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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MDPI AG
2022-11-01
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Series: | Molecules |
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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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issn | 1420-3049 |
language | English |
last_indexed | 2024-03-09T17:39:25Z |
publishDate | 2022-11-01 |
publisher | MDPI AG |
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series | Molecules |
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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