Purification and characterization of a novel angiotensin I-converting enzyme-inhibitory peptide derived from Alaska pollack skins

doi:10.1111/1750-3841.15754

CORC > 烟台海岸带研究所 > 中国科学院烟台海岸带研究所 > 海岸带生物学与生物资源利用重点实验室

	Purification and characterization of a novel angiotensin I-converting enzyme-inhibitory peptide derived from Alaska pollack skins
	Yang, Guilan 2,3; Qin, Song 1,2; Li, Wenjun 1,2
刊名	JOURNAL OF FOOD SCIENCE
	2021-05-30
页码	11
关键词	Alaska pollack skins protein hydrolysate angiotensin I-converting enzyme (ACE)-inhibitory peptide gel filtration chromatography molecular docking ultrafiltration
ISSN号	0022-1147
DOI	10.1111/1750-3841.15754
通讯作者	Li, Wenjun(wjli@yic.ac.cn)
英文摘要	Hydrolysates containing angiotensin I-converting enzyme (ACE)-inhibitory peptide were prepared from protein of Alaska pollack skins using alcalase and trypsin. The protein hydrolysate was separated by ultrafiltration, Sephadex G-25 gel filtration chromatography and reversed phase high-performance liquid chromatography (HPLC), from which a novel purified peptide was obtained. Both random coil structure and beta-sheet in the purified peptide were revealed in Fourier transform infrared spectrum. The amino sequence of the purified peptide was identified as GPLGVP, VLYPVK, VFLENVLR, and FEEF by HPLC-Q-TOF-MS (HPLC-quadrupole time-of-flight mass spectrometry). The peptide GPLGVP whose molecular weight was 538.31 Da showed the highest ACE inhibitory activity (IC50 = 105.8 mu M). The purified peptide featured a noncompetitive inhibition kinetic mechanism was shown in the Lineweaver-Burk plots and was susceptible to enzymes as indicated in the studies on stability of gastrointestinal proteases. Moreover, the peptide GPLGVP can combine ACE catalytic pocket through hydrogen bonds and other forces with high binding power as disclosed in molecular docking simulation, which provides the inhibitory effect of GPLGVP on ACE.
资助项目	National Key Research and Development Program of China[2018YFD0901102] ; Marine Economy Innovation Development Demonstration Project[YHCX-SW-L-201705]
WOS关键词	PROTEIN HYDROLYSATE ; ACE ; STABILITY ; KINETICS ; MUSCLE ; VENOM
WOS研究方向	Food Science & Technology
语种	英语
WOS记录号	WOS:000656102700001
资助机构	National Key Research and Development Program of China ; Marine Economy Innovation Development Demonstration Project
内容类型	期刊论文
源URL	[http://ir.yic.ac.cn/handle/133337/29297]
专题	海岸带生物学与生物资源利用重点实验室烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室中国科学院烟台海岸带研究所
通讯作者	Li, Wenjun
作者单位	1.Chinese Acad Sci, Ctr Ocean Mega Sci, Qingdao, Peoples R China 2.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China 3.Binzhou Med Univ, Sch Pharm, Yantai, Peoples R China
推荐引用方式 GB/T 7714	Yang, Guilan,Qin, Song,Li, Wenjun. Purification and characterization of a novel angiotensin I-converting enzyme-inhibitory peptide derived from Alaska pollack skins[J]. JOURNAL OF FOOD SCIENCE,2021:11.
APA	Yang, Guilan,Qin, Song,&Li, Wenjun.(2021).Purification and characterization of a novel angiotensin I-converting enzyme-inhibitory peptide derived from Alaska pollack skins.JOURNAL OF FOOD SCIENCE,11.
MLA	Yang, Guilan,et al."Purification and characterization of a novel angiotensin I-converting enzyme-inhibitory peptide derived from Alaska pollack skins".JOURNAL OF FOOD SCIENCE (2021):11.