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Influence of Refrigerated Storage on Water Status Protein Oxidation Microstructure and Physicochemical Qualities of Atlantic Mackerel (

机译:冷藏储存对大西洋鲭鱼水土地位蛋白质氧化微观结构和物理化学品质的影响(

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摘要

Moisture migration, protein oxidation, microstructure, and the physicochemical qualities of Atlantic mackerel during storage at 4 °C and 0 °C were explored in this study. Three proton components were observed in mackerel muscle using low-field nuclear magnetic resonance relaxation, which were characterized as bound water, immobilized water, and lipid. The relaxation peak of immobilized water shifted to a shorter relaxation time and its intensity decreased with the proceeding of the storage process. T1 and T2 weighted images obtained by magnetic resonance imaging showed a slightly continuous decrease in the intensity of water. The significant decrease in sulfhydryl (SH) content and the increase in carbonyl group (CP) content, disulfide bond content, and hydrophobicity revealed the oxidation of protein during storage. The contents of α-helixes in proteins decreased while that of random coils increased during storage, which suggested changes in the secondary structure of mackerel protein. The storage process also caused the contraction and fracture of myofibrils, and the granulation of endolysin protein. In addition, the drip loss, total volatile basic nitrogen (TVB-N), thiobarbituric acid-reactive substances (TBARS) value, and b* value increased significantly with the storage time.
机译:本研究探讨了在4°C和0°C储存过程中大西洋鲭鱼的水分迁移,蛋白质氧化,微观结构和物理化学质量。使用低场核磁共振弛豫在鲭鱼肌肉中观察到三种质子组分,其特征为边缘水,固定水和脂质。固定水的弛豫峰变为较短的弛豫时间,并且随着存储过程的进行,其强度降低。通过磁共振成像获得的T1和T2加权图像显示水强度略微连续。巯基(SH)含量的显着降低及羰基含量的增加(CP)含量,二硫键粘合含量和疏水性揭示了储存过程中蛋白质的氧化。蛋白质中α-螺旋的含量降低,而无随机线圈在储存期间增加,这提出了鲭鱼蛋白蛋白二次结构的变化。储存过程还导致肌原纤维的收缩和骨折,以及眼蛋白蛋白的造粒。此外,通过储存时间,滴落损失,总挥发性碱性氮(TVB-N),硫碱酸 - 反应性物质(TBARS)值和B *值显着增加。

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