Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies

(1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2)...

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Autores principales:	Le Ao, Panhang Liu, Annan Wu, Jing Zhao, Xiaosong Hu
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	soybean protein isolate polyphenol molecular docking fluorescence Chemical technology TP1-1185
Acceso en línea:	https://doaj.org/article/89dde0a75e2c41a78e2c493beb09683a
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spelling	oai:doaj.org-article:89dde0a75e2c41a78e2c493beb09683a2021-11-25T17:35:56ZCharacterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies10.3390/foods101128132304-8158https://doaj.org/article/89dde0a75e2c41a78e2c493beb09683a2021-11-01T00:00:00Zhttps://www.mdpi.com/2304-8158/10/11/2813https://doaj.org/toc/2304-8158(1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI–polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein–polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI–polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI–polyphenol interaction.Le AoPanhang LiuAnnan WuJing ZhaoXiaosong HuMDPI AGarticlesoybean protein isolatepolyphenolmolecular dockingfluorescenceChemical technologyTP1-1185ENFoods, Vol 10, Iss 2813, p 2813 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	soybean protein isolate polyphenol molecular docking fluorescence Chemical technology TP1-1185
spellingShingle	soybean protein isolate polyphenol molecular docking fluorescence Chemical technology TP1-1185 Le Ao Panhang Liu Annan Wu Jing Zhao Xiaosong Hu Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
description	(1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI–polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein–polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI–polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI–polyphenol interaction.
format	article
author	Le Ao Panhang Liu Annan Wu Jing Zhao Xiaosong Hu
author_facet	Le Ao Panhang Liu Annan Wu Jing Zhao Xiaosong Hu
author_sort	Le Ao
title	Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_short	Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_full	Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_fullStr	Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_full_unstemmed	Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_sort	characterization of soybean protein isolate-food polyphenol interaction via virtual screening and experimental studies
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/89dde0a75e2c41a78e2c493beb09683a
work_keys_str_mv	AT leao characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies AT panhangliu characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies AT annanwu characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies AT jingzhao characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies AT xiaosonghu characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies
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Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies

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