从种子中分离出的三种新型血管紧张素转换酶抑制肽：纯化、抑制动力学及作用机制

Three Novel ACE Inhibitory Peptides Isolated From Seeds: Purification, Inhibitory Kinetic and Mechanism.

作者信息

Ma Fei-Fei, Wang Hao, Wei Chao-Kun, Thakur Kiran, Wei Zhao-Jun, Jiang Li

机构信息

School of Food Science and Engineering, Hefei University of Technology, Hefei, China.

Anhui Habopharmqnceutical Co., Ltd., Taihe, China.

出版信息

Front Pharmacol. 2019 Jan 15;9:1579. doi: 10.3389/fphar.2018.01579. eCollection 2018.

Alcalase, dispase, trypsin, and flavourzyme were used to hydrolyze the extracted seeds protein isolate (GPI). The protein hydrolyzates (GPHs) with the maximum degree of hydrolysis (DH) and ACE inhibitory activity were selected, and ultra-filtered to obtain components with different molecular weights (MW) (<1 kDa, 1-3, 3-5, and 5-10 kDa). The components with MW of <1 kDa showed better ACE inhibition (IC:0.2227 mg/mL). Purification and identification by Sephadex G-15 gel chromatography and LC-MS/MS conferred three new potential ACE inhibitory peptides [TNLDWY (non-competitive suppression mode), IC: 1.932 mM; RADFY (competitive inhibition modes), IC:1.35 mM; RVFDGAV (competitive inhibition modes), IC:1.006 mM]. Molecular docking depicting the inhibitory mechanism for ACE inhibitory peptides indicated that the peptides bound well to ACE and interacted with amino acid residues at the ACE active site.

使用碱性蛋白酶、中性蛋白酶、胰蛋白酶和风味酶对提取的大豆分离蛋白（GPI）进行水解。选择水解度（DH）和ACE抑制活性最高的蛋白水解物（GPHs），并进行超滤以获得不同分子量（MW）（<1 kDa、1 - 3 kDa、3 - 5 kDa和5 - 10 kDa）的组分。分子量<1 kDa的组分表现出更好的ACE抑制作用（IC：0.2227 mg/mL）。通过葡聚糖G - 15凝胶色谱和LC - MS/MS进行纯化和鉴定，得到了三种新的潜在ACE抑制肽[TNLDWY（非竞争性抑制模式），IC：1.932 mM；RADFY（竞争性抑制模式），IC：1.35 mM；RVFDGAV（竞争性抑制模式），IC：1.006 mM]。描述ACE抑制肽抑制机制的分子对接表明，这些肽与ACE结合良好，并与ACE活性位点的氨基酸残基相互作用。