Fabrication of tannins and oat protein non-covalent complexes: Effect on the structure and in vitro digestion properties of oat proteins
文献类型： 外文期刊
作者： Chen, Xi 1 ; Han, Xue 1 ; Chen, Mianhong 2 ; Lu, Xuli 2 ; Zhou, Wei 2 ; Li, Ruyi 2 ;
作者机构： 1.Harbin Inst Technol, Sch Chem & Chem Engn, Harbin 150001, Peoples R China
2.Chinese Acad Trop Agr Sci, Agr Prod Proc Res Inst, Key Lab Trop Crop Prod Proc, Minist Agr & Rural Affairs, Zhanjiang 524001, Peoples R China
关键词： Oat protein isolate; Proanthocyanidins; Tannic acid; Noncovalent binding; In vitro digestion
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）
ISSN： 0141-8130
年卷期： 2025 年 304 卷
页码：
收录情况： SCI
摘要： This study explored the non-covalent interactions between oat protein isolate (OPI) and two tannic compounds-proanthocyanidins (PA) and tannic acid (TA)-and examined their impact on the structural and digestive properties of oat proteins. The combination of OPI with tannic compounds formed granular complexes with particle sizes ranging from 126 to 240 nm and zeta potentials between-35 and-44 mV. Compared to OPI alone, the alpha-helix and beta-turn contents decreased, while the beta-sheet and random coil contents increased in both OPI-tannin complexes. Fluorescence spectra analysis indicated that hydrogen bonding was the main interaction force in OPI-PA complexes, while OPI and TA were primarily bound by hydrophobic interactions. The simulated digestion analysis showed that the protein digestibility was delayed in the OPI-tannin complexes, likely due to the inhibition of digestive enzyme activity by tannic compounds, which slowed OPI digestibility. Additionally, the oxidation resistance of the OPI-tannin complexes significantly improved after in vitro digestion, indicating that the non-covalent complexes provided superior protection for the tannic compounds. These findings offer theoretical support for the design and utilization of oat- and tannin-rich foods.
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