Characterization of Okra Seed Protein/Rutin Covalent Complex and Its Application in Nanoemulsions

A covalent complex of okra seed protein (OSP) and rutin was prepared using the alkali-induced method and characterized. Its application in nanoemulsions was also evaluated. Multi-spectral analysis confirmed the formation of the covalent complex, with OSP as the main body. With an increasing rutin dosage during the preparation process, the amount of rutin in the complex progressively ascended, and the α-helix structure and surface hydrophobicity of the complex gradually declined. The complex exhibited remarkable ABTS radical scavenging capacity and reducing power, which were proportional to the total phenolic content. The OSP/rutin complex could be utilized for the fabrication of O/W nanoemulsions, which remained stable in terms of droplet size and appearance after 28 days of storage at both 4 °C and 25 °C. Furthermore, lipid oxidation in the nanoemulsion stabilized by the OSP/rutin covalent complex could be effectively inhibited, and the emulsion could enhance the UV irradiation resistance of lutein loaded in the oil phase. Our results can provide a reference for the development of protein-polyphenol covalent complexes.

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Publication Details

Journal
Foods
Published
2025-05-09
DOI
https://doi.org/10.3390/foods14101672
Citations
3
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
3.49

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article

Characterization of Okra Seed Protein/Rutin Covalent Complex and Its Application in Nanoemulsions

Benguo Liu, Chengyun He, Yingxuan Zhou, Sheng Geng et al.
3 citations
Foods
Proteins in Food Systems
3.49
article

Characterization of Okra Seed Protein/Rutin Covalent Complex and Its Application in Nanoemulsions

Benguo Liu, Chengyun He, Yingxuan Zhou, Sheng Geng, Lu Bai
article en
3 citations

Abstract

A covalent complex of okra seed protein (OSP) and rutin was prepared using the alkali-induced method and characterized. Its application in nanoemulsions was also evaluated. Multi-spectral analysis confirmed the formation of the covalent complex, with OSP as the main body. With an increasing rutin dosage during the preparation process, the amount of rutin in the complex progressively ascended, and the α-helix structure and surface hydrophobicity of the complex gradually declined. The complex exhibited remarkable ABTS radical scavenging capacity and reducing power, which were proportional to the total phenolic content. The OSP/rutin complex could be utilized for the fabrication of O/W nanoemulsions, which remained stable in terms of droplet size and appearance after 28 days of storage at both 4 °C and 25 °C. Furthermore, lipid oxidation in the nanoemulsion stabilized by the OSP/rutin covalent complex could be effectively inhibited, and the emulsion could enhance the UV irradiation resistance of lutein loaded in the oil phase. Our results can provide a reference for the development of protein-polyphenol covalent complexes.

FoodsVol. 14(10)
Henan Institute of Science and Technology (CN)
National Natural Science Foundation of China
Openalex Percentile: Top 9%
Proteins in Food Systems
3.49
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