Liang Qingping, Zhong Yiling, Ren Xinmiao, Liang Ziyu, Zhu Changliang, Wang Linbin, Mou Haijin
College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China.
Section of Neurobiology, Department of Biological Sciences, University of Southern California, Los Angeles, California 90089, United States.
J Agric Food Chem. 2025 Jun 25;73(25):15751-15766. doi: 10.1021/acs.jafc.5c04439. Epub 2025 Jun 11.
Flavor-enhancing characteristics of umami peptides have garnered considerable interest, while their functionality has received limited attention. This study screened umami peptides from sea cucumber viscera hydrolysate and further explored peptides with angiotensin converting enzyme (ACE) inhibitory activity. The amino acid sequences of the prepared hydrolysate were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS), and three umami peptides were mined. These peptides were synthesized for evaluating their ACE inhibitory activity, among which NSPGDSFP exhibited the strongest activity with an IC value of 15.92 ± 0.68 μg/mL. NSPGDSFP demonstrated a noncompetitive action mode and resistance to gastrointestinal environments. Molecular docking revealed that it binds to ACE through hydrogen bonds and hydrophobic interactions. Biolayer interferometry assay further demonstrated that NSPGDSFP binds to ACE with an affinity constant of 2.64 × 10 M. Additionally, NSPGDSFP demonstrated umami-enhancement effect associated with varying levels of salt concentration. The affinity of NSPGDSFP for umami receptor T1R1/T1R3 is primarily contributed by hydrogen bonds. Molecular dynamics (MD) simulation analysis was conducted to further validate the stability of the binding complexes formed between NSPGDSFP and ACE, as well as between NSPGDSFP and the T1R1/T1R3 receptor complex. This study lays the foundation for the future exploration of umami peptide as a food seasoning additive with antihypertension effects.
鲜味肽的风味增强特性已引起广泛关注，但其功能却受到较少关注。本研究从海参内脏水解物中筛选鲜味肽，并进一步探索具有血管紧张素转换酶（ACE）抑制活性的肽。通过液相色谱-串联质谱（LC-MS/MS）鉴定制备的水解物的氨基酸序列，并挖掘出三种鲜味肽。合成这些肽以评估其ACE抑制活性，其中NSPGDSFP表现出最强的活性，IC值为15.92±0.68μg/mL。NSPGDSFP表现出非竞争性作用模式且对胃肠道环境具有抗性。分子对接显示它通过氢键和疏水相互作用与ACE结合。生物层干涉测定法进一步证明NSPGDSFP以2.64×10 M的亲和常数与ACE结合。此外，NSPGDSFP在不同盐浓度水平下表现出鲜味增强效果。NSPGDSFP对鲜味受体T1R1/T1R3的亲和力主要由氢键贡献。进行分子动力学（MD）模拟分析以进一步验证NSPGDSFP与ACE之间以及NSPGDSFP与T1R1/T1R3受体复合物之间形成的结合复合物的稳定性。本研究为未来探索具有降压作用的鲜味肽作为食品调味添加剂奠定了基础。
