PDF(Pubmed)
Abstract：
Knowledge regarding the denaturation process and control methods for depolymerized sol-state myofibrillar proteins (MPs) during freezing remains scant. This study investigated the effects of protein cross-linking treatment before freezing on physicochemical and subsequent gelation properties of MPs sol subjected to freeze-thaw (F-T) cycles. Results indicated that after five F-T cycles, cross-linked MPs sols showed increased high molecular weight polymers and bound water (T21a and T21b) mobility, suggesting enhanced protein-protein interactions at the expense of protein-water interactions. Upon heating after F-T cycles, gels formed from cross-linked sols exhibited significantly higher hardness, springiness, and cooking loss (P < 0.05), alongside more contracted gel networks. Correlation analysis revealed that the formation and properties of thermal gel after freezing closely relate to changes in molecular conformation and chemical bonds of cross-linked MPs sol during freezing. This study provides new insights into regulating the freezing stability and post-thawed thermal processing properties of sol-based surimi products.
摘要：
有关冷冻过程中解聚的溶胶态肌原纤维蛋白（MP）的变性过程和控制方法的知识仍然很少。这项研究调查了冷冻前蛋白质交联处理对经过冻融（F-T）循环的MPs溶胶的物理化学和随后的胶凝特性的影响。结果表明，经过五个F-T循环后，交联的MPs溶胶显示高分子量聚合物和结合水(T21a和T21b)迁移率增加，这表明以蛋白质-水相互作用为代价的蛋白质-蛋白质相互作用增强。在F-T循环后加热时，由交联溶胶形成的凝胶表现出明显更高的硬度，弹性，蒸煮损失(P<0.05)，以及更多收缩的凝胶网络。相关分析表明，冷冻后热凝胶的形成和性质与冷冻过程中交联MPs溶胶的分子构象和化学键的变化密切相关。这项研究为调节溶胶基鱼糜产品的冷冻稳定性和解冻后的热加工性能提供了新的见解。
