超声辅助磷酸盐处理在低离子强度下对兔肌原纤维蛋白增溶和稳定分散的影响

IF 9.8 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Chemistry Pub Date : 2025-01-13 DOI:10.1016/j.foodchem.2025.142898

Chang Su , Yuxin Huang , Jiaxin Chen , Hongjun Li , Dong Zhang , Yong Tang

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引用次数: 0

摘要

研究了高强度超声（HIU）对低盐培养基中肌原纤维蛋白（MPs）分散性的影响。hiu辅助的STPP或TSPP可以显著提高MPs的溶解度和分散性（分别从38.12 %提高到94.08 %和37.80 %提高到89.91 %），而NaCl或SHMP的作用可以忽略。MPs在STPP和TSPP介质中比在NaCl和SHMP介质中具有更高的表面电荷和更强的亲水性。CLSM和SDS-PAGE结果显示，MP在STPP和TSPP培养基中解聚。STPP和TSPP中的MPs呈柔性α-螺旋构象。HIU可诱导STPP和TSPP培养基中的肌球蛋白和肌动蛋白重排，并通过二硫键生成可溶性低聚物。相比之下，MPs在SHMP和NaCl中表现出稳定的β-薄片构象，阻碍了HIU的修饰作用。介质可以通过改变表面电荷和亲水性来影响HIU对MPs的修饰效果。

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Effect of ultrasound-assisted phosphates treatment on solubilization and stable dispersion of rabbit Myofibrillar proteins at low ionic strength

The effects of high-intensity ultrasound (HIU) on the dispersibility of myofibrillar proteins (MPs) in low-salt medium were investigated. HIU-assisted STPP or TSPP could sharply improve the solubility and dispersibility of MPs (from 38.12 % to 94.08 % and 37.80 % to 89.91 %, respectively), whereas the use of NaCl or SHMP had negligible effects. MPs in STPP and TSPP medium had higher surface charge and stronger hydrophilic ability than those in NaCl and SHMP medium. The results of CLSM and SDS-PAGE showed MP depolymerization in STPP and TSPP medium. MPs in STPP and TSPP displayed a flexible α-helix conformation. HIU could induce the rearrangement of myosin and actin in STPP and TSPP medium and generated soluble oligomers by disulfide bonds. By contrast, MPs in SHMP and NaCl exhibited a stable β-sheet conformation, hindering the modification effect of HIU. Medium could affect the modification effect of HIU on MPs by changing surface charge and hydrophilicity.

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来源期刊

Food Chemistry 工程技术-食品科技

CiteScore

16.30

自引率

10.20%

发文量

3130

审稿时长

122 days

期刊介绍： Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.