College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi 712100, China.
Shaanxi Baiyue Youlishi Dairy Industry Co. Ltd., Xianyang 712000, China.
Int J Biol Macromol. 2024 Oct;277(Pt 3):134232. doi: 10.1016/j.ijbiomac.2024.134232. Epub 2024 Aug 3.
In this study, double enzyme hydrolysis significantly enhanced the DPP-IV inhibition rate compared to single enzyme. The α + K enzymes exhibited the highest inhibition rate. Ultrasonic pretreatment for 30 min improved the hydrolysis efficiency and DPP-IV inhibition rate, potentially due to the structural changes in hydrolysates, such as the increased surface hydrophobicity, and reduced particle size, α-helix and β-turn. Six peptides were screened and verified in vitro. QPY, WPEYL, and YPPQVM displayed competitive inhibition, while LPAAP and IPAPSFPRL displayed mixed competitive/non-competitive inhibition. The interactions between these six peptides and DPP-IV primarily occurred through hydrogen bonds, electrostatic and hydrophobic interactions. Network pharmacological analysis indicated that LPAAP might inhibit DPP-IV activity trough interactions with diabetes-related targets such as CASP3, HSP90AA1, MMP9, and MMP9. These results uncover the potential mechanism of regulating blood glucose by camel milk hydrolysates, establishing camel milk peptide as a source of DPP-IV inhibitory peptide.
在这项研究中，与单一酶相比，双酶水解显著提高了 DPP-IV 抑制率。α+K 酶表现出最高的抑制率。超声预处理 30 分钟提高了水解效率和 DPP-IV 抑制率，这可能是由于水解产物的结构发生了变化，如表面疏水性增加、粒径减小、α-螺旋和β-转角减少。从体外筛选和验证了 6 种肽。QPY、WPEYL 和 YPPQVM 表现出竞争性抑制，而 LPAAP 和 IPAPSFPRL 则表现出混合竞争/非竞争抑制。这 6 种肽与 DPP-IV 之间的相互作用主要通过氢键、静电和疏水相互作用发生。网络药理学分析表明，LPAAP 可能通过与 CASP3、HSP90AA1、MMP9 和 MMP9 等与糖尿病相关的靶标相互作用来抑制 DPP-IV 活性。这些结果揭示了驼乳水解物调节血糖的潜在机制，确立了驼乳肽作为 DPP-IV 抑制肽的来源。
