Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment

This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i>p</i> &l...

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Main Authors: Zhaojun Wang, Lin Zeng, Liwei Fu, Qiuming Chen, Zhiyong He, Maomao Zeng, Fang Qin, Jie Chen
Format: Article
Language:English
Published: MDPI AG 2022-11-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/27/23/8221
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author Zhaojun Wang
Lin Zeng
Liwei Fu
Qiuming Chen
Zhiyong He
Maomao Zeng
Fang Qin
Jie Chen
author_facet Zhaojun Wang
Lin Zeng
Liwei Fu
Qiuming Chen
Zhiyong He
Maomao Zeng
Fang Qin
Jie Chen
author_sort Zhaojun Wang
collection DOAJ
description This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i>p</i> < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i>p</i> < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.
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spelling doaj.art-31fc2b2a77074d53ae1968ae462d332a2023-11-24T11:38:46ZengMDPI AGMolecules1420-30492022-11-012723822110.3390/molecules27238221Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound TreatmentZhaojun Wang0Lin Zeng1Liwei Fu2Qiuming Chen3Zhiyong He4Maomao Zeng5Fang Qin6Jie Chen7State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaAnalysis Centre, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaThis study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i>p</i> < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i>p</i> < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.https://www.mdpi.com/1420-3049/27/23/8221soy protein isolatesgel propertiesNaCl concentrationultrasoundrheological propertiesprotein interaction
spellingShingle Zhaojun Wang
Lin Zeng
Liwei Fu
Qiuming Chen
Zhiyong He
Maomao Zeng
Fang Qin
Jie Chen
Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
Molecules
soy protein isolates
gel properties
NaCl concentration
ultrasound
rheological properties
protein interaction
title Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
title_full Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
title_fullStr Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
title_full_unstemmed Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
title_short Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
title_sort effect of ionic strength on heat induced gelation behavior of soy protein isolates with ultrasound treatment
topic soy protein isolates
gel properties
NaCl concentration
ultrasound
rheological properties
protein interaction
url https://www.mdpi.com/1420-3049/27/23/8221
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