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Relationship between flexibility and interfacial functional properties of soy protein isolate: succinylation
Ziteng Lian1, Sai Yang1, Shicheng Dai1
1College of Food Science, Northeast Agricultural University, Harbin, China.
Journal of the Science of Food and Agriculture
|May 13, 2022
Summary
Succinic anhydride (SA) modification enhances soy protein isolate (SPI) flexibility and interfacial properties. Optimal results were achieved at a 15% SA/SPI ratio, improving emulsification and foaming capabilities.
Area of Science:
- Food Science
- Protein Chemistry
- Materials Science
Background:
- Investigating the impact of succinic anhydride (SA) on soy protein isolate (SPI) flexibility.
- Measuring changes in protein conformation and interfacial functional properties.
- Establishing the structure-effect relationship between conformation, flexibility, and interfacial properties.
Purpose of the Study:
- To determine the effects of varying succinic anhydride (SA) concentrations on soy protein isolate (SPI) flexibility.
- To analyze the resulting changes in SPI conformation and interfacial functional properties.
- To establish a structure-property relationship for SA-modified SPI.
Main Methods:
- Soy protein isolate (SPI) was modified with different ratios of succinic anhydride (SA).
- Changes in protein conformation (e.g., β-sheet content, tertiary structure) were analyzed.
- Interfacial functional properties, including surface hydrophobicity, emulsification, and foaming, were measured.
Main Results:
- Succinic anhydride (SA) modification reduced SPI's β-sheet content and increased disordered structures, altering tertiary structure and microstructure.
- Optimal SPI flexibility (0.3977) and interfacial properties were achieved at a 15% SA/SPI mass ratio.
- Significant positive correlations were found between SPI flexibility and its emulsifying and foaming properties (correlation coefficients ranging from 0.929 to 0.972).
Conclusions:
- Succinylation-induced conformational changes in SPI enhance its flexibility, leading to improved interfacial functional properties.
- The study provides theoretical guidance for developing and applying highly emulsifiable and stable soy protein products through succinylation.
- Optimized SA modification offers a pathway to tailor SPI for enhanced food applications.
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