从蛋白质的氧化、聚集程度、蛋白质结构以及组织学特性方面,探究不同解冻方式(室温解冻、流水解冻、冷藏解冻和微波解冻)对冷冻鸡腿肉肌原纤维蛋白理化性质的影响。结果表明,室温解冻的羰基含量最高,为3.63 nmol/mg,巯基含量和Ca2+-ATPase活性最低,分别为110.55 μmol/g和0.72 U/mg,说明室温解冻组的蛋白氧化最为严重;肌球蛋白轻链条带模糊,有轻微降解现象;拉曼光谱结果中β-转角含量(26%)和无规则卷曲含量(31%)相对较高,蛋白质结构的稳定性较差。流水解冻的蛋白氧化程度较轻,具体表现为:其羰基含量和表面疏水性最低,分别为0.97 nmol/mg和10.36 μg;Ca2+-ATPase活性最高,为2.95 U/mg;组织结构紧密,α-螺旋含量最高(58%),蛋白质二级结构较为完整。冷藏解冻的巯基损失最小,巯基含量为258.23 μmol/g,肌球蛋白轻链条带颜色较深,有聚集现象,组织结构的紧密性与流水解冻组无明显差异。微波解冻的组织结构破坏严重,肌纤维间隙较大,蛋白质二级结构较紊乱,α-螺旋含量最少,为29%。因此,流水解冻可以作为解冻鸡腿肉的主要解冻方式。
From the aspects of protein oxidation characteristics, aggregation degree, protein structure, and histological characteristics, the effects of different thawing methods (room temperature thawing, flow thawing, cold storage thawing, and microwave thawing) on the physical and chemical properties of frozen chicken thigh myofibrillar protein were explored. Results showed that the carbonyl content of thawed at room temperature was the highest, 3.63 nmol/mg, and the sulfhydryl content and Ca2+-ATPase activity were the lowest, 110.55 μmol/g and 0.72 U/mg, respectively, indicating that the protein oxidization in the room thawed group was the most severe. The light chain band was fuzzy and slightly degraded. The content of β-turn (26%) and the content of random curl (31%) in the Raman spectroscopy results were relatively high, and the stability of the protein structure was poor. The degree of protein oxidation of hydrolyzed fluid was lighter, which was characterized by its lowest carbonyl content and surface hydrophobicity, 0.97 nmol/mg and 10.36 μg, respectively, and the highest Ca2+-ATPase activity at 2.95 U/mg. At the same time, the tissue structure was tight, the α-helix content was the highest (58%), and the protein secondary structure was relatively complete. The loss of sulfhydryl groups in cold storage and thawing was the smallest, the content of sulfhydryl groups was 258.23 μmol/g, the color of the myosin light chain was darker, there was an aggregation phenomenon, and the tightness of tissue structure was not significantly different from that in the fluid thawing group. The tissue structure of microwave thawing was severely damaged, the muscle fiber gap was large, the protein secondary structure was disordered, and the α-helix content was the least, which was 29%. Therefore, flow thawing could be used as the main thawing method for thawing chicken thigh meat.
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