冷等离子体增强卵清蛋白-没食子酸的共价结合及其功能性质。
Cold plasma for enhancing covalent conjugation of ovalbumin-gallic acid and its functional properties.
机构信息
College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China; School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China.
College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China.
出版信息
Food Chem. 2024 Oct 1;454:139753. doi: 10.1016/j.foodchem.2024.139753. Epub 2024 May 20.
The utilization of cold plasma (CP) treatment to promote covalent conjugation of ovalbumin (OVA) and gallic acid (GA), as well as its functionality, were investigated. Results demonstrated that CP significantly enhanced the covalent grafting of OVA and GA. The maximum conjugation of GA, 24.33 ± 2.24 mg/g, was achieved following 45 s of CP treatment. Covalent conjugation between GA and OVA were confirmed through analyses of total sulfhydryl (-SH) group, Fourier transform infrared (FTIR) spectroscopy, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Unfolding of the OVA molecule occurred upon conjugation with GA, as evidenced by multiple spectroscopy analyses. Additionally, conjugation with GA resulted in significant improvements in the antioxidant activity and emulsifying properties of OVA. This study demonstrated that CP is a robust and sustainable technique for promoting the covalent conjugate of polyphenols and proteins, offering a novel approach to enhance the functional properties of proteins.
利用冷等离子体（CP）处理来促进卵清蛋白（OVA）和没食子酸（GA）的共价结合及其功能，进行了研究。结果表明，CP 显著增强了 OVA 和 GA 的共价接枝。CP 处理 45 秒后，GA 的最大接枝量达到 24.33±2.24mg/g。通过总巯基（-SH）基团、傅里叶变换红外（FTIR）光谱和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分析，证实了 GA 与 OVA 之间的共价结合。GA 与 OVA 结合导致 OVA 分子展开，这一点可以通过多种光谱分析得到证明。此外，GA 的结合显著提高了 OVA 的抗氧化活性和乳化性能。本研究表明，CP 是一种促进多酚和蛋白质共价结合的强大且可持续的技术，为增强蛋白质的功能特性提供了一种新方法。
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