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Flaxseed protein isolates-stabilized oil-water interface: Role of globulin and albumin

文献类型： 外文期刊

作者： Yang, Jing 1 ; Li, Dapeng 3 ; Ashokkumar, Muthupandian 5 ; Duan, Yuqing 4 ; Zhang, Haihui 4 ; Shao, Jiaqi 1 ; Peng, Dengfeng 1 ; Deng, Qianchun 1 ;

作者机构： 1.Chinese Acad Agr Sci, Minist Agr & Rural Affairs, Key Lab Oilseeds Proc,Oil Crops Res Inst, Oil Crops & Lipids Proc Technol Natl & Local Joint, Wuhan 430062, Peoples R China

2.Hubei Res Ctr Oil Plant Prot Engn Technol, Wuhan 430062, Hubei, Peoples R China

3.Shandong Agr Univ, Coll Food Sci & Engn, Shandong Engn Res Ctr Food Nutr & Act Hlth, Tai An 271018, Peoples R China

4.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China

5.Univ Melbourne, Sch Chem, Sonochemistry Grp, Parkville, Vic 3010, Australia

关键词： Flaxseed protein fractions; Structure properties; Interfacial behavior; Oil-water interface

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：12.4； 五年影响因子：13.3 ）

ISSN： 0268-005X

年卷期： 2026 年 172 卷

页码：

收录情况： SCI

摘要： Flaxseed protein isolates (FPIs) are widely used in the creation of multiphase system foods owing to their excellent interfacial and multifunctional properties. However, the contributions of their main components to the interfacial and emulsifying properties remain unclear. Therefore, the structural, interfacial, and functional properties of FPIs and their main component proteins were studied. The results showed that high-purity proteins of flaxseed globulin (FG) and flaxseed albumin (FA) were obtained. FG exhibited lower solubility, larger molecular weight, higher hydrophobicity, and higher viscoelastic modulus. The structure of FA was different, and the interfacial film modulus was low. Differences in protein structure led to discrepancies in protein stable interface system. FG tended to form a rigid interfacial layer and exhibited good stability during emulsification. The hydrophobic domains within the protein facilitated the formation of the interfacial network through enhanced structural rearrangement, thereby increasing emulsion stability. Conversely, the FA-stabilized oil-water interfaces exhibited fragile microstructural characteristics that correlated with reduced emulsifying activity. The adsorption behavior of a protein is governed by its structure. Within the interfacial film formed by FPI, FG served as the primary framework, whereas FA functioned as a filler. These findings establish a mechanistic correlation between the structural attributes of proteins and the stability of protein-stabilized emulsions.

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