关键词: Hydrophobic interaction Self-assembly Sodium metabisulfite Surimi gel

Mesh : Animals Gels / chemistry Sulfites / chemistry Catechin / chemistry analogs & derivatives Muscle Proteins / chemistry Carps Fish Proteins / chemistry Hydrophobic and Hydrophilic Interactions Oxidation-Reduction Myofibrils / chemistry

来  源:   DOI:10.1016/j.foodchem.2024.140050

Abstract:
Myofibrillar protein (MP) gels are susceptible to oxidation, which can be prevented by complexing with hydrophilic polyphenols, but may cause gel deterioration. Sodium metabisulfite (Na2S2O5) has been used to induce self-assembly of MP and analyze the impact of self-assembly on the quality of composite gels containing high amounts of (-)-epigallocatechin gallate (EGCG). Hydrophobic forces were confirmed as the main driver of self-assembly. Self-assembly reduced the size of the MP-EGCG complex to approximately 670 nm and increased the gel\'s hydrophobic force by approximately 3.6-fold. The maximum hardness of the Na2S2O5-treated MP-EGCG composite gel was 52.43 g/kg, which was approximately 49% greater than pure MP gel. After oxidative treatment, the Na2S2O5-treated MP-EGCG composite gel had considerably lower carbonyl and dityrosine levels (2.47-μmol/g protein and 450 a.u.) than the control (8.37-μmol/g protein and 964 a.u.). Therefore, Na2S2O5 shows potential as a cost-effective additive for alleviating MP limitations in the food industry.
摘要:
肌原纤维蛋白(MP)凝胶易于氧化,这可以通过与亲水性多酚络合来防止,但可能导致凝胶变质。焦亚硫酸钠(Na2S2O5)已用于诱导MP的自组装,并分析了自组装对含有大量(-)-表没食子儿茶素没食子酸酯(EGCG)的复合凝胶质量的影响。疏水性力被确认为自组装的主要驱动因素。自组装将MP-EGCG复合物的尺寸减小至约670nm,并将凝胶的疏水性力增加约3.6倍。Na2S2O5处理的MP-EGCG复合凝胶的最大硬度为52.43g/kg,比纯MP凝胶高约49%。氧化处理后,Na2S2O5处理的MP-EGCG复合凝胶的羰基和二酪氨酸水平(2.47μmol/g蛋白质和450a.u.)明显低于对照(8.37μmol/g蛋白质和964a.u.)。因此,Na2S2O5显示出作为缓解食品工业中MP限制的成本有效添加剂的潜力。
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