Purification and molecular docking study of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide from alcalase hydrolysate of ultrasonic-pretreated silkworm pupa (Bombyx mori) protein

被引：84
作者：
Jia, Junqiang [1 ,2 ]
Wu, Qiongying [1 ,2 ]
Yan, Hui [1 ,2 ]
Gui, Zhongzheng [1 ,2 ]
机构：
[1] Jiangsu Univ Sci & Technol, Sch Biotechnol, Zhenjiang 212018, Jiangsu, Peoples R China
[2] Chinese Acad Agr Sci, Sericultural Res Inst, Zhenjiang 212018, Jiangsu, Peoples R China
来源：
PROCESS BIOCHEMISTRY | 2015年 / 50卷 / 05期
基金：
中国国家自然科学基金;
关键词：
Silkworm pupa (Bombyx mori); Ultrasonic pretreatment; ACE inhibitory peptide; Purification; Molecular docking; SPONTANEOUSLY HYPERTENSIVE-RATS; ANTIHYPERTENSIVE ACTIVITY; IDENTIFICATION; MILK; OPTIMIZATION; MECHANISM; VITRO;
D O I：
10.1016/j.procbio.2014.12.030
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Silkworm pupa (Bombyx mori) protein (SPP) was treated by ultrasound, and then was hydrolyzed using alcalase. The hydrolysate with the highest ACE inhibitory activity was obtained at hydrolysis of 50 min when SPP was treated at power of 410W/100 ml for 32 min. The hydrolysate was fractionated by ultrafiltration, and peptide with the highest ACE inhibitory activity was purified from <5 kDa fraction using gel filtration and RP-HPLC. A novel peptide was identified as Lys-His-Val (IC50 = 12.82 mu M), and it was stable against the gastrointestinal proteases. The molecular docking study revealed that ACE inhibitory activity of the tripeptide was mainly attributed to the hydrogen bond interactions and Zn(II) interaction between the tripeptide and ACE. These results suggest that the tripeptide is a potential natural ACE inhibitor that can be used as drug or functional food ingredient. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码：876 / 883
页数：8
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