Digestibility of Glyoxal-Glycated beta-Casein and beta-Lactoglobulin and Distribution of Peptide-Bound Advanced Glycation End Products in Gastrointestinal Digests
Digestibility of Glyoxal-Glycated beta-Casein and beta-Lactoglobulin and Distribution of Peptide-Bound Advanced Glycation End Products in Gastrointestinal Digests
复制标题
乙二醛-糖化 β-酪蛋白和 β-乳球蛋白的消化率以及肽结合的高级糖化终产物在胃肠道消化物中的分布
DOI：
10.1021/acs.jafc.7b01951
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发表时间：
2017
影响因子：
6.1
通讯作者：
Li Bing
中科院分区：
文献类型：
--
作者：
Zhao Di;Li Lin;Le Thao T.;Larsen Lotte Bach;Su Guoying;Liang Yi;Li Bing
本研究报道了乙二醛（GO）衍生的糖基化对胃肠道酶解β-乳球蛋白和β-酪蛋白的影响。胃期和肠期糖基化蛋白的消化率均降低。随后研究了美拉德反应产物在不同分子量的消化物中的分布。在小于20kda的消化酶中，主要出现无色和棕色的MRPs。然而，在糖基化过程中，荧光晚期糖基化终产物（AGEs）对酶解的抗性逐渐增强，使得荧光AGEs主要存在于大于20 kDa的酶解中。未检测到游离的N (ε)-羧甲基赖氨酸（CML）。在大于1 kDa的酶解中，CML的相对含量高于赖氨酸，表明CML对酶解有阻碍作用。本研究强调了氧化石墨烯衍生的AGEs对消化蛋白酶的抗性，通过阻断胰蛋白酶裂解位点或位阻，这是饮食中AGEs吸收的障碍。
This work reports the influence of glyoxal (GO)-derived glycation on the gastrointestinal enzymatic hydrolysis of β-lactoglobulin and β-casein. Reduced digestibility of glycated proteins was found in both gastric and intestinal stage. Distribution of Maillard reaction products in digests with different molecular weight ranges was investigated subsequently. The colorless and brown MRPs largely presented in the digests smaller than 20 kDa. However, the resistance of fluorescent advanced glycation end products (AGEs) to enzymatic hydrolysis gradually increased during glycation, rendering fluorescent AGEs largely present in the digests larger than 20 kDa. No free N (ε)-carboxymethyllysine (CML) was detected in digests. The relative amount of CML in digests larger than 1 kDa was higher than that of Lys, demonstrating the hindrance of CML to enzymatic hydrolysis. This study highlights the resistance of GO-derived AGEs to digestive proteases via blockage of tryptic cleavage sites or steric hindrance, which is a barrier to the absorption of dietary AGEs.