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Interaction of soy protein isolate with hydroxytyrosol based on an alkaline method: Implications for structural and
Meiyu Gu1, Jiahui Shi1, Boya Zhang1
1Food College, Northeast Agricultural University, Harbin 150030, Heilongjiang, China.
Food Chemistry
|February 25, 2024
Summary
Hydroxytyrosol (HT) covalently bound to soy protein isolate (SPI) enhances its functional properties. This modification improved solubility, emulsifying, and antioxidant activities, making it a promising ingredient.
Area of Science:
- Food Science and Technology
- Biochemistry
- Materials Science
Background:
- Soy protein isolate (SPI) is a widely used protein source with functional properties that can be modified.
- Hydroxytyrosol (HT), a potent antioxidant polyphenol, has potential health benefits but limited bioavailability.
- Covalent modification offers a method to improve the stability and functionality of bioactive compounds like HT.
Purpose of the Study:
- To investigate the covalent binding of hydroxytyrosol (HT) to soy protein isolate (SPI) using an alkaline method.
- To evaluate the impact of varying HT concentrations on the structural and functional characteristics of SPI-HT adducts.
- To assess the changes in solubility, digestibility, emulsifying, foaming, and antioxidant properties of modified SPI.
Main Methods:
- Covalent binding of hydroxytyrosol (HT) to soy protein isolate (SPI) via an alkaline-assisted method.
- Characterization of SPI-HT adducts, including polyphenol binding efficiency, turbidity, solubility, and water holding capacity.
- Assessment of in vitro protein digestibility, emulsifying properties, foaming capacity, and antioxidant activity (DPPH and ABTS assays).
Main Results:
- Optimal HT binding to SPI was achieved, with adducts exhibiting altered structures.
- Modified SPI showed increased solubility and water holding capacity, alongside decreased turbidity and improved in vitro digestibility.
- Significant enhancements in emulsifying and foaming properties were observed, with antioxidant activity increasing substantially (DPPH: 296.89%, ABTS: 33.80%) at 70 μmol/g HT.
Conclusions:
- Covalent modification of SPI with HT significantly improves its functional attributes, including emulsification, foaming, and antioxidant capacity.
- The resulting SPI-HT adducts demonstrate potential as functional ingredients in food applications.
- This approach offers a strategy for enhancing the value and application scope of both SPI and HT.
Keywords:
Alkali methodCovalent modificationFunctionalityHydroxytyrosolMolecular structureSoy protein isolateMore Related Videos
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