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骆驼乳蛋白水解物中新型二肽基肽酶 IV(DPP-IV)抑制肽的鉴定。

Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel milk protein hydrolysates.

机构信息

Department of Biological Sciences, University of Limerick, Limerick, Ireland; Food for Health Ireland (FHI), University of Limerick, Limerick, Ireland.

Department of Food Science, College of Food and Agriculture, United Arab Emirates University, Al Ain 15551, United Arab Emirates.

出版信息

Food Chem. 2018 Apr 1;244:340-348. doi: 10.1016/j.foodchem.2017.10.033. Epub 2017 Oct 10.

DOI:10.1016/j.foodchem.2017.10.033
PMID:29120791
Abstract

Nine novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (FLQY, FQLGASPY, ILDKEGIDY, ILELA, LLQLEAIR, LPVP, LQALHQGQIV, MPVQA and SPVVPF) were identified in camel milk proteins hydrolysed with trypsin. This was achieved using a sequential approach combining liquid chromatography tandem mass spectrometry (LC-MS/MS), qualitative/quantitative structure activity relationship (QSAR) and confirmatory studies with synthetic peptides. The most potent camel milk protein-derived DPP-IV inhibitory peptides, LPVP and MPVQA, had DPP-IV half maximal inhibitory concentrations (IC) of 87.0 ± 3.2 and 93.3 ± 8.0 µM, respectively. DPP-IV inhibitory peptide sequences identified within camel and bovine milk protein hydrolysates generated under the same hydrolysis conditions differ. This was linked to differences in enzyme selectivity for peptide bond cleavage of camel and bovine milk proteins as well as dissimilarities in their amino acid sequences. Camel milk proteins contain novel DPP-IV inhibitory peptides which may play a role in the regulation of glycaemia in humans.

摘要

九种新型二肽基肽酶 IV(DPP-IV)抑制肽(FLQY、FQLGASPY、ILDKEGIDY、ILELA、LLQLEAIR、LPVP、LQALHQGQIV、MPVQA 和 SPVVPF)在经胰蛋白酶水解的骆驼乳蛋白中被鉴定出来。这是通过结合液相色谱串联质谱(LC-MS/MS)、定性/定量构效关系(QSAR)和合成肽的验证研究的顺序方法实现的。最有效的骆驼乳蛋白衍生的 DPP-IV 抑制肽 LPVP 和 MPVQA 的 DPP-IV 半最大抑制浓度(IC)分别为 87.0±3.2 和 93.3±8.0µM。在相同水解条件下生成的骆驼乳和牛乳蛋白水解物中鉴定出的 DPP-IV 抑制肽序列不同。这与骆驼和牛乳蛋白的酶对肽键裂解的选择性差异以及它们的氨基酸序列的差异有关。骆驼乳蛋白含有新型的 DPP-IV 抑制肽,可能在调节人体血糖方面发挥作用。

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