DHA氧化产物对牛血清白蛋白的修饰作用及其对蛋白质结构的影响

doi:10.12441/spyswjs.20250915002

首页 > 过刊浏览>2026年第45卷第4期 >18-27. DOI:10.12441/spyswjs.20250915002

DHA氧化产物对牛血清白蛋白的修饰作用及其对蛋白质结构的影响
DOI:
                        10.12441/spyswjs.20250915002
                    
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作者单位:1北京工商大学食品与健康学院，北京 100048;2北京工商大学轻工科学与工程学院，北京 100048
作者简介:
通讯作者:肖俊松（1980—），男，博士，副教授，硕士研究生导师，主要从事食品功能成分及膳食因素诱导的代谢综合征的相关机制研究。E-mail：xiaojs@th.btbu.edu.cn
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基金项目:北京市自然科学基金项目（2202014，6212002）。

Modification of Bovine Serum Albumin by DHA Oxidation Products and Its Impact on Protein Structure

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1School of Food and Health, Beijing Technology and Business University, Beijing 100048, China;2School of Light Industry Science and Engineering, Beijing Technology and Business University, Beijing 100048, China

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【目的】探讨二十二碳六烯酸（DHA）氧化衍生的2-烯醛和二烯醛对牛血清白蛋白（BSA）的共价修饰作用及其对蛋白质结构的影响。【方法】采用超高效液相色谱-串联质谱联用技术（UPLC-MS/MS）分析醛类-蛋白质加合物形成情况，通过2，4-二硝基苯肼（DNPH）比色法测定蛋白质羰基化水平，并利用傅里叶变换红外光谱（FT-IR）和紫外可见吸收光谱分析蛋白质二级结构变化。【结果】二烯醛与BSA中组氨酸和赖氨酸残基形成的加合物显著多于2-烯醛；随着醛类浓度的升高，BSA羰基化水平显著上升；醛类修饰导致BSA的α螺旋结构减少、β折叠结构增加，紫外可见吸收光谱显示增色效应，表明蛋白质发生解折叠及分子间交联。【结论】DHA氧化衍生的醛类可通过共价修饰诱导BSA结构紊乱和氧化损伤，该研究为提升多不饱和脂肪酸制剂中蛋白质载体的氧化稳定性提供了理论依据，对于解析富含多不饱和脂肪酸食品在加工贮藏过程中的品质劣变机制具有重要参考价值，并为开发抑制蛋白质氧化、延长食品货架期的策略提供了数据支持。

Abstract:

[Objective] To explore the covalent modification effects of 2-enal and dienal derived from the oxidation of docosahexaenoic acid (DHA) on bovine serum albumin (BSA) and their influences on the protein structure. [Method] The formation of aldehyde-protein adducts was analyzed by ultra-performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS). The level of protein carbonylation was determined by 2,4-dinitrophenylhydrazine (DNPH) colorimetry. The changes in protein secondary structure were analyzed by Fourier transform infrared spectroscopy (FT-IR) and ultraviolet-visible absorption spectroscopy. [Result] The adducts formed by dienal with histidine and lysine residues in BSA were significantly more than those formed by 2-enal. With the increase in aldehyde concentration, the carbonylation level of BSA rose significantly. Aldehyde modification led to reduced α helices and increased β folds of BSA. The ultraviolet-visible absorption spectrum showed a hyperchromic effect, indicating that the protein underwent unfolding and intermolecular cross-linking. [Conclusion] The aldehydes derived from the oxidation of DHA can induce structural disorder and oxidative damage of BSA through covalent modification. This study provides a theoretical basis for improving the oxidative stability of protein carriers in polyunsaturated fatty acid preparations and has important reference value for understanding the quality deterioration mechanism of foods rich in polyunsaturated fatty acids during processing and storage. In addition, it provides data support for the development of strategies to inhibit protein oxidation and extend the shelf life of food.

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王景怡,张志文,吴华,肖俊松. DHA氧化产物对牛血清白蛋白的修饰作用及其对蛋白质结构的影响[J].食品与生物技术学报,2026,45(4):18-27.

WANG Jingyi, ZHANG Zhiwen, WU Hua, XIAO Junsong. Modification of Bovine Serum Albumin by DHA Oxidation Products and Its Impact on Protein Structure[J]. Journal of Food Science and Biotechnology,2026,45(4):18-27.

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收稿日期:2025-09-15
最后修改日期:2025-10-08
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在线发布日期: 2026-08-08
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