pH值对纯化猪肉肌球蛋白热聚集体的影响
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国家自然科学基金青年科学基金项目(31801572);“十三五”国家重点研发计划项目(2018YFD0401205);现代农业产业技术体系北京市生猪产业创新团队项目(BAIC02-2019)


Effects of pH Values on the Heat-Induced Aggregation of Pork Myosin
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    摘要:

    为研究pH值对肌球蛋白热聚集行为的影响,以纯化的猪肉肌球蛋白为对象,在体系pH值5.5,6,6.5,7,7.5,8,8.5条件下,采用动态光散射、差示荧光扫描仪、负染透射电镜等技术进行研究。结果表明:pH值由5.5升至8.5,蛋白变性温度由40.2 ℃降至36.9 ℃,Ca2+-ATP酶失活温度由40 ℃升至60 ℃,电镜观察到蛋白聚集体之间交联程度显著增加。pH 5.5条件下,聚集体结构较为松散,形成颗粒状聚集体。随着pH值的升高,加热过程中蛋白变性,结构充分展开,疏水基团暴露度高,分子间疏水性相互作用强烈,分子之间有序聚集。本研究阐明猪肉肌球蛋白热聚集形成机制,为解析其它纤维状蛋白质聚集机制提供理论基础,对指导肉制品工业生产具有重要的意义。

    Abstract:

    In order to study the effect of different pH value on the thermal aggregation behavior of myosin, the purified pork myosin was used as the research object. Under the pH value of 5.5, 6, 6.5, 7, 7.5, 8, 8.5, the dynamic light scattering, differential fluorescence scanner, negative dye transmission electron microscopy were used. The results showed that the pH increased from 5.5 to 8.5, the denaturation temperature of protein decreased from 40.2 ℃ to 36.9 ℃, the inactivation temperature of Ca2+- ATPase increased from 40 ℃ to 60 ℃, and the degree of cross-linking between protein aggregates increased significantly. Under the condition of pH 5.5, the aggregate structure is relatively loose, forming granular aggregate. With the increase of pH value, the protein denatured, the structure fully expanded, the exposure of hydrophobic groups was high, the hydrophobic interaction between molecules was strong, and the molecules gathered orderly. This study elucidated the formation mechanism of thermal aggregation of pork myosin, provided a theoretical basis for the analysis of other fibrous protein aggregation mechanisms, and had important practical significance for guiding the industrial production of meat products.

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娄爱华;潘腾;陈星;沈清武;张炎;罗洁. pH值对纯化猪肉肌球蛋白热聚集体的影响[J].中国食品学报,2021,21(6):46-53

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  • 在线发布日期: 2021-07-16
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