海参肌原纤维蛋白在羟自由基生成体系中的结构变化
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国家自然科学基金项目(31671822)


Structural Changes of Sea Cucumber (Stichopus japonicus) Myofibrillar Protein in Hydroxyl Radical-generated System
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    摘要:

    氧化是水产品加工和储存过程中质量下降的重要原因。本研究中,将海参肌原纤维蛋白在不同的羟自由基生成系统(0.01 mol/L FeCl3 / 0.1 mol/L VC / 10 mmol/L H2O2和0.01 mol/L FeCl3 / 0.1 mol/L VC / 50 mmol/L H2O2)中分别氧化3,6,9,12 h,评估蛋白质氧化的相关指标。通过电泳分析蛋白质的交联聚集情况,使用冷场扫描电子显微镜观察蛋白质的微观结构。结果表明,当H2O2浓度为10 mmol/L时,羰基含量在3 h时增加到(4.31 ± 0.32) nmol/mg 蛋白;当H2O2浓度为50 mmol/L时,羰基含量在12 h时增加到(3.72 ± 0.30) nmol/mg 蛋白;游离巯基含量在H2O2浓度为10 mmol/L和50 mmol/L条件下,从0 h的(12.17 ± 0.54) μmol/g蛋白降至12 h(7.27 ± 0.52) μmol/g蛋白和(6.64 ± 0.17) μmol/g蛋白。色氨酸荧光含量随氧化时间的增加呈下降趋势,在12 h达到最低值。在50 mmol/L H2O2的处理条件下,游离氨基含量随着氧化时间的增加显著降低,12 h时降低至对照组含量的65%。电泳分析表明,在非还原条件下,蛋白质的聚集程度随着氧化时间的延长而增强,加入β-巯基乙醇后,蛋白质的聚集程度减弱。微观结构表明:随着氧化时间的增加,肌原纤维蛋白的结构越紧凑,蛋白质的铰链程度越高。结论:海参肌原纤维蛋白在羟自由基体系内发生氧化可引起结构变化。本研究结果对于控制海参加工品质有一定的理论意义。

    Abstract:

    Oxidation is an important reason for the decline of quality of the aquatic products during processing and storage. In this study, we oxidized(0, 3, 6, 9 and 12 h) sea cucumber (Stichopus japonicus) myofibrillar proteins in different hydroxyl radical-generated system (0.01 mol/L FeCl3 / 0.1 mol/L VC / 10 mmol/L H2O2 and 0.01 mol/L FeCl3 / 0.1 mol/L VC / 50 mmol/L H2O2). Then the indicators related to protein oxidation were evaluated. The aggregation of the protein was determined by electrophoresis and the microstructure of protein was observed using cold field scanning electron microscopy. The results indicated that when the concentration of H2O2 was 10 mmol/L and 50 mmol/L, the carbonyl content reached (4.31±0.32) nmol/mg protein and (3.72±0.30) nmol/mg protein at 3 h and 12 h. The content of free-SH decreased from 0 h (12.17 ± 0.54) μmol/g protein to 12 h (7.27 ± 0.52) μmol/g protein and (6.64 ± 0.17) μmol/g protein. The fluorescence content showed a decreasing trend with the increase of oxidation time and reached the lowest value at 12 h. Under the treatment conditions of 50 mmol/L H2O2, the free amino group content decreased significantly with the increase of oxidation time, and decreased to 65% of the control group content at 12 h. Electrophoretic analysis showed that under non-reducing conditions, the degree of protein aggregation increased with the prolongation of oxidation time, and the degree of protein aggregation decreased after the addition of β-mercaptoethanol. The microstructure indicated that as the oxidation time increased, the myofibrillar protein had a compact structure and the degree of hinge of the protein was higher. In summary, the structural changes of the sea cucumber myofibrillar protein caused by oxidation in the hydroxyl radical system. This research has certain theoretical significance for controlling the quality of participation in the sea cucumber.

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贺宝玉;董秀芳;奚倩;白颖;隋悦;启航.海参肌原纤维蛋白在羟自由基生成体系中的结构变化[J].中国食品学报,2020,20(12):16-23

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  • 在线发布日期: 2021-01-12
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