文献类型：期刊文献

英文题名：In vitro and in vivo ACE inhibitory of pistachio hydrolysates and in silico mechanism of identified peptide binding with ACE

作者：Li, Peng[1];Jia, Jia[2];Fang, Ming[1];Zhang, Lujia[1];Guo, Mingrong[1];Xie, Jingli[1];Xia, Yuelan[1];Zhou, Li[1];Wei, Dongzhi[1]

机构：[1]E China Univ Sci & Technol, Dept Food Sci & Engn, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Shandong Silk Text Vocat Coll, Zibo 255300, Shandong, Peoples R China

年份：2014

卷号：49

期号：5

起止页码：898

外文期刊名：PROCESS BIOCHEMISTRY

收录：;EI(收录号：20141617589965);WOS:【SCI-EXPANDED(收录号:WOS:000336111700024)】；

基金：This work was supported by "National Natural Science Foundation of China (No. 31301413)", "National Major Science and Technology Projects of China (No. 2012ZX09304009)", "the Fundamental Research Funds for the Central Universities", P. R. China. The authors are highly thankful to Paramount Farms Ltd. Co. (San QiaoKun valley, CA, USA) for providing the pistachio nuts.

语种：英文

外文关键词：ACE inhibitory peptide; Molecular docking; Pistacia vera L.; Purification; Spontaneously hypertensive rats (SHRs)

摘要：The ACE inhibitory activity of pistachio (Pistacia vera L.) kernel's hydrolysates by gastrointestinal enzymes was studied. Results indicated that hydrolysate successively hydrolyzed by pepsin and trypsin, Pe-Tr-H, presented in vitro ACE inhibitory activity as IC50 0.87 +/- 0.04 mg/ml. The Pe-Tr-H can in vivo decrease around 22 mmHg in systolic blood pressure (SBP) and 16 mmHg in the diastolic blood pressure (DBP) at 4h after the oral administration, however the pistachio kernel powder can slightly lower SBP and DBP. The Pe-Tr-H with the highest activity was then separated by ultrafiltration membrane of 3 kDa, size exclusion chromatography on Sephadex G-15 and G-10 columns and reversed phase high-performance liquid chromatography (RP-HPLC) consecutively. A novel ACE inhibitory peptide, ACKEP, with the IC50 value of 126 mu M, was identified by MALDI-TOF/TOF system. ACKEP has the same C-terminal residue as Lisinopril and Enalapril, which plays a key role in binding with ACE. The binding mechanism was explored at a molecular basis by docking experiments, which revealed that seven residues from ACE active site (His383, His387, Glu384, Arg522, Asp358, Ala356 and Asn70) and two atoms of ACKEP (O5, H60) greatly contributed to the combinative stabilization. (C) 2014 Elsevier Ltd. All rights reserved.