Purification and identification of an ACE inhibitory peptide from walnut protein

Meng Liu; Ming Du; Yingchun Zhang; Weili Xu; Cong Wang; Kejian Wang; Lanwei Zhang

doi:10.1021/jf4001378

Purification and identification of an ACE inhibitory peptide from walnut protein

Meng Liu
, Ming Du^*
, Yingchun Zhang
, Weili Xu
, Cong Wang
, Kejian Wang
, Lanwei Zhang

^*Corresponding author for this work

Harbin Institute of Technology
Northeast Agricultural University
Beijing Academy of Agriculture and Forestry Sciences

Research output: Contribution to journal › Article › peer-review

106 Scopus citations

Abstract

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 IC₅₀ value of 25.67 μg/mL.

Original language	English
Pages (from-to)	4097-4100
Number of pages	4
Journal	Journal of Agricultural and Food Chemistry
Volume	61
Issue number	17
DOIs	https://doi.org/10.1021/jf4001378
State	Published - 1 May 2013

Keywords

ACE-inhibitory activity
characterization
peptide
purification
walnut

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10.1021/jf4001378

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title = "Purification and identification of an ACE inhibitory peptide from walnut protein",

abstract = "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 IC50 value of 25.67 μg/mL.",

keywords = "ACE-inhibitory activity, characterization, peptide, purification, walnut",

author = "Meng Liu and Ming Du and Yingchun Zhang and Weili Xu and Cong Wang and Kejian Wang and Lanwei Zhang",

year = "2013",

month = may,

day = "1",

doi = "10.1021/jf4001378",

language = "英语",

volume = "61",

pages = "4097--4100",

journal = "Journal of Agricultural and Food Chemistry",

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TY - JOUR

T1 - Purification and identification of an ACE inhibitory peptide from walnut protein

AU - Liu, Meng

AU - Du, Ming

AU - Zhang, Yingchun

AU - Xu, Weili

AU - Wang, Cong

AU - Wang, Kejian

AU - Zhang, Lanwei

PY - 2013/5/1

Y1 - 2013/5/1

N2 - 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 IC50 value of 25.67 μg/mL.

AB - 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 IC50 value of 25.67 μg/mL.

KW - ACE-inhibitory activity

KW - characterization

KW - peptide

KW - purification

KW - walnut

UR - https://www.scopus.com/pages/publications/84877015635

U2 - 10.1021/jf4001378

DO - 10.1021/jf4001378

M3 - 文章

C2 - 23566262

AN - SCOPUS:84877015635

SN - 0021-8561

VL - 61

SP - 4097

EP - 4100

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 17

ER -

Purification and identification of an ACE inhibitory peptide from walnut protein

Abstract

Keywords

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