Oxidative modification of malondialdehyde influences the structure and emulsification properties of egg yolk high-density lipoprotein
Oxidative modification of malondialdehyde influences the structure and emulsification properties of egg yolk high-density lipoprotein
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DOI：
10.1016/j.fbio.2023.102444
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发表时间：
2023-01
期刊：
影响因子：
5.2
通讯作者：
Yang Tian;Songyi Lin;Pengfei Jiang;Guangshun Jiang;Zhijie Bao
中科院分区：
文献类型：
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作者：
Yang Tian;Songyi Lin;Pengfei Jiang;Guangshun Jiang;Zhijie Bao
丙二醛(MDA)是脂质过氧化过程中的次级活性氧化产物。本研究利用丙二醛建立模拟氧化体系，研究其对蛋黄高密度脂蛋白(EYHDL)结构和乳化性能的影响。结果表明，EYHDL2与丙二醛共孵育后，蛋白质发生了羰化反应，巯基含量逐渐降低。傅立叶变换红外光谱(FT-IR)和荧光光谱分析表明，丙二醛氧化破坏了EYHDL的有序结构和蛋白质的结构稳定性。氧化可能导致EYHDL分子间的交联和氧化聚集体的形成，导致表面疏水性降低。对于丙二醛氧化改性的EYHDL型乳液，宏观上有明显的乳液分层现象，倒置荧光显微镜观察到EYHDL型乳液的粒径随丙二醛浓度的增加而增大。丙二醛氧化修饰降低了EYHDL的乳化活性(EAI)和乳化稳定性(ESI)，这可能是由于蛋白质表面疏水性和氧化聚集性的降低所致。
Malondialdehyde (MDA) represents secondary active oxidation products in lipid peroxidation. This research used MDA to establish a simulated oxidation system to study its effects on egg yolk high-density lipoprotein (EYHDL) structure and emulsifying properties. It was shown that incubation of EYHDL with MDA resulted in protein carbonylation and a gradual reduction in the sulfhydryl content. Fourier transform infrared spectroscopy (FT-IR), and fluorescence spectroscopy indicated that MDA oxidation would destroy the ordered structure of EYHDL and the structural stability of the protein. Oxidation might result in the intermolecular cross-linking of EYHDL and the formation of oxidized aggregates, leading to a reduction in surface hydrophobicity. For the EYHDL emulsion modified by MDA oxidation, it could be seen that the emulsion stratification was evident at the macroscopic level, and the grain diameter of the EYHDL emulsion was observed to increase with the MDA concentration by inverted fluorescence microscopy. The emulsification activity (EAI) and emulsification stability (ESI) of EYHDL were decreased by malondialdehyde oxidation modification, which may be due to the decrease of protein surface hydrophobicity and oxidation aggregation.