Impact of salt content and hydrogen peroxide-induced oxidative stress on protein oxidation, conformational/morphological changes, and micro-rheological properties of porcine myofibrillar proteins
Impact of salt content and hydrogen peroxide-induced oxidative stress on protein oxidation, conformational/morphological changes, and micro-rheological properties of porcine myofibrillar proteins
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盐含量和过氧化氢诱导的氧化应激对猪肌原纤维蛋白的蛋白质氧化、构象/形态变化和微流变特性的影响
DOI：
10.1016/j.foodchem.2021.131074
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发表时间：
2022
期刊：
影响因子：
8.8
通讯作者：
Guofeng Jin
中科院分区：
文献类型：
--
作者：
Min Zhang;Chengliang Li;Yangping Zhang;Jiajing Pan;Shuangjia Huang;Lichao He;Guofeng Jin
自由基扩散过程可干扰肌原纤维的盐化和再水化。研究了盐含量（0、1、3和5%）和H2 O2/抗坏血酸基羟基自由基（自由基dotOH）产生体系（1、10、20 mM H2 O2）对猪肌原纤维蛋白（MP）氧化、构象、聚集和热稳定性的影响。结果表明，5%的食盐抑制了MP的羰基化反应，巯基损失和色氨酸淬灭都很严重。傅里叶变换红外光谱（FTIR）、激光散射和扫描电子显微镜（SEM）表明，20 mM H2 O2使MP的α-螺旋转化为β-折叠，有利于较大的聚集体在盐诱导的纤维溶胀过程中选择性地暴露于溶剂。当盐浓度≤1%时，氧化MPs发生部分解折叠并具有较高的柔韧性;当盐浓度高达5%时，氧化MPs的水化能力降低，纤维间氢键减弱，蛋白溶解度提高。微观流变学结果表明，1%的盐和10 mM的H2 O2呈现了一个更致密的热定型MPs凝胶的结构。
Salting and rehydration of myofibrils can be interfered with free radical diffusion process. This study investigated the effects of salt content (0, 1, 3 and 5%) and H2O2/ascorbate-based hydroxyl radical (radical dotOH)-generating system (1, 10, 20 mM H2O2) on the oxidation, conformation, aggregation, and thermal stability of porcine myofibrillar proteins (MPs). Results showed that 5% of salt inhibited carbonylation of MPs with intensive sulfhydryl loss and tryptophan quenching. Fourier transform infrared (FTIR), laser light scattering, and scanning electron microscopy (SEM) suggested that 20 mM H2O2transformed more α-helix into β-sheet of MPs, favoring larger aggregates being selectively exposed towards solvent during salt-induced fiber swelling. Oxidized MPs brined with ≤1% salt underwent partial unfolding with higher flexibility, while up to 5% of salt greatly hampered their hydration potential and weakened inter-fibrillar hydrogen bond with an improved protein solubility. Micro-rheology revealed that 1% of salt and 10 mM H2O2rendered a denser structure of heat-set MPs gels.