Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition

The interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3-<i>O</i>-glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs...

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Main Authors: Yaru Wu, Zhucheng Yin, Xuejiao Qie, Yao Chen, Maomao Zeng, Zhaojun Wang, Fang Qin, Jie Chen, Zhiyong He
Format: Article
Language:English
Published: MDPI AG 2021-03-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/26/6/1721
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author Yaru Wu
Zhucheng Yin
Xuejiao Qie
Yao Chen
Maomao Zeng
Zhaojun Wang
Fang Qin
Jie Chen
Zhiyong He
author_facet Yaru Wu
Zhucheng Yin
Xuejiao Qie
Yao Chen
Maomao Zeng
Zhaojun Wang
Fang Qin
Jie Chen
Zhiyong He
author_sort Yaru Wu
collection DOAJ
description The interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3-<i>O</i>-glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs mainly through hydrophobic interaction, and the binding affinity of SPI was stronger than that of SPIHs. Circular dichroism and Fourier-transform infrared spectroscopy analyses revealed that the interaction with C3G did not significantly change the secondary structures of SPI/SPIHs, while the surface hydrophobicity and average particle size of proteins decreased. Furthermore, the SPI/SPIHs-C3G interaction induced an antagonistic effect on the antioxidant capacity (ABTS and DPPH) of the complex system, with the masking effect on the ABTS scavenging capacity of the SPIHs-C3G complexes being lower than that of the SPI-C3G complexes. This study contributes to the design and development of functional beverages that are rich in hydrolysates and anthocyanins.
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spelling doaj.art-b06449bf347c4608981cfbef29636e052023-11-21T11:12:38ZengMDPI AGMolecules1420-30492021-03-01266172110.3390/molecules26061721Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral ConditionYaru Wu0Zhucheng Yin1Xuejiao Qie2Yao Chen3Maomao Zeng4Zhaojun Wang5Fang Qin6Jie Chen7Zhiyong He8State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, ChinaThe interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3-<i>O</i>-glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs mainly through hydrophobic interaction, and the binding affinity of SPI was stronger than that of SPIHs. Circular dichroism and Fourier-transform infrared spectroscopy analyses revealed that the interaction with C3G did not significantly change the secondary structures of SPI/SPIHs, while the surface hydrophobicity and average particle size of proteins decreased. Furthermore, the SPI/SPIHs-C3G interaction induced an antagonistic effect on the antioxidant capacity (ABTS and DPPH) of the complex system, with the masking effect on the ABTS scavenging capacity of the SPIHs-C3G complexes being lower than that of the SPI-C3G complexes. This study contributes to the design and development of functional beverages that are rich in hydrolysates and anthocyanins.https://www.mdpi.com/1420-3049/26/6/1721soy protein isolatehydrolysatecyanidin-3-<i>O</i>-glucosidenoncovalent interactionantioxidant capacity
spellingShingle Yaru Wu
Zhucheng Yin
Xuejiao Qie
Yao Chen
Maomao Zeng
Zhaojun Wang
Fang Qin
Jie Chen
Zhiyong He
Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition
Molecules
soy protein isolate
hydrolysate
cyanidin-3-<i>O</i>-glucoside
noncovalent interaction
antioxidant capacity
title Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition
title_full Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition
title_fullStr Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition
title_full_unstemmed Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition
title_short Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-<i>O</i>-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition
title_sort interaction of soy protein isolate hydrolysates with cyanidin 3 i o i glucoside and its effect on the in vitro antioxidant capacity of the complexes under neutral condition
topic soy protein isolate
hydrolysate
cyanidin-3-<i>O</i>-glucoside
noncovalent interaction
antioxidant capacity
url https://www.mdpi.com/1420-3049/26/6/1721
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