Soy protein gels based on ultrasonic treatment: Effects of Ca2+ and 11S/7S ratio on gel structures and digestive properties

This study aimed to explore the impact of varying Ca<sup>2+</sup> concentrations and 11S/7S ratios on the gel performance of soybean protein gels (SPGs) under ultrasonication (400 W, 15 min) and to clarify the mechanisms involved. Results showed Ca<sup>2+</sup> addition altered the structure of soybean 11S/7S protein gels. Low Ca<sup>2+</sup> levels increased the turbidity, hardness, and water retention of the gels, whereas high levels disrupted the orderly aggregation of 11S/7S proteins, creating a rough, porous network. The effect of Ca<sup>2+</sup> was more pronounced with a higher 11S ratio, significantly influencing turbidity, disulfide bonding, and gel hardness. Conversely, 7S-rich gels showed reduced sensitivity to Ca<sup>2+</sup>. In vitro digestion and SDS-PAGE results indicated that 7S globulin's α, α', and β subunits were more digestible than the A and B subunits of 11S globulin. In conclusion, ultrasound combined with Ca<sup>2+</sup> can enhance the cross-linking degree between 11S and 7S globulin, forming a dense network structure.

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Publication Details

Journal
Ultrasonics Sonochemistry
Published
2024-11-06
DOI
https://doi.org/10.1016/j.ultsonch.2024.107143
Citations
13
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
4.53
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article

Soy protein gels based on ultrasonic treatment: Effects of Ca2+ and 11S/7S ratio on gel structures and digestive properties

Ying Zhu, Xiaoqi Deng, Ruqi Guo, Qinlin Hu et al.
13 citations
Ultrasonics Sonochemistry
Proteins in Food Systems
4.53
article

Soy protein gels based on ultrasonic treatment: Effects of Ca2+ and 11S/7S ratio on gel structures and digestive properties

Ying Zhu, Xiaoqi Deng, Ruqi Guo, Qinlin Hu, Xiuqing Zhu
article en
13 citations

Abstract

This study aimed to explore the impact of varying Ca<sup>2+</sup> concentrations and 11S/7S ratios on the gel performance of soybean protein gels (SPGs) under ultrasonication (400 W, 15 min) and to clarify the mechanisms involved. Results showed Ca<sup>2+</sup> addition altered the structure of soybean 11S/7S protein gels. Low Ca<sup>2+</sup> levels increased the turbidity, hardness, and water retention of the gels, whereas high levels disrupted the orderly aggregation of 11S/7S proteins, creating a rough, porous network. The effect of Ca<sup>2+</sup> was more pronounced with a higher 11S ratio, significantly influencing turbidity, disulfide bonding, and gel hardness. Conversely, 7S-rich gels showed reduced sensitivity to Ca<sup>2+</sup>. In vitro digestion and SDS-PAGE results indicated that 7S globulin's α, α', and β subunits were more digestible than the A and B subunits of 11S globulin. In conclusion, ultrasound combined with Ca<sup>2+</sup> can enhance the cross-linking degree between 11S and 7S globulin, forming a dense network structure.

Ultrasonics SonochemistryVol. 111
Heilongjiang University (CN)
Zero hunger
Openalex Percentile: Top 6%
Proteins in Food Systems
4.53
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