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中国精品科技期刊2020
郭月,代世杰,吴汉东. 儿茶素结合对蛋清蛋白结构、乳化性及抗氧化性的影响J. 食品工业科技,2026,47(19):1−9. doi: 10.13386/j.issn1002-0306.2025090200.
引用本文: 郭月,代世杰,吴汉东. 儿茶素结合对蛋清蛋白结构、乳化性及抗氧化性的影响J. 食品工业科技,2026,47(19):1−9. doi: 10.13386/j.issn1002-0306.2025090200.
GUO Yue, DAI Shijie, WU Handong. Effects of Catechin Binding on the Structure, Emulsifying Properties, and Antioxidant Activity of Egg White ProteinJ. Science and Technology of Food Industry, 2026, 47(19): 1−9. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025090200.
Citation: GUO Yue, DAI Shijie, WU Handong. Effects of Catechin Binding on the Structure, Emulsifying Properties, and Antioxidant Activity of Egg White ProteinJ. Science and Technology of Food Industry, 2026, 47(19): 1−9. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025090200.

儿茶素结合对蛋清蛋白结构、乳化性及抗氧化性的影响

Effects of Catechin Binding on the Structure, Emulsifying Properties, and Antioxidant Activity of Egg White Protein

  • 摘要: 本研究针对蛋清蛋白(egg white protein,EWP)在乳液体系中应用时存在的易聚集及抗氧化能力较弱等问题,旨在通过多酚非共价结合同步提升其乳化性和抗氧化活性。采用表没食子儿茶素没食子酸酯(Epigallocatechingallate,EGCG)、表儿茶素没食子酸酯(Epicatechingallate,ECG)、表没食子儿茶素(Epigallocatechin,EGC)、表儿茶素(Epicatechin,EC)四种不同结构的儿茶素单体与蛋清蛋白(egg white protein,EWP)进行非共价结合,调整儿茶素浓度为0~180 µmol/g。通过测定EWP-儿茶素复合物的结合酚含量、内源荧光光谱、傅里叶变换红外光谱、表面疏水性、粒径、电位、还原型十二烷基硫酸钠聚丙烯酰胺凝胶电泳、乳化性及抗氧化性等指标,探究四种儿茶素单体非共价结合对EWP结构、乳化性及抗氧化活性的影响。结果表明:复合物的结合酚含量随儿茶素添加量增加而上升,相同添加量条件下EWP-EGCG结合酚含量更高。复合物的平均粒径随结合酚含量增大呈现先增大后减小趋势,其中60 µmol/g 添加量时EWP-EGCG和EWP-ECG复合物粒径较大,分别为140.43 nm和135.86 nm。复合物Zeta电位随结合酚含量增加而降低,其中EWP-EGCG的效果最为显著,由−4.82 mV下降到−14.80 mV。与EWP相比,EWP-EGCG和EWP-ECG的乳化活性分别提高了2.05倍和1.25倍,乳化稳定性提高了1.08倍和0.67倍。同时,复合物抗氧化活性有效提升,EWP-EGCG和EWP-ECG的Fe3+还原能力较EWP均提高了2.7倍,ABTS阳离子自由基清除率较EWP分别提升了44.3%和46.5%,DPPH自由基清除率较EWP分别提升了16%和14.4%。本研究为开发强乳化稳定性和抗氧化功能的蛋白质配料提供了一定的理论依据,推动其在功能性食品和健康产品中的高值化应用。

     

    Abstract: This study addressed the issues of easy aggregation and weak antioxidant capacity of egg white protein (EWP) in emulsion systems, aiming to simultaneously improve the emulsifying properties and antioxidant activity of EWP through non-covalent binding between EWP and polyphenols. Four catechin monomers with different structures—epigallocatechin gallate (EGCG), epicatechin gallate (ECG), epigallocatechin (EGC), and epicatechin (EC)—were non-covalently bound to EWP, with catechin concentrations ranging from 0 to 180 µmol/g. Various properties of the EWP-catechin complexes were measured, including bound phenol content, intrinsic fluorescence spectroscopy, Fourier-transform infrared spectroscopy, surface hydrophobicity, particle size, Zeta potential, reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, emulsifying properties, and antioxidant activity. The aim was to investigate the effects of the non-covalent binding of the four catechin monomers on the structure, emulsifying properties, and antioxidant activity of EWP. The results showed that the bound phenol content of the complexes increased with the addition level of catechins. Under the same addition level, the bound phenol content was higher for the EWP-EGCG complex. The average particle size of the complexes initially increased and then decreased with increasing bound phenol content. At an additional level of 60 µmol/g, the particle sizes of the EWP-EGCG and EWP-ECG complexes were 140.43 nm and 135.86 nm, respectively. The Zeta potential of the complexes decreased with increasing bound phenol content, with the most significant effect observed for EWP-EGCG, decreasing from −4.82 mV to −14.80 mV. Compared to EWP, the emulsifying activity of EWP-EGCG and EWP-ECG increased by 2.05-fold and 1.25-fold, respectively, while their emulsifying stability improved by 1.08-fold and 0.67-fold, respectively. Meanwhile, the antioxidant activity of the complexes was effectively enhanced. The Fe3+-reducing capacity of both EWP-EGCG and EWP-ECG increased by 2.7-fold compared to EWP. The ABTS cation radical scavenging rate of EWP-EGCG and EWP-ECG improved by 44.3% and 46.5%, respectively, compared to EWP, while their DPPH radical scavenging rate increased by 16% and 14.4%, respectively. This study provides a theoretical basis for the development of protein ingredients with strong emulsifying stability and antioxidant properties, thereby advancing their high-value applications in functional foods and health products.

     

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