Purification and identification of an ACE inhibitory peptide from walnut protein

J Agric Food Chem. 2013 May 1;61(17):4097-100. doi: 10.1021/jf4001378. Epub 2013 Apr 19.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry
  • Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
  • Chromatography, High Pressure Liquid
  • Juglans / chemistry*
  • Molecular Weight
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Peptidyl-Dipeptidase A / metabolism
  • Plant Proteins / chemistry
  • Plant Proteins / isolation & purification*
  • Protein Hydrolysates / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Peptides
  • Plant Proteins
  • Protein Hydrolysates
  • Peptidyl-Dipeptidase A