The effects of air thawing (AT), water immersion thawing (WT), microwave thawing (MT) and ultrasound combined with slightly acidic electrolyzed water thawing (UST) on the myofibrillar protein (MP) properties (surface hydrophobicity, solubility, turbidity, particle size and zeta potential), protein oxidation (carbonyl content and sulfhydryl content) and structure (primary, secondary and tertiary) of frozen mutton were investigated in comparison with fresh mutton (FM). The solubility and turbidity results showed that the MP properties were significantly improved in the UST treatment. UST treatment could effectively reduce the MP aggregation and enhance the stability, which was similar to the FM. In addition, UST treatment could effectively inhibit protein oxidation during thawing as well. The primary structure of MP was not damaged by the thawing methods. UST treatment could reduce the damage to MP secondary and tertiary structure during the thawing process compared to other thawing methods. Overall, the UST treatment had a positive influence in maintaining the MP properties by inhibiting protein oxidation and protecting protein structure.

空气解冻（AT）、浸水解冻（WT）、微波解冻（MT）和超声联合微酸性电解水解冻（UST）对肌原纤维蛋白（MP）性质（表面疏水性、溶解度、浊度、颗粒度）的影响与新鲜羊肉 (FM) 相比，研究了冷冻羊肉的大小和 zeta 电位）、蛋白质氧化（羰基含量和巯基含量）和结构（一级、二级和三级）。溶解度和浊度结果表明，在 UST 处理中，MP 特性得到显着改善。UST 处理可以有效减少 MP 聚集并增强稳定性，这与 FM 相似。此外，UST处理也能有效抑制解冻过程中的蛋白质氧化。解冻方法未破坏 MP 的一级结构。与其他解冻方法相比，UST处理可以减少解冻过程中MP二级和三级结构的损伤。总体而言，UST 处理通过抑制蛋白质氧化和保护蛋白质结构对维持 MP 特性产生积极影响。