Separation and identification of ACE inhibitory peptides from defatted walnut meal

被引：23

作者：

Chen, Yonghao ^{[1
]}

Li, Jun ^{[2
]}

Dong, Ningguang ^{[1
]}

Zhang, Yunqi ^{[1
]}

Lu, Xiaodan ^{[1
]}

Hao, Yanbin ^{[1
]}

Qi, Jianxun ^{[1
]}

机构：

[1] Beijing Acad Forestry & Pomol Sci, Jia 12 Xiangshan Ruiwangfen, Beijing 100093, Peoples R China

[2] Beijing Inst Landscape Architecture, Beijing Key Lab Greening Plants Breeding, Jia 7 Huajiadi, Beijing 100102, Peoples R China

来源：

EUROPEAN FOOD RESEARCH AND TECHNOLOGY | 2020年 / 246卷 / 10期

关键词：

Walnut peptide; ACE inhibitory activity; Purification; Identification; Amino acid sequence; ANGIOTENSIN-CONVERTING ENZYME; SPECTROPHOTOMETRIC ASSAY; PURIFICATION; PROTEIN; MILK; FRAGMENT;

D O I：

10.1007/s00217-020-03553-5

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The peptide obtained from walnut protein enzymatic hydrolysate had high ACE inhibitory activity. Through centrifugation, ultrafiltration, gel chromatography and high performance liquid chromatography (HPLC), the walnut oligo-peptide, which was denoted as P4-c with high ACE inhibitory activity was obtained. Three novel ACE inhibitory peptides, GVVPHN, EHSLDPLK and KTLLNFGPN, were identified from P4-c by high-resolution ion mobility mass spectrometry (IM-MS). The three novel ACE inhibitory peptides possessed good ACE inhibitory activity and the fraction GVVPHN had high ACE inhibitory activity with 27.3 mu mol L(-1)of IC50. The molar percentage of hydrophobic amino acids in the peptide GVVPHN was 50% while the hydrophobic amino acid contents of EHSLDPLK and KTLLNFGPN were 37.5% and 44.4%, respectively, which indicates ACE inhibitory activities were hydrophobicity of amino acid-dependent.

引用

页码：2029 / 2038

页数：10

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