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甲基乙二醛对模拟热加工条件下α-乳白蛋白结构和消化率变化以及晚期糖基化终产物形成的影响。

Effect of methylglyoxal on the alteration in structure and digestibility of α-lactalbumin, and the formation of advanced glycation end products under simulated thermal processing.

作者信息

Wu Yuekun, Dong Lu, Wu Yajing, Wu Dongyan, Zhang Yan, Wang Shuo

机构信息

Tianjin Key Laboratory of Food Science and Health School of Medicine Nankai University Tianjin China.

State Key Laboratory of Food Nutrition and Safety Tianjin University of Science and Technology Tianjin China.

出版信息

Food Sci Nutr. 2021 Feb 28;9(4):2299-2307. doi: 10.1002/fsn3.2211. eCollection 2021 Apr.

Abstract

α-Dicarbonyl compounds (α-DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α-DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α-DCs, was selected to investigate the alteration effects on the structure and digestibility of α-lactalbumin (αLA) under thermal processing (60-100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High-resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and N-(carboxyethyl)-L-lysine is the main modification type. Since the Lys and Arg are also the cleavage sites of trypsin, the digestibility of MG modified αLA (MG-αLA) by trypsin correspondingly decreased with an increase of processing temperature. The reacted Lys and Arg residues, and the protein-bound AGEs were quantified, and the contents were found to be highly dependent on the temperature.

摘要

α-二羰基化合物(α-DCs)是一类在食品热加工过程中产生的化合物。由于其高反应活性,α-DCs能够与食品成分发生反应,从而降低营养价值,甚至带来食品安全隐患。在本研究中,选择了含量最高的α-DCs——甲基乙二醛(MG),来研究其在热加工(60-100°C)条件下对α-乳白蛋白(αLA)结构和消化率的改变作用。结果表明,MG对αLA的修饰程度随加工温度的升高而增加,同时伴随着αLA分子量、内源荧光和二级结构的显著变化。高分辨率质谱分析确定赖氨酸(Lys)和精氨酸(Arg)为修饰位点,N-(羧乙基)-L-赖氨酸为主要修饰类型。由于Lys和Arg也是胰蛋白酶的切割位点,MG修饰的αLA(MG-αLA)被胰蛋白酶的消化率随加工温度的升高而相应降低。对反应后的Lys和Arg残基以及与蛋白质结合的晚期糖基化终产物进行了定量分析,发现其含量高度依赖于温度。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcdc/8020911/4def17b7e4c5/FSN3-9-2299-g004.jpg

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