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Purification and Identification of an ACE Inhibitory Peptide from Walnut Protein

文献类型： 外文期刊

作者： Liu, Meng 1 ; Du, Ming 1 ; Zhang, Yingchun 1 ; Xu, Weili 1 ; Wang, Cong 2 ; Wang, Kejian 3 ; Zhang, Lanwei 1 ;

作者机构： 1.Harbin Inst Technol, Sch Food Sci & Technol, Harbin 150090, Peoples R China

2.NE Agr Univ, Coll Food Sci, Harbin 150030, Peoples R China

3.Beijing Acad Agr & Forestry Sci, Inst Forestry & Pomol, Beijing 100093, Peoples R China

关键词： walnut;peptide;ACE-inhibitory activity;purification;characterization

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN：

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收录情况： SCI

摘要： In the present study, a novel angiotensin I-converting enzyme (ACE)-inhibitory peptide, P-2a2, was purified to homogeneity from walnut protein hydrolysate by ultrafiltration, consecutive column chromatography, and high-performance liquid chromatography. The purified peptide was characterized by matrix-assisted laser desorption ionization time-of-flight mass spectrophotometry and a liquid-phase peptide sequencer. The molecular mass of P-2a2 was tested to be 1033.42 D. Its amino acid sequence was determined to be Trp-Pro-Glu-Arg-Pro-Pro-Gln-Ile-Pro. The potent ACE-inhibitory peptide is an enneapeptide and shows a high ACE-inhibitory activity, with an IC_(50) value of 25.67 μg/mL.

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