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Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates

Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean prote...

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Autores principales: Wang, Yichang, Li, Bailiang, Guo, Yanan, Liu, Caihua, Liu, Jun, Tan, Bin, Guo, Zengwang, Wang, Zhongjiang, Jiang, Lianzhou
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9149199/
https://www.ncbi.nlm.nih.gov/pubmed/35636156
http://dx.doi.org/10.1016/j.ultsonch.2022.106046
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author Wang, Yichang
Li, Bailiang
Guo, Yanan
Liu, Caihua
Liu, Jun
Tan, Bin
Guo, Zengwang
Wang, Zhongjiang
Jiang, Lianzhou
author_facet Wang, Yichang
Li, Bailiang
Guo, Yanan
Liu, Caihua
Liu, Jun
Tan, Bin
Guo, Zengwang
Wang, Zhongjiang
Jiang, Lianzhou
author_sort Wang, Yichang
collection PubMed
description Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean protein aggregates (OSPI). The results showed that oxidative treatment could disrupt the native soy protein (SPI) structure by promoting the formation of oxidized aggregates with β1-sheet structures through hydrophobic interactions. These changes led to a decrease in the solubility, emulsification ability and interfacial activity of soybean protein. After low-power ultrasound (100 W, 200 W) treatment, the relative contents of β1-sheets, β2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute ζ-potential value and free sulfhydryl content decreased. Moreover, protein aggregates with larger particle sizes and poor solubility were formed. The emulsions prepared using the OSPI showed bridging flocculation and decreased protein adsorption and interfacial tension. After applying medium-power ultrasound (300 W, 400 W, and 500 W) treatments, the OSPI solubility increased and particle size decreased. The α-helix and β-turn contents, surface hydrophobicity and absolute ζ-potential value increased, the structure unfolded, and the disulfide bond content decreased. These changes improved the emulsification activity and emulsion state of the OSPI and increased the protein adsorption capacity and interfacial tension of the emulsion. However, after a high-power ultrasound (600 W) treatment, the OSPI showed a tendency to reaggregate, which had a certain negative effect on the emulsification activity and interfacial activity. The results showed that UT at an appropriate power could depolymerize OSPI and improve the emulsification and interfacial activity of soybean protein.
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spelling pubmed-91491992022-05-31 Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates Wang, Yichang Li, Bailiang Guo, Yanan Liu, Caihua Liu, Jun Tan, Bin Guo, Zengwang Wang, Zhongjiang Jiang, Lianzhou Ultrason Sonochem Short Communication Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean protein aggregates (OSPI). The results showed that oxidative treatment could disrupt the native soy protein (SPI) structure by promoting the formation of oxidized aggregates with β1-sheet structures through hydrophobic interactions. These changes led to a decrease in the solubility, emulsification ability and interfacial activity of soybean protein. After low-power ultrasound (100 W, 200 W) treatment, the relative contents of β1-sheets, β2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute ζ-potential value and free sulfhydryl content decreased. Moreover, protein aggregates with larger particle sizes and poor solubility were formed. The emulsions prepared using the OSPI showed bridging flocculation and decreased protein adsorption and interfacial tension. After applying medium-power ultrasound (300 W, 400 W, and 500 W) treatments, the OSPI solubility increased and particle size decreased. The α-helix and β-turn contents, surface hydrophobicity and absolute ζ-potential value increased, the structure unfolded, and the disulfide bond content decreased. These changes improved the emulsification activity and emulsion state of the OSPI and increased the protein adsorption capacity and interfacial tension of the emulsion. However, after a high-power ultrasound (600 W) treatment, the OSPI showed a tendency to reaggregate, which had a certain negative effect on the emulsification activity and interfacial activity. The results showed that UT at an appropriate power could depolymerize OSPI and improve the emulsification and interfacial activity of soybean protein. Elsevier 2022-05-23 /pmc/articles/PMC9149199/ /pubmed/35636156 http://dx.doi.org/10.1016/j.ultsonch.2022.106046 Text en © 2022 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 Short Communication
Wang, Yichang
Li, Bailiang
Guo, Yanan
Liu, Caihua
Liu, Jun
Tan, Bin
Guo, Zengwang
Wang, Zhongjiang
Jiang, Lianzhou
Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
title Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
title_full Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
title_fullStr Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
title_full_unstemmed Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
title_short Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
title_sort effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9149199/
https://www.ncbi.nlm.nih.gov/pubmed/35636156
http://dx.doi.org/10.1016/j.ultsonch.2022.106046
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