Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells.
Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells.
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DOI：
10.3390/nu14030686
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发表时间：
2022-02-06
期刊：
影响因子：
5.9
通讯作者：
Shi J
中科院分区：
文献类型：
--
作者：
Chen N;Wang L;Zhang Q;Zhao XH;Shi J
本研究通过转谷氨酰胺酶(TGase)催化壳寡糖糖化牛奶蛋白酪蛋白，然后用胰酶对酪蛋白进行酶解。以脂多糖(LPS)刺激的大鼠肠上皮细胞(IEC-6)为细胞模型，未经TGase催化的酪蛋白水解物(CNH)为对照，对所得糖化酪蛋白水解物(GCNH)的抗炎活性进行了评价。结果表明，GCNH含有壳寡糖，氨基葡萄糖含量为5.74g/kg蛋白质。总体而言，25~100μg/mLGCNH能促进IEC-6细胞生长，25~50μg/mLGCNH还能有效地提高细胞存活率，减轻内毒素诱导的细胞毒作用。尽管内毒素能引起明显的炎症反应，但GCNH能减少IL-1β(IL-1β)、IL-6和肿瘤坏死因子-α三种促炎介质的分泌，或促进IL-10和转化生长因子-β两种抗炎介质的分泌，显示其对刺激细胞的抗炎活性。此外，GCNH还可下调TLR4、p-p38和p-p65三种炎症相关蛋白在刺激细胞中的表达，从而抑制p38和p65蛋白的磷酸化，并使NF-κB和MAPK信号通路失活。此外，更高的GCNH剂量水平始终导致更高的细胞抗炎作用，而在执行抗炎功能靶点方面，GCNH总是比CNH更有效。因此，TGase催化的酪蛋白壳寡糖糖基化反应可以有效地增强酪蛋白水解物的抗炎活性。因此，TGase催化的蛋白质糖基化可能会增强蛋白质成分在体内的保健功能。
In this study, milk protein casein was glycated by oligochitosan through the catalysis of transglutaminase (TGase) and then hydrolyzed by trypsin. The obtained glycated casein hydrolysates (GCNH) were assessed for their anti-inflammatory activities, using the lipopolysaccharide (LPS)-stimulated rat intestinal epithelial cells (IEC-6) as cell models and the casein hydrolysates (CNH) without TGase catalysis as controls. The results showed that GCNH had oligochitosan incorporation and thus possessed a glucosamine content of 5.74 g/kg protein. In general, GCNH at dose levels of 25–100 μg/mL could elevate IEC-6 cell growth, and at dose levels of 25–50 μg/mL, they were also able to alleviate the LPS-induced cytotoxicity by increasing cell viability efficiently. Although LPS caused clear inflammation in the LPS-stimulated cells, GCNH were capable of reducing the secretion of three pro-inflammatory mediators including interleukin-1β (IL-1β), IL-6, and tumor necrosis factor-α, or promoting the secretion of two anti-inflammatory mediators like IL-10 and transforming growth factor-β, demonstrating their anti-inflammatory activities to the stimulated cells. Moreover, GCNH also could down-regulate the expression of three inflammation-related proteins including TLR4, p-p38, and p-p65 in the stimulated cells, and thus possessed a capacity to suppress the phosphorylation of p38 and p65 proteins as well as to inactivate the NF-κB and MAPK signaling pathways. Additionally, a higher GCNH dose level consistently led to higher anti-inflammatory effect in the cells, while GCNH were always more potent than CNH at performing anti-inflammatory function targets. It is thus suggested that the TGase-catalyzed casein oligochitosan-glycation could enhance the anti-inflammatory activities of casein hydrolysates efficiently. TGase-catalyzed protein glycation thus might enhance the healthcare function of protein ingredients in the body.
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