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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...

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Detalles Bibliográficos
Autores principales: Yan, Shizhang, Wang, Qi, Yu, Jiaye, Li, Yang, Qi, Baokun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10534206/
https://www.ncbi.nlm.nih.gov/pubmed/37780344
http://dx.doi.org/10.1016/j.fochx.2023.100866
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author Yan, Shizhang
Wang, Qi
Yu, Jiaye
Li, Yang
Qi, Baokun
author_facet Yan, Shizhang
Wang, Qi
Yu, Jiaye
Li, Yang
Qi, Baokun
author_sort Yan, Shizhang
collection PubMed
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.
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spelling pubmed-105342062023-09-29 Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms Yan, Shizhang Wang, Qi Yu, Jiaye Li, Yang Qi, Baokun Food Chem X Research Article 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. Elsevier 2023-09-06 /pmc/articles/PMC10534206/ /pubmed/37780344 http://dx.doi.org/10.1016/j.fochx.2023.100866 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Yan, Shizhang
Wang, Qi
Yu, Jiaye
Li, Yang
Qi, Baokun
Soy protein interactions with polyphenols: Structural and functional changes in natural and cationized forms
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 Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10534206/
https://www.ncbi.nlm.nih.gov/pubmed/37780344
http://dx.doi.org/10.1016/j.fochx.2023.100866
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