4.4 Article

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

Journal

PEPTIDES
Volume 25, Issue 4, Pages 621-627

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2004.01.015

Keywords

Tricholoma giganteum; angiotensin I-converting enzyme inhibitor; anti hypertension

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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 degreesC 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 anti hypertensive effect in spontaneously hypertensive rats (SHR), at a dosage of 1 mg/kg. (C) 2004 Elsevier Inc. All fights reserved.

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