Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms
Herein, cationic soy protein (NSPI) was synthesized by grafting Ethylenediamine (EDA) onto soy protein isolate (SPI), and protein–gallic acid (GA) complexes were formed by mixing NSPI with GA in various ratios. We assessed the structure, particle size, thermal stability, emulsifying ability, and ant...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-10-01
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| Series: | Food Chemistry: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157523003097 |
| _version_ | 1827808635280949248 |
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| author | Shizhang Yan Qi Wang Jiaye Yu Yang Li Baokun Qi |
| author_facet | Shizhang Yan Qi Wang Jiaye Yu Yang Li Baokun Qi |
| author_sort | Shizhang Yan |
| collection | DOAJ |
| description | Herein, cationic soy protein (NSPI) was synthesized by grafting Ethylenediamine (EDA) onto soy protein isolate (SPI), and protein–gallic acid (GA) complexes were formed by mixing NSPI with GA in various ratios. We assessed the structure, particle size, thermal stability, emulsifying ability, and antioxidant capacity of NSPI and complexes. Results show that grafting with EDA introduced a positive charge to SPI and resulted in a uniform particle size, and enhanced thermal stability, emulsifying ability, and antioxidant capacity. In addition, NSPI presented more amino groups and stronger interactions with GA compared to SPI. EDA and GA synergistically increased the flexibility of SPI, reducing the α-helix content and increasing the random coil content. Moreover, the interactions between SPI, NSPI, and GA were static, and hydrophobic and electrostatic between GA and SPI and NSPI, respectively. Grafting SPI with EDA improved functionality and interactions with GA, implying that NSPI-GA complexes may function as emulsifiers and antioxidants. |
| first_indexed | 2024-03-11T22:31:03Z |
| format | Article |
| id | doaj.art-90d365b80967497ab4fa6f134be324a0 |
| institution | Directory Open Access Journal |
| issn | 2590-1575 |
| language | English |
| last_indexed | 2024-03-11T22:31:03Z |
| publishDate | 2023-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj.art-90d365b80967497ab4fa6f134be324a02023-09-23T05:12:35ZengElsevierFood Chemistry: X2590-15752023-10-0119100866Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized formsShizhang Yan0Qi Wang1Jiaye Yu2Yang Li3Baokun Qi4College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCorresponding author.; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaHerein, cationic soy protein (NSPI) was synthesized by grafting Ethylenediamine (EDA) onto soy protein isolate (SPI), and protein–gallic acid (GA) complexes were formed by mixing NSPI with GA in various ratios. We assessed the structure, particle size, thermal stability, emulsifying ability, and antioxidant capacity of NSPI and complexes. Results show that grafting with EDA introduced a positive charge to SPI and resulted in a uniform particle size, and enhanced thermal stability, emulsifying ability, and antioxidant capacity. In addition, NSPI presented more amino groups and stronger interactions with GA compared to SPI. EDA and GA synergistically increased the flexibility of SPI, reducing the α-helix content and increasing the random coil content. Moreover, the interactions between SPI, NSPI, and GA were static, and hydrophobic and electrostatic between GA and SPI and NSPI, respectively. Grafting SPI with EDA improved functionality and interactions with GA, implying that NSPI-GA complexes may function as emulsifiers and antioxidants.http://www.sciencedirect.com/science/article/pii/S2590157523003097Soy protein isolateGallic acidCationic soybean protein isolatePhenolic bindingFunctional property |
| spellingShingle | Shizhang Yan Qi Wang Jiaye Yu Yang Li Baokun Qi Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms Food Chemistry: X Soy protein isolate Gallic acid Cationic soybean protein isolate Phenolic binding Functional property |
| title | Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms |
| title_full | Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms |
| title_fullStr | Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms |
| title_full_unstemmed | Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms |
| title_short | Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms |
| title_sort | soy protein interactions with polyphenols structural and functional changes in natural and cationized forms |
| topic | Soy protein isolate Gallic acid Cationic soybean protein isolate Phenolic binding Functional property |
| url | http://www.sciencedirect.com/science/article/pii/S2590157523003097 |
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