氧化还原蛋白质组学分析揭示了来自鲢鱼 (Hypophthalmichthys molitrix) 的肌原纤维蛋白的微波诱导氧化修饰,Journal of Agricultural and Food Chemistry

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氧化还原蛋白质组学分析揭示了来自鲢鱼 (Hypophthalmichthys molitrix) 的肌原纤维蛋白的微波诱导氧化修饰
Journal of Agricultural and Food Chemistry ( IF 5.7 ) Pub Date : 2021-08-03 , DOI: 10.1021/acs.jafc.1c03045
Xidong Jiao _{1,

2} , Bowen Yan _{1,

2} , Jianlian Huang _{3,

4,

5} , Jianxin Zhao _{1,

2} , Hao Zhang _{1,

2} , Wei Chen _{1,

2} , Daming Fan _{1,

2,

3}

Affiliation

为了深入了解微波加热 (MW) 过程中肌原纤维蛋白 (MPs) 中半胱氨酸的氧化行为，本研究应用了基于同量异位碘乙酰串联质量标签技术的定量氧化还原蛋白质组学分析。来自鲢鱼肌肉的 MP 经受 MW 和水浴加热 (WB)，具有相同的时间 - 温度曲线，以消除由不均匀能量输入引起的热差异。与未热处理的相比，总共发现 422 种蛋白质在热处理后差异表达。然而，MW 触发了大量的蛋白质和半胱氨酸位点进行氧化。肌球蛋白重链、肌球蛋白结合蛋白 C、nebulin、α-actinin-3-like 和肌动蛋白被发现在微波辐射下对氧化非常敏感。尤其，MW 在肌球蛋白头部的半胱氨酸位点 9 处引起这种修饰，揭示了微波处理过程中过量半胱氨酸交联导致 MP 凝胶化的增强机制。此外，基因本体论和功能富集分析表明，两种热处理导致了离子结合、肌肉细胞发育和含蛋白质复合物组装的一些差异。总体而言，这项研究首次报道了由 MW 和 WB 处理引起的氧化还原蛋白质组学变化，从而进一步了解微波诱导的 MPs 氧化修饰。基因本体论和功能富集分析表明，两种热处理导致离子结合、肌肉细胞发育和含蛋白质复合物组装的一些差异。总体而言，这项研究首次报道了由 MW 和 WB 处理引起的氧化还原蛋白质组学变化，从而进一步了解微波诱导的 MPs 氧化修饰。基因本体论和功能富集分析表明，两种热处理导致离子结合、肌肉细胞发育和含蛋白质复合物组装的一些差异。总体而言，这项研究首次报道了由 MW 和 WB 处理引起的氧化还原蛋白质组学变化，从而进一步了解微波诱导的 MPs 氧化修饰。

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Redox Proteomic Analysis Reveals Microwave-Induced Oxidation Modifications of Myofibrillar Proteins from Silver Carp (Hypophthalmichthys molitrix)

To provide an insight into the oxidation behavior of cysteines in myofibrillar proteins (MPs) during microwave heating (MW), a quantitative redox proteomic analysis based on the isobaric iodoacetyl tandem mass tag technology was applied in this study. MPs from silver carp muscles were subjected to MW and water bath heating (WB) with the same time–temperature profiles to eliminate the thermal differences caused by an uneven energy input. Altogether, 422 proteins were found to be differentially expressed after thermal treatments as compared to that with no heat treatment. However, MW triggered a larger number of proteins and cysteine sites for oxidation. Myosin heavy chain, myosin-binding protein C, nebulin, α-actinin-3-like, and titin were found to be highly susceptible to oxidation under microwave irradiation. Notably, MW caused such modifications at cysteine site 9 in the head of myosin, revealing the enhancement mechanism of MP gelation by excess cysteine cross-linking during microwave processing. Furthermore, Gene Ontology and functional enrichment analyses suggested that the two thermal treatments resulted in some differences in ion binding, muscle cell development, and protein-containing complex assembly. Overall, this study is the first to report the redox proteomic changes caused by MW and WB treatments, thus providing a further understanding of the microwave-induced oxidative modifications of MPs.

更新日期：2021-08-25

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