capacity, and emulsifying stability of SPI. These findings provide useful information about the interaction mechanism of SPI and β-carotene, which contributes to the further development and application of SPI products rich in β-carotene in the food industry. |
| first_indexed | 2024-04-12T23:33:48Z |
| format | Article |
| id | doaj.art-68c63e1b5a864a4cb15f7290fd810676 |
| institution | Directory Open Access Journal |
| issn | 2296-861X |
| language | English |
| last_indexed | 2024-04-12T23:33:48Z |
| publishDate | 2022-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Nutrition |
| spelling | doaj.art-68c63e1b5a864a4cb15f7290fd8106762022-12-22T03:12:12ZengFrontiers Media S.A.Frontiers in Nutrition2296-861X2022-09-01910.3389/fnut.2022.984490984490Study on the binding behavior and functional properties of soybean protein isolate and β-caroteneYating Zhang0Wenqi Zhao1Zhuqing Xing2Beibei Zhu3Ruiyang Hou4Junxi Zhang5Taoran Li6Zifan Zhang7Hongwu Wang8Zheng Li9College of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Chinese Medicine Pharmaceutical Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Healthy Science and Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCollege of Chinese Medicine Pharmaceutical Engineering, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaThis study focused on the non-covalent interaction between soybean protein isolate (SPI) and β-carotene (BC). The conformational changes of SPI with β-carotene in varying proportions (BC/SPI: 2%, 4%, 6%, 8%, and 10%) were investigated by multi-spectroscopy and molecular docking. Results showed that the quenching mode is static quenching and binding affinity increased with temperature. The stoichiometry was 1:1, indicating there was only one binding site in SPI. The binding was based on entropy and primarily driven by hydrophobic interactions and its binding constant was in the order of 104 L⋅mol–1. The addition of the β-carotene affected the secondary structure of SPI resulting in an increase in α-Helix and a decrease in random coil and β-turn content, indicating protein aggregated and hydrophobic interactions occurred. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) verified that no new larger molecular weight substance was formed and no covalent interaction existed. Molecular docking corroborated that electrostatic and hydrophobic interactions were both involved in the formation of complexes, where hydrophobic interaction was the dominant one. Moreover, β-carotene improved 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, foaming capacity, and emulsifying stability of SPI. These findings provide useful information about the interaction mechanism of SPI and β-carotene, which contributes to the further development and application of SPI products rich in β-carotene in the food industry.https://www.frontiersin.org/articles/10.3389/fnut.2022.984490/fullsoybean protein isolateβ-carotenemulti-spectroscopic techniquesmolecular dockingemulsifying properties |
| spellingShingle | Yating Zhang Wenqi Zhao Zhuqing Xing Beibei Zhu Ruiyang Hou Junxi Zhang Taoran Li Zifan Zhang Hongwu Wang Zheng Li Study on the binding behavior and functional properties of soybean protein isolate and β-carotene Frontiers in Nutrition soybean protein isolate β-carotene multi-spectroscopic techniques molecular docking emulsifying properties |
| title | Study on the binding behavior and functional properties of soybean protein isolate and β-carotene |
| title_full | Study on the binding behavior and functional properties of soybean protein isolate and β-carotene |
| title_fullStr | Study on the binding behavior and functional properties of soybean protein isolate and β-carotene |
| title_full_unstemmed | Study on the binding behavior and functional properties of soybean protein isolate and β-carotene |
| title_short | Study on the binding behavior and functional properties of soybean protein isolate and β-carotene |
| title_sort | study on the binding behavior and functional properties of soybean protein isolate and β carotene |
| topic | soybean protein isolate β-carotene multi-spectroscopic techniques molecular docking emulsifying properties |
| url | https://www.frontiersin.org/articles/10.3389/fnut.2022.984490/full |
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