Effects of non-covalent binding of different proteins and apple polyphenols on structure and functional properties

文献类型： 外文期刊

第一作者： Yin, Bangfeng

作者： Yin, Bangfeng;Wang, Ruiqi;Zhao, Yuanyuan;Zhao, Wenting;Wang, Dan;Qin, Peiyou;Zhao, Shuang;Zhao, Xiaoyan;Wang, Pan;Wu, Qiming;Kan, Juntao;Yin, Bangfeng;Zheng, Zhenjia

作者机构：

关键词： Apple polyphenols; Plant proteins; Non-covalent binding; Enzyme activity; Bio-accessibility; Antioxidant activity

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： 2025 年 166 卷

页码：

收录情况： SCI

摘要： Apple polyphenols (AP) exhibit diverse biological activities but have limited bio-accessibility, while plant proteins often suffer from poor solubility, limiting their functional properties. Therefore, there is a significant research interest in synergistically enhancing the bio-accessibility of AP and improving the functional characteristics of plant proteins. In this study, soy protein isolate (SPI), whey protein isolate (WPI), chickpea protein (CP), and tartary buckwheat protein (TBP) were utilized to synthesize AP-protein complexes through non- covalent binding with AP. Structural characterization found that the polyphenol contents were as follows: TBP-AP > CP-AP > SPI-AP > WPI-AP. Multi-spectral analysis indicated that AP altered the secondary structures of the four proteins, are reduced their surface hydrophobicity. In vitro, antioxidant activity assessments demonstrated that polyphenols significantly enhanced the antioxidant capacity of the proteins. AP-protein complexes protected against H2O2-induced oxidative stress in HepG2 cells, and restored antioxidant enzyme activity (WPI-AP > TBP-AP > SPI-AP > CP-AP). Furthermore, it enhanced alpha-amylase and alpha-glucosidase inhibition, demonstrating the potential to regulate blood sugar levels. In simulated digestion models, the sequence of TBP-AP > WPI-AP > CP-AP > SPI-AP effectively protected AP from delayed release in the intestinal phase, thereby enhancing the bio-accessibility of AP. This study not only identifies the optimal synergistic interaction between AP and TBP but also provides new insights into enhancing the bioavailability of AP and effectively replacing animal protein application with plant proteins for potential high-value utilization of AP and plant proteins.

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