Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum

Peptides. 2004 Apr;25(4):621-7. doi: 10.1016/j.peptides.2004.01.015.

Abstract

The fruiting body of Tricholoma giganteum has many pharmaceutical uses and has long been utilized as a home remedy in Asia. This study describes the extraction and characterization of the first angiotensin I-converting enzyme (ACE) inhibitory peptide from T. giganteum. The maximum ACE inhibitory activity (IC50: 0.31 mg) was obtained when the fruiting body of T. giganteum was extracted with distilled water at 30 degrees C for 3 h. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an IC50 of 0.04 mg and a yield of 0.3% was obtained. The ACE inhibitory peptide was a novel tripeptide, showing very low similarity to other ACE inhibitory peptide sequences, and was sequenced as Gly-Glu-Pro. The purified ACE inhibitor from T. giganteum competitively inhibited ACE, and it maintained inhibitory activity even after incubation with proteases. ACE inhibitor from T. giganteum showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR), at a dosage of 1 mg/kg.

MeSH terms

  • Agaricales / chemistry*
  • Agaricales / growth & development
  • Animals
  • Chromatography, Liquid
  • Enzyme Inhibitors / administration & dosage
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / isolation & purification*
  • Fungal Proteins / administration & dosage
  • Fungal Proteins / chemistry*
  • Fungal Proteins / isolation & purification*
  • Hypertension / drug therapy
  • Oligopeptides / administration & dosage
  • Oligopeptides / chemistry*
  • Oligopeptides / isolation & purification*
  • Peptidyl-Dipeptidase A / chemistry*
  • Rabbits
  • Rats
  • Rats, Inbred SHR

Substances

  • Enzyme Inhibitors
  • Fungal Proteins
  • Oligopeptides
  • Peptidyl-Dipeptidase A