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.
authors.forename: Meng
authors.initials: M
authors.lastname: Liu
authors.forename: Ming
authors.initials: M
authors.lastname: Du
authors.forename: Yingchun
authors.initials: Y
authors.lastname: Zhang
authors.forename: Weili
authors.initials: W
authors.lastname: Xu
authors.forename: Cong
authors.initials: C
authors.lastname: Wang
authors.forename: Kejian
authors.initials: K
authors.lastname: Wang
authors.forename: Lanwei
authors.initials: L
authors.lastname: Zhang
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D031324:Juglans / Q000737:chemistry*; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D011492:Protein Hydrolysates / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D010940:Plant Proteins; D011492:Protein Hydrolysates; D007703:Peptidyl-Dipeptidase A