Generation and characterization of dipeptidyl peptidase-IV inhibitory peptides from trypsin-hydrolyzed alpha-lactalbumin-rich whey proteins

文献类型： 外文期刊

第一作者： Jia, Cheng-li

作者： Jia, Cheng-li;Hussain, Naveed;Ujiroghene, Obaroakpo Joy;Pang, Xiao-yang;Zhang, Shu-wen;Lu, Jing;Lv, Jia-ping;Liu, Lu

作者机构：

关键词： Dipeptidyl peptidase-IV (DPP-IV); alpha-Lactalbumin; Response surface methodology; Bioactive peptides; Mode of inhibition

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2020 年 318 卷

页码：

收录情况： SCI

摘要： Dipeptidyl peptidase-IV (DPP-IV) is an enzyme that break down the antidiabetic hormone glucagon-like peptide1. Therefore, inhibition of DPP-IV could be an effective strategy to treat Type 2 diabetes (T2D). The alpha-lactalbumin-rich whey protein concentrate was hydrolyzed by trypsin, and the hydrolysates were then fractionated at a semi-preparative scale using a Superdex Gel filtration Chromatography. The peptides were analyzed by using HPLC coupled with tandem mass spectrometry (RP-HPLC-MS/MS), and their Dipeptidyl peptidase-IV inhibitory activity was determined by the enzymatic assay. Among tested fragments, a potent fragment (LDQWLCEKL), with the half-maximal inhibitory concentration (IC50) of 131 mu M was obtained. Further analysis shows that the LDQWLCEKL peptide corresponds to the amino acid sequence of f(115-123) in alpha-lactalbumin. Furthermore, LDQWLCEKL exhibited a typical non-competitive mode of inhibition. The results indicate that alpha-lactalbumin contains active peptides with DPP-IV inhibitory activity that may be used to prevent and treat T2D.

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