关键词: Cooking loss Epigallocatechin-3-gallate Gel strength Molecular docking Myofibrillar protein Soy protein isolate

Mesh : Catechin / chemistry analogs & derivatives metabolism pharmacology Soybean Proteins / chemistry metabolism Gels / chemistry Molecular Docking Simulation Antioxidants / chemistry pharmacology Hydrophobic and Hydrophilic Interactions Animals Muscle Proteins / chemistry metabolism Cooking Protein Binding

来  源:   DOI:10.1016/j.foodchem.2024.140655

Abstract:
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.
摘要:
这项研究主要研究了大豆分离蛋白(SPI)添加对高剂量表没食子儿茶素-3-没食子酸酯(EGCG)诱导的MP凝胶变质的改善。结果显示EGCG与MP有相互作用,SPI,和HSPI(加热),表明SPI/HSPI与MP对EGCG的竞争力。用SPI/HSPI封装EGCG,具有较高的封装效率和抗氧化性能,抗氧化活性为78.5%~79.2%。FTIR和分子对接结果表明,MP,SPI,HSPI通过氢键和疏水相互作用与EGCG相互作用。SPI/HSPI与MP竞争EGCG,导致MHC和肌动蛋白带的恢复,减轻EGCG和氧化引起的聚集。此外,SPI/HSPI-E显着降低了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结合位点以改善MP凝胶特性,从而减轻高剂量EGCG和氧化引起的MP的有害变化。
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