焦磷酸钠对肌原纤维蛋白的磷酸化修饰会影响乳液在不同pH条件下凝胶的形成和氧化稳定性。,Food & Function

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焦磷酸钠对肌原纤维蛋白的磷酸化修饰会影响乳液在不同pH条件下凝胶的形成和氧化稳定性。
Food & Function ( IF 5.1 ) Pub Date : 2019-10-16 , DOI: 10.1039/c9fo01397k
Jinyu Chen ₁ , Yunxia Ren , Kunsheng Zhang , Jinping Qu , Fangyang Hu , Yijun Yan

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涉及蛋白质，脂质和水之间相互作用的凝胶基质的形成在加工肉的质地特性中起着至关重要的作用。本研究研究了焦磷酸钠（SPP）在不同pH条件（5.0-9.0）下对肌原纤维蛋白（MP）稳定的乳液凝胶的质构性质和氧化稳定性的影响。SPP改性的MP乳液凝胶在pH 6.0和7.0时具有改善的弹性，强度，持水能力和氧化稳定性。这种改善应主要归因于通过磷酸基团和氨基酸的-NH3 +之间的离子相互作用增强了蛋白质-蛋白质交联，这些相互作用是在吸附和/或未吸附的蛋白质之间均匀形成的，截留了MPs的一部分（肌球蛋白重链，肌动蛋白和网络中的肌钙蛋白T）。所以，油滴更好地粘附在凝胶基质上。然而，由于在pH 8.0和9.0下MPs附着过多的磷酸盐导致蛋白质分子之间的静电排斥力增加，以及在pH 5.0时蛋白质沉淀，导致MP稳定的乳液凝胶结构崩溃，因此总体上降低了凝胶性能和氧化稳定性。LC-MS / MS结果证实，在pH 6.0时，磷酸基团通过COP键成功地引入了MP，磷酸化位点位于丝氨酸残基（Ser14，Ser79，Ser96，Ser148，Ser2427和Ser5272），苏氨酸残基上。（Thr118和Thr926），以及酪氨酸残基（Tyr215和Tyr425）。该结果为更好地理解多磷酸盐在肉蛋白/油复合系统中的作用提供了一个新的方面。

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Phosphorylation modification of myofibrillar proteins by sodium pyrophosphate affects emulsion gel formation and oxidative stability under different pH conditions.

Formation of a gel matrix, involving interactions between proteins, lipids, and water, plays an essential role in the textural properties of processed meats. This study investigated the effects of sodium pyrophosphate (SPP) on the textural properties and oxidative stability of myofibrillar protein (MP)-stabilized emulsion gels under different pH conditions (5.0-9.0). The SPP-modified MP emulsion gels showed an improved elasticity, strength, water-holding capacity, and oxidative stability at pH 6.0 and 7.0. This improvement should be mainly attributed to the enhanced protein-protein crosslinks via ionic interaction between phosphate groups and -NH3+ of amino acids, which were homogeneously formed among adsorbed and/or unadsorbed proteins, entrapping fractions of MPs (myosin heavy chain, actin, and troponin T) within the network. Therefore, the oil droplets were better adherent to the gel matrix. Nevertheless, increased electrostatic repulsion between protein molecules due to excessive phosphates attached to MPs at pH 8.0 and 9.0, as well as protein precipitation at pH 5.0, caused the collapse of the MP-stabilized emulsion gel structure, and thus, overall decreased the gel properties and oxidative stability. LC-MS/MS results confirmed that phosphate groups were successfully introduced to MPs through C-O-P bonds at pH 6.0, and the phosphorylation sites were found to be on serine residues (Ser14, Ser79, Ser96, Ser148, Ser2427, and Ser5272), threonine residues (Thr118 and Thr926), and tyrosine residues (Tyr215 and Tyr425). The results provided a new aspect for better understanding the effect of polyphosphates in meat protein/oil composite systems.

更新日期：2019-10-17

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