大豆分离蛋白通过调节表没食子儿茶素没食子酸酯和肌原纤维蛋白之间的非共价相互作用来改善凝胶特性。
Soy protein isolate ameliorate gel properties by regulating the non-covalent interaction between epigallocatechin-3-gallate and myofibrillar protein.
机构信息
College of Food Science and Engineering, Northwest A&F University, No. 22 Xinong Road, Yangling, Shaanxi 712100, China.
College of Food Science and Engineering, Northwest A&F University, No. 22 Xinong Road, Yangling, Shaanxi 712100, China.
出版信息
Food Chem. 2024 Dec 1;460(Pt 3):140655. doi: 10.1016/j.foodchem.2024.140655. Epub 2024 Jul 31.
This study primarily investigated the improvement of high-dose Epigallocatechin-3-Gallate (EGCG)-induced deterioration of MP gel by soy protein isolate (SPI) addition. The results showed that EGCG could interact with MP, SPI, and HSPI (heated), indicating the competitive ability of SPI/HSPI against EGCG with MP. EGCG was encapsulated by SPI/HSPI with high encapsulation efficiency and antioxidation, with antioxidant activities of 78.5% ∼ 79.2%. FTIR and molecular docking results revealed that MP, SPI, and HSPI interacted with EGCG through hydrogen bonding and hydrophobic interactions. SPI/HSPI competed with MP for EGCG, leading to the restoration of MHC and Actin bands, alleviating the aggregation caused by EGCG and oxidation. Additionally, SPI/HSPI-E significantly reduced the high cooking loss (23.71 and 26.65%) and gel strength (13.60 and 17.02%) induced by EGCG. Hence, SPI competed with MP for EGCG binding site to ameliorate MP gel properties, thereby alleviating the detrimental changes in MP caused by high-dose EGCG and oxidation.
本研究主要探讨了添加大豆分离蛋白（SPI）对高剂量表没食子儿茶素没食子酸酯（EGCG）诱导的鱼糜凝胶劣化的改善作用。结果表明，EGCG 可与 MP、SPI 和热变性 SPI（HSPI）相互作用，表明 SPI/HSPI 与 MP 竞争 EGCG 的能力。SPI/HSPI 对 EGCG 具有高包封效率和抗氧化能力，包封率高达 78.5%79.2%，具有 78.5%79.2%的抗氧化活性。傅里叶变换红外光谱（FTIR）和分子对接结果表明，MP、SPI 和 HPI 通过氢键和疏水相互作用与 EGCG 相互作用。SPI/HSPI 与 MP 竞争 EGCG，从而恢复 MHC 和肌动蛋白条带，缓解 EGCG 和氧化引起的聚集。此外，SPI/HSPI-E 显著降低了 EGCG 诱导的高蒸煮损失（23.71%和 26.65%）和凝胶强度（13.60%和 17.02%）。因此，SPI 与 MP 竞争 EGCG 结合位点，改善了 MP 凝胶的性质，从而缓解了高剂量 EGCG 和氧化对 MP 产生的不利变化。
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