Functional Characteristics of Walnut Protein Fractions and Rutin Loading by Albumin

This study aimed to systematically compare the functional properties of the four major components (albumin, globulin, prolamin, and glutelin) of protein from Yunnan deep-veined walnuts to screen for protein-based carrier materials with good processing adaptability and the ability to efficiently encapsulate the active ingredient rutin. In addition, the binding and molecular interactions between the preferred protein and rutin were analyzed. The results indicated that albumin exhibited superior performance compared to the other three components in solubility, emulsifying properties, foaming properties, and gel properties, and demonstrated the strongest processing applicability. Further analysis revealed that albumin possessed an excellent amino acid composition (essential amino acid content accounting for 42.30%) and antioxidant activity (with the highest ABTS scavenging rate reaching 85.71 ± 0.26%), which indicated its considerable potential as a functional carrier. Loading rutin onto albumin yielded a walnut albumin–rutin complex (WA@Rut), which significantly enhanced the thermal stability of albumin (with the thermal denaturation temperature elevated to 108.72 °C) and the storage stability of rutin (66.16 ± 5.05% retention after 22 days of storage). Combined analyses of FT-IR spectroscopy, intrinsic fluorescence spectroscopy, molecular docking, and molecular dynamics simulations confirmed that rutin primarily bound to albumin via hydrogen bonding and electrostatic interactions, and formed a stable complex structure. SEM images revealed that the composite surface was smooth and exhibited a flake-like morphology. In conclusion, walnut albumin is a protein resource with significant functional potential in Yunnan deep-veined walnuts, and it exhibits strong processing applicability and enables efficient encapsulation and protection of active ingredients. This study provides novel strategies and theoretical foundations for the high-value utilization of walnut protein.

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Publication Details

Journal
Foods
Published
2026-06-14
DOI
https://doi.org/10.3390/foods15122144
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
0.00

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article

Functional Characteristics of Walnut Protein Fractions and Rutin Loading by Albumin

Yuanli Wang, Yue Wang, Xiang Li, Zilin Wang et al.
Foods
Proteins in Food Systems
article

Functional Characteristics of Walnut Protein Fractions and Rutin Loading by Albumin

Yuanli Wang, Yue Wang, Xiang Li, Zilin Wang, Yang Tian, Fengyating Wu, Yu Zhou, Liang Tao
article en

Abstract

This study aimed to systematically compare the functional properties of the four major components (albumin, globulin, prolamin, and glutelin) of protein from Yunnan deep-veined walnuts to screen for protein-based carrier materials with good processing adaptability and the ability to efficiently encapsulate the active ingredient rutin. In addition, the binding and molecular interactions between the preferred protein and rutin were analyzed. The results indicated that albumin exhibited superior performance compared to the other three components in solubility, emulsifying properties, foaming properties, and gel properties, and demonstrated the strongest processing applicability. Further analysis revealed that albumin possessed an excellent amino acid composition (essential amino acid content accounting for 42.30%) and antioxidant activity (with the highest ABTS scavenging rate reaching 85.71 ± 0.26%), which indicated its considerable potential as a functional carrier. Loading rutin onto albumin yielded a walnut albumin–rutin complex (WA@Rut), which significantly enhanced the thermal stability of albumin (with the thermal denaturation temperature elevated to 108.72 °C) and the storage stability of rutin (66.16 ± 5.05% retention after 22 days of storage). Combined analyses of FT-IR spectroscopy, intrinsic fluorescence spectroscopy, molecular docking, and molecular dynamics simulations confirmed that rutin primarily bound to albumin via hydrogen bonding and electrostatic interactions, and formed a stable complex structure. SEM images revealed that the composite surface was smooth and exhibited a flake-like morphology. In conclusion, walnut albumin is a protein resource with significant functional potential in Yunnan deep-veined walnuts, and it exhibits strong processing applicability and enables efficient encapsulation and protection of active ingredients. This study provides novel strategies and theoretical foundations for the high-value utilization of walnut protein.

FoodsVol. 15(12)
Yunnan Agricultural University (CN)
Yunnan Provincial Science and Technology Department
Openalex Percentile: Top 9%
Proteins in Food Systems
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